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Vladimir N Uversky, Ph.D., D.Sc. - Publications

Affiliations: 
1986-1998 Laboratory of Protein Physics Institute of Protein Research, Russian Academy of Sciences 
 1998- Laboratory of New Methods in Biology Institute for Biological Instrumentation, Russian Academy of Sciences 
 1998-2004 Chemistry and Biochemistry University of California, Santa Cruz, Santa Cruz, CA, United States 
 2004-2010 Center for Computational Biology and Bioinformatics Indiana University - Purdue University in Indianapolis Medical School 
 2010- Molecular Medicine University of South Florida, Tampa, FL, United States 
Area:
protein physics
Website:
https://health.usf.edu/medicine/molecularmedicine/faculty/2838234/Uversky
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Year Citation  Score
2020 Zhao B, Katuwawala A, Uversky VN, Kurgan L. IDPology of the living cell: intrinsic disorder in the subcellular compartments of the human cell. Cellular and Molecular Life Sciences : Cmls. PMID 32997198 DOI: 10.1007/s00018-020-03654-0  0.346
2020 Van Bibber NW, Haerle C, Khalife R, Dayhoff GW, Uversky VN. Intrinsic Disorder in Human Proteins Encoded by Core Duplicon Gene Families. The Journal of Physical Chemistry. B. 124: 8050-8070. PMID 32880174 DOI: 10.1021/Acs.Jpcb.0C07676  0.435
2020 Mendes LFS, Fontana NA, Reddy ST, Uversky VN, Costa-Filho AJ. The exquisite structural biophysics of the Golgi reassembly and stacking proteins. International Journal of Biological Macromolecules. PMID 32871120 DOI: 10.1016/J.Ijbiomac.2020.08.203  0.446
2020 Elrashdy F, Redwan EM, Uversky VN. Intrinsic disorder perspective of an interplay between the renin-angiotensin-aldosterone system and SARS-CoV-2. Infection, Genetics and Evolution. 85: 104510. PMID 32853823 DOI: 10.1016/J.Meegid.2020.104510  0.388
2020 Bhopatkar AA, Uversky VN, Rangachari V. Disorder and cysteines in proteins: A design for orchestration of conformational see-saw and modulatory functions. Progress in Molecular Biology and Translational Science. 174: 331-373. PMID 32828470 DOI: 10.1016/Bs.Pmbts.2020.06.001  0.478
2020 Nagibina GS, Melnik TN, Glukhova KA, Uversky VN, Melnik BS. Intrinsic disorder-based design of stable globular proteins. Progress in Molecular Biology and Translational Science. 174: 157-186. PMID 32828465 DOI: 10.1016/bs.pmbts.2020.05.005  0.324
2020 Mishra PM, Verma NC, Rao C, Uversky VN, Nandi CK. Intrinsically disordered proteins of viruses: Involvement in the mechanism of cell regulation and pathogenesis. Progress in Molecular Biology and Translational Science. 174: 1-78. PMID 32828463 DOI: 10.1016/Bs.Pmbts.2020.03.001  0.44
2020 Weisz J, Uversky VN. Zooming into the Dark Side of Human Annexin-S100 Complexes: Dynamic Alliance of Flexible Partners. International Journal of Molecular Sciences. 21. PMID 32824294 DOI: 10.3390/Ijms21165879  0.461
2020 Reddy ST, Uversky VN, Costa-Filho AJ. Biophysical characterization of intrinsically disordered human Golgi matrix protein GRASP65. International Journal of Biological Macromolecules. PMID 32822731 DOI: 10.1016/J.Ijbiomac.2020.08.126  0.463
2020 Kostetsky EY, Uversky VN. On the origin of matrix mechanism in protocells and key problems of molecular biology. Journal of Biomolecular Structure & Dynamics. 1-12. PMID 32820704 DOI: 10.1080/07391102.2020.1809523  0.331
2020 Goh GK, Dunker AK, Foster JA, Uversky VN. Shell disorder analysis suggests that pangolins offered a window for a silent spread of an attenuated SARS-CoV-2 precursor among humans. Journal of Proteome Research. PMID 32790362 DOI: 10.1021/Acs.Jproteome.0C00460  0.342
2020 Majorina MA, Balobanov VA, Uversky VN, Melnik BS. Loops linking secondary structure elements affect the stability of the molten globule intermediate state of apomyoglobin. Febs Letters. PMID 32770670 DOI: 10.1002/1873-3468.13905  0.36
2020 Webster JM, Darling AL, Sanders TA, Blazier DM, Vidal-Aguiar Y, Beaulieu-Abdelahad D, Plemmons DG, Hill SE, Uversky VN, Bickford PC, Dickey CA, Blair LJ. Hsp22 with an N-Terminal Domain Truncation Mediates a Reduction in Tau Protein Levels. International Journal of Molecular Sciences. 21. PMID 32751642 DOI: 10.3390/Ijms21155442  0.769
2020 Na I, Choi S, Son SH, Uversky VN, Kim CG. Drug Discovery Targeting the Disorder-To-Order Transition Regions through the Conformational Diversity Mimicking and Statistical Analysis. International Journal of Molecular Sciences. 21. PMID 32722024 DOI: 10.3390/Ijms21155248  0.801
2020 Giri R, Bhardwaj T, Shegane M, Gehi BR, Kumar P, Gadhave K, Oldfield CJ, Uversky VN. Understanding COVID-19 via comparative analysis of dark proteomes of SARS-CoV-2, human SARS and bat SARS-like coronaviruses. Cellular and Molecular Life Sciences. 78: 1655-1688. PMID 32712910 DOI: 10.1007/S00018-020-03603-X  0.456
2020 Uversky VN. Analyzing IDPs in Interactomes. Methods of Molecular Biology. 2141: 895-945. PMID 32696395 DOI: 10.1007/978-1-0716-0524-0_46  0.477
2020 da Silva NR, Ferreira LA, Madeira PP, Teixeira JA, Uversky VN, Zaslavsky BY. Linear Relationships between Partition Coefficients of Different Organic Compounds and Proteins in Aqueous Two-Phase Systems of Various Polymer and Ionic Compositions. Polymers. 12. PMID 32610437 DOI: 10.3390/Polym12071452  0.33
2020 Dayhoff GW, van Regenmortel MHV, Uversky VN. Intrinsic disorder in protein sense-antisense recognition. Journal of Molecular Recognition : Jmr. 33: e2868. PMID 32573020 DOI: 10.1002/Jmr.2868  0.403
2020 Bhardwaj T, Saumya KU, Kumar P, Sharma N, Gadhave K, Uversky VN, Giri R. Japanese Encephalitis Virus: Exploring the dark proteome and disorder-function paradigm. The Febs Journal. PMID 32473054 DOI: 10.1111/Febs.15427  0.465
2020 Van Bibber NW, Haerle C, Khalife R, Xue B, Uversky VN. Intrinsic Disorder in Tetratricopeptide Repeat Proteins. International Journal of Molecular Sciences. 21. PMID 32466138 DOI: 10.3390/Ijms21103709  0.502
2020 Gadhave K, Kumar P, Kapuganti SK, Uversky VN, Giri R. Unstructured Biology of Proteins from Ubiquitin-Proteasome System: Roles in Cancer and Neurodegenerative Diseases. Biomolecules. 10. PMID 32455657 DOI: 10.3390/biom10050796  0.377
2020 Khanppnavar B, Roy A, Chandra K, Uversky VN, Maiti NC, Datta S. Deciphering the structural intricacy in virulence effectors for proton-motive force mediated unfolding in type-III protein secretion. International Journal of Biological Macromolecules. 159: 18-33. PMID 32437799 DOI: 10.1016/J.Ijbiomac.2020.04.266  0.428
2020 Lee YJ, Son SH, Lim CS, Kim MY, Lee SW, Lee S, Jeon J, Ha DH, Jung NR, Han SY, Do BR, Na I, Uversky VN, Kim CG. MMTR/Dmap1 Sets the Stage for Early Lineage Commitment of Embryonic Stem Cells by Crosstalk with PcG Proteins. Cells. 9. PMID 32403252 DOI: 10.3390/Cells9051190  0.76
2020 Lapteva YS, Vologzhannikova AA, Sokolov AS, Ismailov RG, Uversky VN, Permyakov SE. In Vitro N-Terminal Acetylation of Bacterially Expressed Parvalbumins by N-Terminal Acetyltransferases from Escherichia coli. Applied Biochemistry and Biotechnology. PMID 32394317 DOI: 10.1007/S12010-020-03324-8  0.368
2020 Badierah RA, Uversky VN, Redwan EM. Dancing with Trojan horses: an interplay between the extracellular vesicles and viruses. Journal of Biomolecular Structure & Dynamics. 1-27. PMID 32351170 DOI: 10.1080/07391102.2020.1756409  0.301
2020 Camponeschi I, Damasco A, Uversky VN, Giuliani A, Bianchi MM. Phenotypic suppression caused by resonance with light-dark cycles indicates the presence of a 24-hours oscillator in yeast and suggests a new role of intrinsically disordered protein regions as internal mediators. Journal of Biomolecular Structure & Dynamics. 1-12. PMID 32223547 DOI: 10.1080/07391102.2020.1749133  0.385
2020 Kumar A, Kumar P, Kumari S, Uversky VN, Giri R. Folding and structural polymorphism of p53 C-terminal domain: One peptide with many conformations. Archives of Biochemistry and Biophysics. 108342. PMID 32184088 DOI: 10.1016/J.Abb.2020.108342  0.411
2020 Permyakov SE, Yundina EN, Kazakov AS, Permyakova ME, Uversky VN, Permyakov EA. Mouse S100G protein exhibits properties characteristic of a calcium sensor. Cell Calcium. 87: 102185. PMID 32114281 DOI: 10.1016/J.Ceca.2020.102185  0.358
2020 Uversky VN. New technologies to analyse protein function: an intrinsic disorder perspective. F1000research. 9. PMID 32089835 DOI: 10.12688/F1000Research.20867.1  0.467
2020 Dey A, Sen S, Uversky VN, Maulik U. Structural Facets of POU2F1 in Light of the Functional Annotations and Sequence-Structure Patterns. Journal of Biomolecular Structure & Dynamics. 1-16. PMID 32081083 DOI: 10.1080/07391102.2020.1733092  0.375
2020 Kian-Meng Goh G, Dunker AK, Foster JA, Uversky VN. Nipah shell disorder, modes of infection, and virulence. Microbial Pathogenesis. 103976. PMID 31940461 DOI: 10.1016/J.Micpath.2020.103976  0.341
2020 Reddy ST, Uversky VN, Costa-Filho AJ. Nucleation-dependent amyloid fibrillation of human GRASP55 in aqueous solution. European Biophysics Journal : Ebj. PMID 31915857 DOI: 10.1007/S00249-019-01419-7  0.36
2020 Matos CO, Passos YM, Amaral MJd, Macedo B, Tempone MH, Bezerra OCL, Moraes MO, Almeida MS, Weber G, Missailidis S, Silva JL, Uversky VN, Pinheiro AS, Cordeiro Y. Liquid‐liquid phase separation and fibrillation of the prion protein modulated by a high‐affinity DNA aptamer The Faseb Journal. 34: 365-385. PMID 31914616 DOI: 10.1096/Fj.201901897R  0.342
2020 Bhopatkar AA, Uversky VN, Rangachari V. Granulins modulate liquid-liquid phase separation and aggregation of the prion-like C-terminal domain of the neurodegeneration-associated protein TDP-43. The Journal of Biological Chemistry. 295: 2506-2519. PMID 31911437 DOI: 10.1074/Jbc.Ra119.011501  0.369
2020 Mandaci SY, Caliskan M, Sariaslan MF, Uversky VN, Coskuner-Weber O. Epitope Region Identification Challenges of Intrinsically Disordered Proteins in Neurodegenerative Diseases: Secondary Structure Dependence of α-Synuclein on Simulation Techniques and Force Field Parameters. Chemical Biology & Drug Design. PMID 31903719 DOI: 10.1111/Cbdd.13662  0.401
2020 Gadhave K, Gehi BR, Kumar P, Xue B, Uversky VN, Giri R. The dark side of Alzheimer's disease: unstructured biology of proteins from the amyloid cascade signaling pathway. Cellular and Molecular Life Sciences : Cmls. PMID 31894361 DOI: 10.1007/S00018-019-03414-9  0.453
2020 Uversky VN. Torches, Candles, Lamps, Lanterns, Flashlights, Spotlights, Night Vision Goggles… You Need Them All to See in Darkness. Proteomics. 19: e1900085. PMID 30829430 DOI: 10.1002/Pmic.201900085  0.38
2020 Almehdar HA, El-Baky NA, Alhaider AA, Almuhaideb SA, Alhaider AA, Albiheyri RS, Uversky VN, Redwan EM. Bacteriostatic and Bactericidal Activities of Camel Lactoferrins Against Salmonella enterica Serovar Typhi. Probiotics and Antimicrobial Proteins. 12: 18-31. PMID 30723884 DOI: 10.1007/S12602-019-9520-5  0.304
2020 Uversky VN. Functions of short lifetime biological structures at large: the case of intrinsically disordered proteins. Briefings in Functional Genomics. 19: 60-68. PMID 29982297 DOI: 10.1093/Bfgp/Ely023  0.502
2020 Polanco C, Uversky VN, Huberman A, Andrés L, Buhse T, Castañón-González J, Sánchez-Guerrero A. Bioinformatics-based identification of proteins expressed by arthropod-borne viruses transmitted by Aedes aegypti mosquito Current Proteomics. 17. DOI: 10.2174/1570164617999200422123618  0.337
2020 Zakariya SM, Furkan M, Zaman M, Chandel TI, Ali SM, Uversky VN, Khan RH. An in-vitro elucidation of inhibitory potential of carminic acid: Possible therapeutic approach for neurodegenerative diseases Journal of Molecular Liquids. 303: 112692. DOI: 10.1016/J.Molliq.2020.112692  0.394
2020 Fonin AV, Antifeeva IA, Shpironok OG, Uversky VN, Kuznetsova IM, Turoverov KK. The Role of Polyampholyte Regions of Intrinsically Disordered Proteins in the Formation of Membraneless Organelles Biophysical Journal. 118. DOI: 10.1016/J.Bpj.2019.11.2114  0.454
2019 Nagibina GS, Glukhova KA, Uversky VN, Melnik TN, Melnik BS. Intrinsic Disorder-Based Design of Stable Globular Proteins. Biomolecules. 10. PMID 31906016 DOI: 10.1016/Bs.Pmbts.2020.05.005  0.477
2019 Kim MY, Na I, Kim JS, Son SH, Choi S, Lee SE, Kim JH, Jang K, Alterovitz G, Chen Y, van der Vaart A, Won HS, Uversky VN, Kim CG. Rational discovery of antimetastatic agents targeting the intrinsically disordered region of MBD2. Science Advances. 5: eaav9810. PMID 31799386 DOI: 10.1126/Sciadv.Aav9810  0.776
2019 Puster LO, Stanley CB, Uversky VN, Curtis JE, Krueger S, Chu Y, Peterson CB. Characterization of An Extensive Interface on Vitronectin for Binding to PAI-1: Adoption of Structure in an Intrinsically Disordered Region. Biochemistry. PMID 31793295 DOI: 10.1021/Acs.Biochem.9B00605  0.382
2019 Djulbegovic MB, Uversky VN. Expanding the understanding of the heterogeneous nature of melanoma with bioinformatics and disorder-based proteomics. International Journal of Biological Macromolecules. 150: 1281-1293. PMID 31743721 DOI: 10.1016/J.Ijbiomac.2019.10.139  0.775
2019 Kumar D, Singh A, Kumar P, Uversky VN, Rao CD, Giri R. Understanding the penetrance of intrinsic protein disorder in Rotavirus proteome. International Journal of Biological Macromolecules. PMID 31739058 DOI: 10.1016/J.Ijbiomac.2019.09.166  0.475
2019 Sharma N, Fonin AV, Shpironok OG, Silonov SA, Turoverov KK, Uversky VN, Kuznetsova IM, Giri R. Folding perspectives of an intrinsically disordered transactivation domain and its single mutation breaking the folding propensity. International Journal of Biological Macromolecules. PMID 31733244 DOI: 10.1016/J.Ijbiomac.2019.11.111  0.355
2019 Majid N, Siddiqi MK, Khan AN, Shabnam S, Malik S, Alam A, Uversky VN, Khan RH. Biophysical Elucidation of Amyloid Fibrillation Inhibition and Prevention of Secondary Nucleation by Cholic Acid: An Unexplored Function of Cholic Acid. Acs Chemical Neuroscience. PMID 31661243 DOI: 10.1021/Acschemneuro.9B00482  0.301
2019 El Hadidy N, Uversky VN. Intrinsic Disorder of the BAF Complex: Roles in Chromatin Remodeling and Disease Development. International Journal of Molecular Sciences. 20. PMID 31652801 DOI: 10.3390/Ijms20215260  0.301
2019 Webster JM, Darling AL, Uversky VN, Blair LJ. Small Heat Shock Proteins, Big Impact on Protein Aggregation in Neurodegenerative Disease. Frontiers in Pharmacology. 10: 1047. PMID 31619995 DOI: 10.3389/Fphar.2019.01047  0.789
2019 Coskuner O, Uversky VN. Intrinsically disordered proteins in various hypotheses on the pathogenesis of Alzheimer's and Parkinson's diseases. Progress in Molecular Biology and Translational Science. 166: 145-223. PMID 31521231 DOI: 10.1016/Bs.Pmbts.2019.05.007  0.401
2019 Uversky VN. Protein intrinsic disorder and structure-function continuum. Prog Mol Biol Transl Sci. 166: 1-17. PMID 31521229 DOI: 10.1016/Bs.Pmbts.2019.05.003  0.47
2019 Uversky VN. Supramolecular Fuzziness of Intracellular Liquid Droplets: Liquid-Liquid Phase Transitions, Membrane-Less Organelles, and Intrinsic Disorder Molecules. 24: E3265. PMID 31500307 DOI: 10.3390/Molecules24183265  0.403
2019 Yan J, Cheng J, Kurgan L, Uversky VN. Structural and functional analysis of "non-smelly" proteins Cell Mol Life Sci. PMID 31486849 DOI: 10.1007/s00018-019-03292-1  0.395
2019 Yan J, Cheng J, Kurgan L, Uversky VN. Structural and functional analysis of "non-smelly" proteins. Cellular and Molecular Life Sciences : Cmls. PMID 31486849 DOI: 10.1007/S00018-019-03292-1  0.496
2019 Nwanochie E, Uversky VN. Structure Determination by Single-Particle Cryo-Electron Microscopy: Only the Sky (and Intrinsic Disorder) is the Limit. Int J Mol Sci. 20: E4186. PMID 31461845 DOI: 10.3390/Ijms20174186  0.37
2019 Fonin AV, Darling AL, Kuznetsova IM, Turoverov KK, Uversky VN. Multi-functionality of proteins involved in GPCR and G protein signaling: making sense of structure-function continuum with intrinsic disorder-based proteoforms. Cellular and Molecular Life Sciences : Cmls. PMID 31428838 DOI: 10.1007/S00018-019-03276-1  0.773
2019 Stojanovski BM, Hunter GA, Na I, Uversky VN, Jiang RHY, Ferreira GC. 5-Aminolevulinate synthase catalysis: The catcher in heme biosynthesis. Molecular Genetics and Metabolism. PMID 31345668 DOI: 10.1016/J.Ymgme.2019.06.003  0.773
2019 Alghamdi M, Al Ghamdi KA, Khan RH, Uversky VN, Redwan EM. An interplay of structure and intrinsic disorder in the functionality of peptidylarginine deiminases, a family of key autoimmunity-related enzymes. Cellular and Molecular Life Sciences : Cmls. PMID 31342121 DOI: 10.1007/S00018-019-03237-8  0.377
2019 Palumbo E, Zhao B, Xue B, Uversky VN, Davé V. Analyzing aggregation propensities of clinically relevant PTEN mutants: a new culprit in pathogenesis of cancer and other PTENopathies. Journal of Biomolecular Structure & Dynamics. 1-14. PMID 31232187 DOI: 10.1080/07391102.2019.1630005  0.377
2019 Djulbegovic MB, Uversky VN. Ferroptosis - An iron- and disorder-dependent programmed cell death Int J Biol Macromol. 135: 1052-1069. PMID 31175900 DOI: 10.1016/J.Ijbiomac.2019.05.221  0.802
2019 Oldfield CJ, Peng Z, Uversky VN, Kurgan L. Codon selection reduces GC content bias in nucleic acids encoding for intrinsically disordered proteins. Cellular and Molecular Life Sciences : Cmls. PMID 31175370 DOI: 10.1007/S00018-019-03166-6  0.337
2019 Darling AL, Zaslavsky BY, Uversky VN. Intrinsic Disorder-Based Emergence in Cellular Biology: Physiological and Pathological Liquid-Liquid Phase Transitions in Cells. Polymers. 11. PMID 31167414 DOI: 10.3390/Polym11060990  0.727
2019 Appadurai R, Uversky VN, Srivastava A. The Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins. The Journal of Membrane Biology. PMID 31139867 DOI: 10.1007/S00232-019-00069-2  0.455
2019 Polanco C, Uversky VN, Márquez MF, Buhse T, Estrada MA, Huberman A. Bioinformatics characterisation of the (mutated) proteins related to Andersen-Tawil syndrome. Mathematical Biosciences and Engineering : Mbe. 16: 2532-2548. PMID 31137226 DOI: 10.3934/Mbe.2019127  0.387
2019 Turoverov KK, Kuznetsova IM, Fonin AV, Darling AL, Zaslavsky BY, Uversky VN. Stochasticity of Biological Soft Matter: Emerging Concepts in Intrinsically Disordered Proteins and Biological Phase Separation. Trends in Biochemical Sciences. PMID 31023505 DOI: 10.1016/J.Tibs.2019.03.005  0.772
2019 Chowdhury S, Sen S, Banerjee A, Uversky VN, Maulik U, Chattopadhyay K. Network mapping of the conformational heterogeneity of SOD1 by deploying statistical cluster analysis of FTIR spectra. Cellular and Molecular Life Sciences : Cmls. PMID 31011770 DOI: 10.1007/S00018-019-03108-2  0.331
2019 Redwan EM, Alkarim SA, El-Hanafy AA, Saad YM, Almehdar HA, Uversky VN. Disorder in milk proteins: adipophilin and TIP47, important constituents of the milk fat globule membrane. Journal of Biomolecular Structure & Dynamics. 1-16. PMID 30896308 DOI: 10.1080/07391102.2019.1592027  0.403
2019 Daniels MJ, Nourse JB, Kim H, Sainati V, Schiavina M, Murrali MG, Pan B, Ferrie JJ, Haney CM, Moons R, Gould NS, Natalello A, Grandori R, Sobott F, Petersson EJ, ... ... Uversky VN, et al. Cyclized NDGA modifies dynamic α-synuclein monomers preventing aggregation and toxicity. Scientific Reports. 9: 2937. PMID 30814575 DOI: 10.1038/S41598-019-39480-Z  0.342
2019 Vincent M, Uversky VN, Schnell S. On the Need to Develop Guidelines for Characterizing and Reporting Intrinsic Disorder in Proteins. Proteomics. e1800415. PMID 30793871 DOI: 10.1002/Pmic.201800415  0.415
2019 Coskuner O, Uversky VN. Alanine Scanning Effects on the Biochemical and Biophysical Properties of Intrinsically Disordered Proteins: A Case Study of the Histidine to Alanine Mutations in Amyloid-β42. Journal of Chemical Information and Modeling. PMID 30694660 DOI: 10.1021/Acs.Jcim.8B00926  0.457
2019 Darling AL, Breydo L, Rivas EG, Gebru NT, Zheng D, Baker JD, Blair LJ, Dickey CA, Koren J, Uversky VN. Repeated repeat problems: Combinatorial effect of C9orf72-derived dipeptide repeat proteins. International Journal of Biological Macromolecules. PMID 30639592 DOI: 10.1016/J.Ijbiomac.2019.01.035  0.789
2019 Redwan EM, AlJaddawi AA, Uversky VN. Structural disorder in the proteome and interactome of Alkhurma virus (ALKV) Cellular and Molecular Life Sciences. 76: 577-608. PMID 30443749 DOI: 10.1007/S00018-018-2968-8  0.453
2019 Oldfield CJ, Uversky VN, Kurgan L. Predicting Functions of Disordered Proteins with MoRFpred. Methods in Molecular Biology (Clifton, N.J.). 1851: 337-352. PMID 30298407 DOI: 10.1007/978-1-4939-8736-8_19  0.462
2019 Sabha BH, Alzahrani F, Almehdar HA, Uversky VN, Redwan EM. Disorder in Milk Proteins: Lactadherin Multifunctionality and Structure. Current Protein & Peptide Science. 19: 983-997. PMID 29879884 DOI: 10.2174/1389203719666180608091849  0.404
2019 Uversky VN. Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics Frontiers in Physics. 7. DOI: 10.3389/Fphy.2019.00010  0.506
2019 Chandel TI, Masroor A, Siddiqi MK, Siddique IA, Jahan I, Ali M, Nayeem SM, Uversky VN, Khan RH. Molecular basis of the inhibition and disaggregation of thermally-induced amyloid fibrils of human serum albumin by an anti-Parkinson's drug, benserazide hydrochloride Journal of Molecular Liquids. 278: 553-567. DOI: 10.1016/J.Molliq.2018.12.127  0.322
2019 Vincent M, Uversky VN, Schnell S. Front Cover: On the Need to Develop Guidelines for Characterizing and Reporting Intrinsic Disorder in Proteins Proteomics. 19: 1970041. DOI: 10.1002/Pmic.201970041  0.429
2018 Deryusheva E, Nemashkalova E, Galloux M, Richard CA, Eléouët JF, Kovacs D, Van Belle K, Tompa P, Uversky VN, Permyakov S. Does intrinsic disorder in proteins favors their interaction with lipids? Proteomics. e1800098. PMID 30592560 DOI: 10.1002/Pmic.201800098  0.402
2018 Fonin AV, Stepanenko OV, Sitdikova AK, Antifeeva IA, Kostyleva EI, Polyanichko AM, Karasev MM, Silonov SA, Povarova OI, Kuznetsova IM, Uversky VN, Turoverov KК. Folding of poly-amino acids and intrinsically disordered proteins in overcrowded milieu induced by pH change. International Journal of Biological Macromolecules. PMID 30529354 DOI: 10.1016/J.Ijbiomac.2018.12.038  0.682
2018 Kutyshenko VP, Mikoulinskaia GV, Chernyshov SV, Yegorov AY, Prokhorov DA, Uversky VN. Effect of C-terminal His-tag and purification routine on the activity and structure of the metalloenzyme, l-alanyl-d-glutamate peptidase from the T5 bacteriophage. International Journal of Biological Macromolecules. PMID 30500497 DOI: 10.1016/J.Ijbiomac.2018.11.219  0.344
2018 Hakeem S, Singh I, Sharma P, Uppal A, Khajuria Y, Verma V, Uversky VN, Chandra R. Molecular dynamics analysis of the effects of GTP, GDP, and benzimidazole derivative on structural dynamics of a cell division protein FtsZ from Mycobacterium tuberculosis. Journal of Biomolecular Structure & Dynamics. 1-25. PMID 30466358 DOI: 10.1080/07391102.2018.1548979  0.373
2018 da Silva NR, Ferreira LA, Teixeira JA, Uversky VN, Zaslavsky BY. Effects of sodium chloride and sodium perchlorate on properties and partition behavior of solutes in aqueous dextran-polyethylene glycol and polyethylene glycol-sodium sulfate two-phase systems. Journal of Chromatography. A. PMID 30448052 DOI: 10.1016/J.Chroma.2018.11.015  0.335
2018 Chandel TI, Zaidi N, Zaman M, Jahan I, Masroor A, Siddique IA, Nayeem SM, Ali M, Uversky VN, Khan RH. A multiparametric analysis of the synergistic impact of anti-Parkinson's drugs on the fibrillation of human serum albumin. Biochimica Et Biophysica Acta. Proteins and Proteomics. PMID 30312771 DOI: 10.1016/J.Bbapap.2018.10.003  0.359
2018 Ferreira LA, Walczyk Mooradally A, Zaslavsky B, Uversky VN, Graether SP. Effect of an Intrinsically Disordered Plant Stress Protein on the Properties of Water. Biophysical Journal. PMID 30297135 DOI: 10.1016/J.Bpj.2018.09.014  0.323
2018 Sanina N, Chopenko N, Mazeika A, Davydova L, Leonova G, Stenkova A, Uversky VN, Kostetsky E. Immunogenicity and Protective Activity of a Chimeric Protein Based on the Domain III of the Tick-Borne Encephalitis Virus E Protein and the OmpF Porin of Incorporated into the TI-Complex. International Journal of Molecular Sciences. 19. PMID 30274357 DOI: 10.3390/Ijms19102988  0.335
2018 Siddiqi MK, Alam P, Malik S, Majid N, Chaturvedi SK, Rajan S, Ajmal MR, Khan MV, Uversky VN, Khan RH. Stabilizing proteins to prevent conformational changes required for amyloid fibril formation. Journal of Cellular Biochemistry. PMID 30242891 DOI: 10.1002/Jcb.27576  0.412
2018 Kulkarni P, Uversky VN. Intrinsically Disordered Proteins: The Dark Horse of the Dark Proteome. Proteomics. 18: e1800061. PMID 30218496 DOI: 10.1002/Pmic.201800061  0.446
2018 Hu G, Wang K, Song J, Uversky VN, Kurgan L. Taxonomic Landscape of the Dark Proteomes: Whole-Proteome Scale Interplay Between Structural Darkness, Intrinsic Disorder, and Crystallization Propensity. Proteomics. e1800243. PMID 30198635 DOI: 10.1002/Pmic.201800243  0.452
2018 Permyakov SE, Vologzhannikova AA, Khorn PA, Shevelyova MP, Kazakov AS, Emelyanenko VI, Denesyuk AI, Denessiouk K, Uversky VN, Permyakov EA. Comprehensive analysis of the roles of 'black' and 'gray' clusters in structure and function of rat β-parvalbumin. Cell Calcium. 75: 64-78. PMID 30176502 DOI: 10.1016/J.Ceca.2018.08.005  0.303
2018 Paraan M, Bhattacharya N, Uversky VN, Stagg SM. Flexibility of the sec13/31 cage is influenced by the sec31 C-terminal disordered domain. Journal of Structural Biology. PMID 30172710 DOI: 10.1016/J.Jsb.2018.08.016  0.362
2018 Basavanhally T, Fonseca R, Uversky VN. Born This Way: Using Intrinsic Disorder to Map the Connections between SLITRKs, TSHR, and Male Sexual Orientation. Proteomics. 18: e1800307. PMID 30156382 DOI: 10.1002/Pmic.201800307  0.38
2018 Fonin AV, Darling AL, Kuznetsova IM, Turoverov KK, Uversky VN. Intrinsically disordered proteins in crowded milieu: when chaos prevails within the cellular gumbo. Cellular and Molecular Life Sciences : Cmls. PMID 30066087 DOI: 10.1007/S00018-018-2894-9  0.802
2018 Na I, Catena D, Kong MJ, Ferreira GC, Uversky VN. Anti-Correlation between the Dynamics of the Active Site Loop and C-Terminal Tail in Relation to the Homodimer Asymmetry of the Mouse Erythroid 5-Aminolevulinate Synthase. International Journal of Molecular Sciences. 19. PMID 29958424 DOI: 10.3390/Ijms19071899  0.768
2018 Zaslavsky BY, Ferreira LA, Darling AL, Uversky VN. The solvent side of proteinaceous membrane-less organelles in light of aqueous two-phase systems. International Journal of Biological Macromolecules. PMID 29890250 DOI: 10.1016/J.Ijbiomac.2018.06.030  0.725
2018 Askenasy I, Murray D, Andrews RM, Uversky VN, He H, Stroupe ME. Structure-Function Relationships in the Oligomeric NADPH-Dependent Assimilatory Sulfite Reductase. Biochemistry. PMID 29787249 DOI: 10.1021/Acs.Biochem.8B00446  0.399
2018 Darling AL, Uversky VN. Intrinsic Disorder and Posttranslational Modifications: The Darker Side of the Biological Dark Matter. Frontiers in Genetics. 9: 158. PMID 29780404 DOI: 10.3389/Fgene.2018.00158  0.78
2018 Singh A, Kumar A, Yadav R, Uversky VN, Giri R. Deciphering the dark proteome of Chikungunya virus. Scientific Reports. 8: 5822. PMID 29643398 DOI: 10.1038/S41598-018-23969-0  0.419
2018 Polanco C, Samaniego Mendoza JL, Buhse T, Uversky VN, Bañuelos Chao IP, Bañuelos Cedano MA, Tavera FM, Tavera DM, Falconi M, Ponce de León AV. On the Regularities of the Polar Profiles of Proteins Related to Ebola Virus Infection and their Functional Domains. Cell Biochemistry and Biophysics. 76: 411-431. PMID 29511990 DOI: 10.1007/S12013-018-0839-4  0.379
2018 Gurevich VV, Gurevich EV, Uversky VN. Arrestins: structural disorder creates rich functionality. Protein & Cell. 9: 986-1003. PMID 29453740 DOI: 10.1007/S13238-017-0501-8  0.461
2018 Fealey ME, Binder BP, Uversky VN, Hinderliter A, Thomas DD. Structural Impact of Phosphorylation and Dielectric Constant Variation on Synaptotagmin's IDR. Biophysical Journal. 114: 550-561. PMID 29414700 DOI: 10.1016/J.Bpj.2017.12.013  0.353
2018 Redwan EM, Al-Hejin AM, Almehdar HA, Elsaway AM, Uversky VN. Prediction of Disordered Regions and Their Roles in the Anti-Pathogenic and Immunomodulatory Functions of Butyrophilins. Molecules (Basel, Switzerland). 23. PMID 29401697 DOI: 10.3390/Molecules23020328  0.427
2018 Coskuner-Weber O, Uversky VN. Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology. International Journal of Molecular Sciences. 19. PMID 29364151 DOI: 10.3390/Ijms19020336  0.366
2018 Ferreira LA, Uversky VN, Zaslavsky BY. Phase equilibria, solvent properties, and protein partitioning in aqueous polyethylene glycol-600-trimethylamine N-oxide and polyethylene glycol-600-choline chloride two-phase systems. Journal of Chromatography. A. PMID 29307533 DOI: 10.1016/J.Chroma.2018.01.010  0.303
2018 Zaslavsky BY, Uversky VN. In Aqua Veritas: The Indispensable yet Mostly Ignored Role of Water in Phase Separation and Membrane-less Organelles. Biochemistry. 57: 2437-2451. PMID 29303563 DOI: 10.1021/Acs.Biochem.7B01215  0.305
2018 Breydo L, Almehdar HA, El-Fakharany EM, Redwan EM, Uversky VN. Not all AMLETs are made equal: complexes of cow and camel α-lactalbumin with oleic acid show different structure and stability. Journal of Biomolecular Structure & Dynamics. 36: 4405-4412. PMID 29237329 DOI: 10.1080/07391102.2017.1417163  0.626
2018 Litus EA, Permyakov SE, Uversky VN, Permyakov EA. Intrinsically Disordered Regions in Serum Albumin: What Are They For? Cell Biochemistry and Biophysics. 76: 39-57. PMID 28281231 DOI: 10.1007/S12013-017-0785-6  0.366
2018 Uversky VN. How to Predict Disorder in a Protein of Interest. Methods in Molecular Biology (Clifton, N.J.). 1484: 137-158. PMID 27787825 DOI: 10.1007/978-1-4939-6406-2_11  0.382
2017 Uversky VN. Paradoxes and wonders of intrinsic disorder: Stability of instability. Intrinsically Disordered Proteins. 5: e1327757. PMID 30250771 DOI: 10.1080/21690707.2017.1327757  0.329
2017 Uversky VN. Intrinsic Disorder, Protein-Protein Interactions, and Disease. Advances in Protein Chemistry and Structural Biology. 110: 85-121. PMID 29413001 DOI: 10.1016/Bs.Apcsb.2017.06.005  0.492
2017 Hu G, Wu Z, Uversky VN, Kurgan L. Functional Analysis of Human Hub Proteins and Their Interactors Involved in the Intrinsic Disorder-Enriched Interactions. International Journal of Molecular Sciences. 18. PMID 29257115 DOI: 10.3390/Ijms18122761  0.499
2017 Varricchio L, Falchi M, Dall'Ora M, De Benedittis C, Ruggeri A, Uversky VN, Migliaccio AR. Calreticulin: Challenges Posed by the Intrinsically Disordered Nature of Calreticulin to the Study of Its Function. Frontiers in Cell and Developmental Biology. 5: 96. PMID 29218307 DOI: 10.3389/Fcell.2017.00096  0.468
2017 Darling AL, Uversky VN. Intrinsic Disorder in Proteins with Pathogenic Repeat Expansions. Molecules (Basel, Switzerland). 22. PMID 29186753 DOI: 10.3390/Molecules22122027  0.797
2017 Kuppireddy VS, Uversky VN, Toh SS, Tsai MC, Beckerson WC, Cahill C, Carman B, Perlin MH. Identification and Initial Characterization of the Effectors of an Anther Smut Fungus and Potential Host Target Proteins. International Journal of Molecular Sciences. 18. PMID 29165363 DOI: 10.3390/Ijms18112489  0.377
2017 Mishra PM, Uversky VN, Giri R. Molecular Recognition Features in Zika Virus Proteome. Journal of Molecular Biology. PMID 29080786 DOI: 10.1016/J.Jmb.2017.10.018  0.483
2017 Darling A, Liu Y, Oldfield CJ, Uversky VN. Intrinsically Disordered Proteome of Human Membrane-Less Organelles. Proteomics. PMID 29068531 DOI: 10.1002/Pmic.201700193  0.769
2017 Vologzhannikova AA, Khorn PA, Kazakov AS, Ismailov RG, Sokolov AS, Uversky VN, Permyakov EA, Permyakov SE. In search for globally disordered apo-parvalbumins: Case of parvalbumin β-1 from coho salmon. Cell Calcium. 67: 53-64. PMID 29029791 DOI: 10.1016/J.Ceca.2017.08.011  0.403
2017 Uversky VN. The roles of intrinsic disorder-based liquid-liquid phase transitions in the "Dr. Jekyll-Mr. Hyde" behavior of proteins involved in amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Autophagy. 13: 2115-2162. PMID 28980860 DOI: 10.1080/15548627.2017.1384889  0.465
2017 Janis B, Uversky VN, Menze MA. Potential functions of LEA proteins from the brine shrimp Artemia franciscana - anhydrobiosis meets bioinformatics. Journal of Biomolecular Structure & Dynamics. 36: 3291-3309. PMID 28971739 DOI: 10.1080/07391102.2017.1387177  0.468
2017 Du Z, Uversky VN. A Comprehensive Survey of the Roles of Highly Disordered Proteins in Type 2 Diabetes. International Journal of Molecular Sciences. 18. PMID 28934129 DOI: 10.3390/Ijms18102010  0.463
2017 Fonin AV, Golikova AD, Zvereva IA, D'Auria S, Staiano M, Uversky VN, Kuznetsova IM, Turoverov KK. Osmolyte-Like Stabilizing Effects of Low GdnHCl Concentrations on d-Glucose/d-Galactose-Binding Protein. International Journal of Molecular Sciences. 18. PMID 28925982 DOI: 10.3390/Ijms18092008  0.394
2017 Coskuner O, Uversky VN. BMP-2 and BMP-9 binding specificities with ALK-3 in aqueous solution with dynamics. Journal of Molecular Graphics & Modelling. 77: 181-188. PMID 28869862 DOI: 10.1016/J.Jmgm.2017.08.005  0.366
2017 Liu Y, Yang M, Cheng H, Sun N, Liu S, Li S, Wang Y, Zheng Y, Uversky VN. The Effect of Phosphorylation on the Salt-Tolerance-Related Functions of the Soybean Protein PM18, a Member of the Group-3 LEA Protein Family. Biochimica Et Biophysica Acta. PMID 28867216 DOI: 10.1016/J.Bbapap.2017.08.020  0.456
2017 Uversky VN, El-Baky NA, El-Fakharany EM, Sabry A, Mattar EH, Uversky AV, Redwan EM. Functionality of intrinsic disorder in tumor necrosis factor-α and its receptors. The Febs Journal. 284: 3589-3618. PMID 28746777 DOI: 10.1111/Febs.14182  0.367
2017 Palombo M, Bonucci A, Etienne E, Ciurli S, Uversky VN, Guigliarelli B, Belle V, Mileo E, Zambelli B. The relationship between folding and activity in UreG, an intrinsically disordered enzyme. Scientific Reports. 7: 5977. PMID 28729736 DOI: 10.1038/S41598-017-06330-9  0.424
2017 Novikova OD, Chistyulin DK, Khomenko VA, Sidorin EV, Kim NY, Sanina NM, Portnyagina OY, Solov'eva TF, Uversky VN, Shnyrov VL. Peculiarities of thermal denaturation of OmpF porin from Yersinia ruckeri. Molecular Biosystems. PMID 28726924 DOI: 10.1039/C7Mb00239D  0.429
2017 Du Z, Uversky VN. Functional roles of intrinsic disorder in CRISPR-associated protein Cas9. Molecular Biosystems. PMID 28692085 DOI: 10.1039/C7Mb00279C  0.486
2017 Baker JD, Shelton LB, Zheng D, Favretto F, Nordhues BA, Darling A, Sullivan LE, Sun Z, Solanki PK, Martin MD, Suntharalingam A, Sabbagh JJ, Becker S, Mandelkow E, Uversky VN, et al. Human cyclophilin 40 unravels neurotoxic amyloids. Plos Biology. 15: e2001336. PMID 28654636 DOI: 10.1371/Journal.Pbio.2001336  0.775
2017 Ghag G, Holler CJ, Taylor G, Kukar TL, Uversky VN, Rangachari V. Disulfide Bonds and Disorder in Granulin-3: an Unusual Handshake between Structural Stability and Plasticity. Protein Science : a Publication of the Protein Society. PMID 28608407 DOI: 10.1002/Pro.3212  0.45
2017 Meng F, Uversky VN, Kurgan L. Comprehensive review of methods for prediction of intrinsic disorder and its molecular functions. Cellular and Molecular Life Sciences : Cmls. PMID 28589442 DOI: 10.1007/S00018-017-2555-4  0.404
2017 Uversky VN. Intrinsic disorder here, there, and everywhere, and nowhere to escape from it. Cellular and Molecular Life Sciences : Cmls. 74: 3065-3067. PMID 28589440 DOI: 10.1007/S00018-017-2554-5  0.473
2017 Niyangoda C, Miti T, Breydo L, Uversky V, Muschol M. Carbonyl-based blue autofluorescence of proteins and amino acids. Plos One. 12: e0176983. PMID 28542206 DOI: 10.1371/Journal.Pone.0176983  0.676
2017 Liu Y, Wu J, Sun N, Tu C, Shi X, Cheng H, Liu S, Li S, Wang Y, Zheng Y, Uversky VN. Intrinsically disordered proteins as important players during desiccation stress of the soybean radicles. Journal of Proteome Research. PMID 28525284 DOI: 10.1021/Acs.Jproteome.6B01045  0.457
2017 Migliaccio AR, Uversky VN. Dissecting physical structure of calreticulin, an intrinsically disordered Ca-buffering chaperone from endoplasmic reticulum. Journal of Biomolecular Structure & Dynamics. 36: 1617-1636. PMID 28504081 DOI: 10.1080/07391102.2017.1330224  0.395
2017 Nascimento TP, Sales AE, Porto TS, Costa RMPB, Breydo L, Uversky VN, Porto ALF, Converti A. Purification, biochemical, and structural characterization of a novel fibrinolytic enzyme from Mucor subtilissimus UCP 1262. Bioprocess and Biosystems Engineering. PMID 28500420 DOI: 10.1007/S00449-017-1781-3  0.652
2017 Uversky VN. Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism. F1000research. 6: 525-525. PMID 28491292 DOI: 10.12688/F1000Research.10536.1  0.358
2017 Coskuner O, Uversky VN. Tyrosine Regulates β-Sheet Structure Formation in Amyloid-β42: A New Clustering Algorithm for Disordered Proteins. Journal of Chemical Information and Modeling. PMID 28474890 DOI: 10.1021/Acs.Jcim.6B00761  0.382
2017 Meng F, Uversky V, Kurgan L. Computational Prediction of Intrinsic Disorder in Proteins. Current Protocols in Protein Science. 88: 2.16.1-2.16.14. PMID 28369666 DOI: 10.1002/Cpps.28  0.37
2017 Kulkarni P, Uversky VN. Cancer/Testis Antigens: "Smart" Biomarkers for Diagnosis and Prognosis of Prostate and Other Cancers. International Journal of Molecular Sciences. 18. PMID 28362316 DOI: 10.3390/Ijms18040740  0.337
2017 Sormanni P, Piovesan D, Heller GT, Bonomi M, Kukic P, Camilloni C, Fuxreiter M, Dosztanyi Z, Pappu RV, Babu MM, Longhi S, Tompa P, Dunker AK, Uversky VN, Tosatto SC, et al. Simultaneous quantification of protein order and disorder. Nature Chemical Biology. 13: 339-342. PMID 28328918 DOI: 10.1038/Nchembio.2331  0.457
2017 DeForte S, Uversky VN. Quarterly intrinsic disorder digest (April-May-June, 2014). Intrinsically Disordered Proteins. 5: e1287505. PMID 28321370 DOI: 10.1080/21690707.2017.1287505  0.781
2017 Malaney P, Uversky VN, Davé V. PTEN proteoforms in biology and disease. Cellular and Molecular Life Sciences : Cmls. 74: 2783-2794. PMID 28289760 DOI: 10.1007/S00018-017-2500-6  0.403
2017 Redington JM, Breydo L, Uversky VN. When Good Goes Awry: The Aggregation of Protein Therapeutics. Protein and Peptide Letters. 24: 340-347. PMID 28190397 DOI: 10.2174/0929866524666170209153421  0.698
2017 Fonin AV, Silonov SA, Sitdikova AK, Kuznetsova IM, Uversky VN, Turoverov KK. Structure and Conformational Properties of d-Glucose/d-Galactose-Binding Protein in Crowded Milieu. Molecules (Basel, Switzerland). 22. PMID 28178192 DOI: 10.3390/Molecules22020244  0.42
2017 DeForte S, Uversky VN. Not an exception to the rule: the functional significance of intrinsically disordered protein regions in enzymes. Molecular Biosystems. 13: 463-469. PMID 28098335 DOI: 10.1039/C6Mb00741D  0.797
2017 Kathiriya JJ, Pathak RR, Bezginov A, Xue B, Uversky VN, Tillier ER, Davé V. Data on evolution of intrinsically disordered regions of the human kinome and contribution of FAK1 IDRs to cytoskeletal remodeling. Data in Brief. 10: 315-324. PMID 28004021 DOI: 10.1016/J.Dib.2016.11.099  0.419
2017 Permyakov EA, Uversky VN, Permyakov SE. Parvalbumin as a Pleomorphic Protein. Current Protein & Peptide Science. 18: 780-794. PMID 27964700 DOI: 10.2174/1389203717666161213115746  0.364
2017 Uversky VN, Redwan EM. Erythropoietin and co.: intrinsic structure and functional disorder. Molecular Biosystems. 13: 56-72. PMID 27833947 DOI: 10.1039/C6Mb00657D  0.421
2017 Polanco C, Castañón-González JA, Uversky VN, Buhse T, Samaniego Mendoza JL, Calva JJ. Electronegativity and intrinsic disorder of preeclampsia-related proteins. Acta Biochimica Polonica. 64: 99-111. PMID 27824362 DOI: 10.18388/Abp.2016_1300  0.477
2017 Merone J, Nwogu O, Redington JM, Uversky VN. Intrinsic Disorder in Male Sex Determination: Disorderedness of Proteins from the Sry Transcriptional Network. Current Protein & Peptide Science. 18: 482-514. PMID 27804859 DOI: 10.2174/1389203717666161028150244  0.398
2017 Peng Z, Wang C, Uversky VN, Kurgan L. Prediction of Disordered RNA, DNA, and Protein Binding Regions Using DisoRDPbind. Methods in Molecular Biology (Clifton, N.J.). 1484: 187-203. PMID 27787828 DOI: 10.1007/978-1-4939-6406-2_14  0.406
2017 Permyakov EA, Permyakov SE, Breydo L, Redwan EM, Almehdar HA, Uversky VN. Disorder in Milk Proteins: α-Lactalbumin. Part C. Peculiarities of Metal Binding. Current Protein & Peptide Science. 17: 735-745. PMID 27238572 DOI: 10.2174/1389203717666160530151534  0.668
2017 Redington JM, Breydo L, Almehdar HA, Redwan EM, Uversky VN. α-Lactalbumin: Of Camels and Cows. Protein and Peptide Letters. 23: 1072-1080. PMID 27184498 DOI: 10.2174/0929866523666160517123738  0.686
2017 Uversky VN, Permyakov SE, Breydo L, Redwan EM, Almehdar HA, Permyakov EA. Disorder in Milk Proteins: α-Lactalbumin. Part B. A Multifunctional Whey Protein Acting as an Oligomeric Molten Globular "Oil Container" in the Anti-Tumorigenic Drugs, Liprotides. Current Protein & Peptide Science. 17: 612-28. PMID 26916155 DOI: 10.2174/1389203717666151203003151  0.71
2017 Rodina NP, Sulatsky MI, Sulatskaya AI, Kuznetsova IM, Uversky VN, Turoverov KK. Photophysical Properties of Fluorescent Probe Thioflavin T in Crowded Milieu Journal of Spectroscopy. 2017: 1-10. DOI: 10.1155/2017/2365746  0.3
2017 Gagarskaia IA, Povarova OI, Uversky VN, Kuznetsova IM, Turoverov KK. The effects of crowding agents Dextran-70k and PEG-8k on actin structure and unfolding reaction Journal of Molecular Structure. 1140: 46-51. DOI: 10.1016/J.Molstruc.2016.12.029  0.317
2017 Ferreira LA, Wu Z, Kurgan L, Uversky VN, Zaslavsky BY. How to manipulate partition behavior of proteins in aqueous two-phase systems: Effect of trimethylamine N-oxide (TMAO) Fluid Phase Equilibria. 449: 217-224. DOI: 10.1016/J.Fluid.2017.07.004  0.325
2016 Lieutaud P, Ferron F, Uversky AV, Kurgan L, Uversky VN, Longhi S. How disordered is my protein and what is its disorder for? A guide through the "dark side" of the protein universe. Intrinsically Disordered Proteins. 4: e1259708. PMID 28232901 DOI: 10.1080/21690707.2016.1259708  0.371
2016 Alowolodu O, Johnson G, Alashwal L, Addou I, Zhdanova IV, Uversky VN. Intrinsic disorder in spondins and some of their interacting partners. Intrinsically Disordered Proteins. 4: e1255295. PMID 28232900 DOI: 10.1080/21690707.2016.1255295  0.304
2016 Fitzsimmons R, Amin N, Uversky VN. Understanding the roles of intrinsic disorder in subunits of hemoglobin and the disease process of sickle cell anemia. Intrinsically Disordered Proteins. 4: e1248273. PMID 28232898 DOI: 10.1080/21690707.2016.1248273  0.305
2016 DeForte S, Reddy KD, Uversky VN. Quarterly intrinsic disorder digest (January-February-March, 2014). Intrinsically Disordered Proteins. 4: e1153395. PMID 28232896 DOI: 10.1080/21690707.2016.1153395  0.806
2016 Uversky VN. Paradoxes and wonders of intrinsic disorder: Complexity of simplicity. Intrinsically Disordered Proteins. 4: e1135015. PMID 28232895 DOI: 10.1080/21690707.2015.1135015  0.335
2016 Breydo L, Redington JM, Uversky VN. Effects of Intrinsic and Extrinsic Factors on Aggregation of Physiologically Important Intrinsically Disordered Proteins. International Review of Cell and Molecular Biology. 329: 145-185. PMID 28109327 DOI: 10.1016/Bs.Ircmb.2016.08.011  0.715
2016 Piovesan D, Tabaro F, Mičetić I, Necci M, Quaglia F, Oldfield CJ, Aspromonte MC, Davey NE, Davidović R, Dosztányi Z, Elofsson A, Gasparini A, Hatos A, Kajava AV, Kalmar L, ... ... Uversky VN, et al. DisProt 7.0: a major update of the database of disordered proteins. Nucleic Acids Research. PMID 27965415 DOI: 10.1093/Nar/Gkw1279  0.344
2016 Dentovskaya SV, Platonov ME, Svetoch TE, Kopylov PK, Kombarova TI, Ivanov SA, Shaikhutdinova RZ, Kolombet LV, Chauhan S, Ablamunits VG, Motin VL, Uversky VN, Anisimov AP. Two Isoforms of Yersinia pestis Plasminogen Activator Pla: Intraspecies Distribution, Intrinsic Disorder Propensity, and Contribution to Virulence. Plos One. 11: e0168089. PMID 27936190 DOI: 10.1371/Journal.Pone.0168089  0.32
2016 Na I, DeForte S, Stojanovski BM, Ferreira GC, Uversky VN. Molecular Dynamics Analysis of the Structural and Dynamic Properties of the Functionally Enhanced Hepta-Variant of Mouse 5-Aminolevulinate Synthase. Journal of Biomolecular Structure & Dynamics. 1-31. PMID 27928941 DOI: 10.1080/07391102.2016.1269688  0.789
2016 Piovesan D, Tabaro F, Mičetić I, Necci M, Quaglia F, Oldfield CJ, Aspromonte MC, Davey NE, Davidović R, Dosztányi Z, Elofsson A, Gasparini A, Hatos A, Kajava AV, Kalmar L, ... ... Uversky VN, et al. DisProt 7.0: a major update of the database of disordered proteins. Nucleic Acids Research. PMID 27899601 DOI: 10.1093/Nar/Gkw1056  0.452
2016 Giri R, Kumar D, Sharma N, Uversky VN. Intrinsically Disordered Side of the Zika Virus Proteome. Frontiers in Cellular and Infection Microbiology. 6: 144. PMID 27867910 DOI: 10.3389/Fcimb.2016.00144  0.45
2016 El-Fakharany EM, Uversky VN, Redwan EM. Comparative Analysis of the Antiviral Activity of Camel, Bovine, and Human Lactoperoxidases Against Herpes Simplex Virus Type 1. Applied Biochemistry and Biotechnology. 182: 294-310. PMID 27854033 DOI: 10.1007/S12010-016-2327-X  0.311
2016 Santamaria N, Alhothali M, Alfonso MH, Breydo L, Uversky VN. Intrinsic disorder in proteins involved in amyotrophic lateral sclerosis. Cellular and Molecular Life Sciences : Cmls. 74: 1297-1318. PMID 27838743 DOI: 10.1007/S00018-016-2416-6  0.731
2016 Uversky VN. Intrinsically disordered proteins in overcrowded milieu: Membrane-less organelles, phase separation, and intrinsic disorder. Current Opinion in Structural Biology. 44: 18-30. PMID 27838525 DOI: 10.1016/J.Sbi.2016.10.015  0.368
2016 Fratz-Berilla EJ, Breydo L, Gouya L, Puy H, Uversky VN, Ferreira GC. Isoniazid inhibits human erythroid 5-aminolevulinate synthase: Molecular mechanism and tolerance study with four X-linked protoporphyria patients. Biochimica Et Biophysica Acta. PMID 27838491 DOI: 10.1016/J.Bbadis.2016.11.011  0.644
2016 Uversky VN. p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure-Function Continuum Concept. International Journal of Molecular Sciences. 17. PMID 27834926 DOI: 10.3390/Ijms17111874  0.455
2016 Uversky VN, Na I, Landau KS, Schenk RO. Highly Disordered Proteins in Prostate Cancer. Current Protein & Peptide Science. PMID 27804860 DOI: 10.2174/1389203717666161028145848  0.775
2016 Stepanenko OV, Stepanenko OV, Kuznetsova IM, Uversky VN, Turoverov KK. Peculiarities of the Super-Folder GFP Folding in a Crowded Milieu. International Journal of Molecular Sciences. 17. PMID 27801849 DOI: 10.3390/Ijms17111805  0.705
2016 Stojanovski BM, Breydo L, Uversky VN, Ferreira GC. The unfolding pathways of the native and molten globule states of 5-aminolevulinate synthase. Biochemical and Biophysical Research Communications. PMID 27751851 DOI: 10.1016/J.Bbrc.2016.10.037  0.627
2016 Carmell MA, Dokshin GA, Skaletsky H, Hu YC, von Wolfswinkel JC, Igarashi KJ, Bellott DW, Nefedov M, Reddien PW, Enders GC, Uversky VN, Mello CC, Page DC. A widely employed germ cell marker is an ancient disordered protein with reproductive functions in diverse eukaryotes. Elife. 5. PMID 27718356 DOI: 10.7554/Elife.19993  0.385
2016 Szénási T, Oláh J, Szabó A, Szunyogh S, Láng A, Perczel A, Lehotzky A, Uversky VN, Ovádi J. Challenging drug target for Parkinson's disease: Pathological complex of the chameleon TPPP/p25 and alpha-synuclein proteins. Biochimica Et Biophysica Acta. PMID 27671864 DOI: 10.1016/J.Bbadis.2016.09.017  0.378
2016 Wu Z, Hu G, Wang K, Zaslavsky BY, Kurgan L, Uversky VN. What are the structural features that drive partitioning of proteins in aqueous two-phase systems? Biochimica Et Biophysica Acta. PMID 27663889 DOI: 10.1016/J.Bbapap.2016.09.010  0.44
2016 Zambelli B, Uversky VN, Ciurli S. Nickel impact on human health: An intrinsic disorder perspective. Biochimica Et Biophysica Acta. 1864: 1714-1731. PMID 27645710 DOI: 10.1016/J.Bbapap.2016.09.008  0.32
2016 Melnik BS, Nagibina GS, Glukhov AS, Melnik TN, Uversky VN. Substitutions of Amino Acids with Large Number of Contacts in the Native State Have no Effect on the Rates of Protein Folding. Biochimica Et Biophysica Acta. 1864: 1809-1817. PMID 27639966 DOI: 10.1016/J.Bbapap.2016.09.006  0.409
2016 Kopylov PK, Platonov ME, Ablamunits VG, Kombarova TI, Ivanov SA, Kadnikova LA, Somov AN, Dentovskaya SV, Uversky VN, Anisimov AP. Yersinia pestis Caf1 Protein: Effect of Sequence Polymorphism on Intrinsic Disorder Propensity, Serological Cross-Reactivity and Cross-Protectivity of Isoforms. Plos One. 11: e0162308. PMID 27606595 DOI: 10.1371/Journal.Pone.0162308  0.394
2016 Shaban H, Na I, Kislichkina AA, Dentovskaya SV, Anisimov AP, Uversky VN. Effect of natural polymorphism on structure and function of the Yersinia pestis outer membrane porin F (OmpF protein): a computational study. Journal of Biomolecular Structure & Dynamics. 1-16. PMID 27593697 DOI: 10.1080/07391102.2016.1224734  0.333
2016 DeForte S, Uversky VN. Order, Disorder, and Everything in Between. Molecules (Basel, Switzerland). 21. PMID 27548131 DOI: 10.3390/Molecules21081090  0.831
2016 Reddy KD, Malipeddi J, DeForte S, Pejaver V, Radivojac P, Uversky VN, Deschenes RJ. Physicochemical sequence characteristics that influence S-palmitoylation propensity. Journal of Biomolecular Structure & Dynamics. 1-14. PMID 27498722 DOI: 10.1080/07391102.2016.1217275  0.818
2016 Javadi S, Yousefi R, Hosseinkhani S, Tamaddon AM, Uversky VN. Protective effects of carnosine on dehydroascorbate-induced structural alteration and opacity of lens crystallins: important implications of carnosine pleiotropic functions to combat cataractogenesis. Journal of Biomolecular Structure & Dynamics. 35: 1766-1784. PMID 27472261 DOI: 10.1080/07391102.2016.1194230  0.413
2016 Landau KS, Na I, Schenck RO, Uversky VN. Unfoldomics of prostate cancer: on the abundance and roles of intrinsically disordered proteins in prostate cancer. Asian Journal of Andrology. PMID 27453073 DOI: 10.4103/1008-682X.184999  0.769
2016 Bürgi J, Xue B, Uversky VN, van der Goot FG. Intrinsic Disorder in Transmembrane Proteins: Roles in Signaling and Topology Prediction. Plos One. 11: e0158594. PMID 27391701 DOI: 10.1371/Journal.Pone.0158594  0.465
2016 Na I, Meng F, Kurgan L, Uversky VN. Autophagy-related intrinsically disordered proteins in intra-nuclear compartments. Molecular Biosystems. PMID 27377881 DOI: 10.1039/C6Mb00069J  0.806
2016 Kutyshenko VP, Mikoulinskaia GV, Molochkov NV, Prokhorov DA, Taran SA, Uversky VN. Structure and dynamics of the retro-form of the bacteriophage T5 endolysin. Biochimica Et Biophysica Acta. 1864: 1281-91. PMID 27376687 DOI: 10.1016/J.Bbapap.2016.06.018  0.388
2016 Luna-Martínez OD, Vidal-Limón A, Villalba-Velázquez MI, Sánchez-Alcalá R, Garduño-Juárez R, Uversky VN, Becerril B. Simple approach for ranking structure determining residues. Peerj. 4: e2136. PMID 27366642 DOI: 10.7717/Peerj.2136  0.448
2016 Breydo L, Kurouski D, Rasool S, Milton S, Wu JW, Uversky VN, Lednev IK, Glabe CG. Structural differences between amyloid beta oligomers. Biochemical and Biophysical Research Communications. PMID 27363332 DOI: 10.1016/J.Bbrc.2016.06.122  0.661
2016 Lobbens ES, Breydo L, Skamris T, Vestergaard B, Jäger AK, Jorgensen L, Uversky V, van de Weert M. Mechanistic study of the inhibitory activity of Geum urbanum extract against α-Synuclein fibrillation. Biochimica Et Biophysica Acta. 1864: 1160-9. PMID 27353564 DOI: 10.1016/J.Bbapap.2016.06.009  0.645
2016 Permyakov EA, Uversky VN, Permyakov SE. Interleukin-11: A Multifunctional Cytokine with Intrinsically Disordered Regions. Cell Biochemistry and Biophysics. 74: 285-96. PMID 27334537 DOI: 10.1007/S12013-016-0752-7  0.375
2016 Yacoub HA, Elazzazy AM, Mahmoud MM, Baeshen MN, Al-Maghrabi OA, Alkarim S, Ahmed ES, Almehdar HA, Uversky VN. Chicken cathelicidins as potent intrinsically disordered biocides with antimicrobial activity against infectious pathogens. Developmental and Comparative Immunology. PMID 27328070 DOI: 10.1016/J.Dci.2016.06.012  0.322
2016 Uversky VN. Protein intrinsic disorder-based liquid-liquid phase transitions in biological systems: Complex coacervates and membrane-less organelles. Advances in Colloid and Interface Science. 239: 97-114. PMID 27291647 DOI: 10.1016/J.Cis.2016.05.012  0.354
2016 Stepanenko OV, Roginskii DO, Stepanenko OV, Kuznetsova IM, Uversky VN, Turoverov KK. Structure and stability of recombinant bovine odorant-binding protein: I. Design and analysis of monomeric mutants. Peerj. 4: e1933. PMID 27114880 DOI: 10.7717/peerj.1933  0.676
2016 Stepanenko OV, Roginskii DO, Stepanenko OV, Kuznetsova IM, Uversky VN, Turoverov KK. Structure and stability of recombinant bovine odorant-binding protein: III. Peculiarities of the wild type bOBP unfolding in crowded milieu. Peerj. 4: e1642. PMID 27114858 DOI: 10.7717/peerj.1642  0.666
2016 Stepanenko OV, Roginskii DO, Stepanenko OV, Kuznetsova IM, Uversky VN, Turoverov KK. Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms. Peerj. 4: e1574. PMID 27114857 DOI: 10.7717/Peerj.1574  0.702
2016 Kutyshenko VP, Prokhorov DA, Mikoulinskaia GV, Molochkov NV, Paskevich SI, Uversky VN. Evidence for the residual tertiary structure in the urea-unfolded form of bacteriophage T5 endolysin. Journal of Biomolecular Structure & Dynamics. 35: 1331-1338. PMID 27109308 DOI: 10.1080/07391102.2016.1182948  0.399
2016 Goh GK, Dunker AK, Uversky VN. Correlating Flavivirus virulence and levels of intrinsic disorder in shell proteins: protective roles vs. immune evasion. Molecular Biosystems. PMID 27102744 DOI: 10.1039/C6Mb00228E  0.357
2016 Na I, Kong MJ, Straight S, Pinto JR, Uversky VN. Troponins, intrinsic disorder, and cardiomyopathy. Biological Chemistry. PMID 27074551 DOI: 10.1515/Hsz-2015-0303  0.785
2016 Whelan JN, Reddy KD, Uversky VN, Teng MN. Functional correlations of respiratory syncytial virus proteins to intrinsic disorder. Molecular Biosystems. 12: 1507-26. PMID 27062995 DOI: 10.1039/C6Mb00122J  0.624
2016 Polanco C, Buhse T, Uversky VN. Structure and function relationships of proteins based on polar profile: a review. Acta Biochimica Polonica. 63: 229-33. PMID 27059018 DOI: 10.18388/Abp.2014_919  0.384
2016 Wang C, Uversky VN, Kurgan L. Disordered nucleiome: Abundance of intrinsic disorder in the DNA and RNA binding proteins in 1121 species from Eukaryota, Bacteria and Archaea. Proteomics. PMID 27037624 DOI: 10.1002/Pmic.201500177  0.461
2016 Ferreira LA, Breydo L, Reichardt C, Uversky VN, Zaslavsky BY. Effects of osmolytes on solvent features of water in aqueous solutions. Journal of Biomolecular Structure & Dynamics. 1-41. PMID 27026414 DOI: 10.1080/07391102.2016.1170633  0.612
2016 Ferreira LA, da Silva NR, Wlodarczyk SR, Loureiro JA, Madeira PP, Teixeira JA, Uversky VN, Zaslavsky BY. Interrelationship between partition behavior of organic compounds and proteins in aqueous dextran-polyethylene glycol and polyethylene glycol-sodium sulfate two-phase systems. Journal of Chromatography. A. PMID 27016118 DOI: 10.1016/J.Chroma.2016.03.032  0.306
2016 Yacoub HA, Al-Maghrabi OA, Ahmed ES, Uversky VN. Abundance and functional roles of intrinsic disorder in the antimicrobial peptides of the NK-lysin family. Journal of Biomolecular Structure & Dynamics. 1-21. PMID 26957115 DOI: 10.1080/07391102.2016.1164077  0.426
2016 Permyakov EA, Permyakov SE, Breydo L, Redwan EM, Almehdar HA, Uversky VN. Disorder in Milk Proteins: α -Lactalbumin. Part A. Structural Properties and Conformational Behavior. Current Protein & Peptide Science. 17: 352-67. PMID 26956441 DOI: 10.2174/138920371704160405001222  0.715
2016 Zaslavsky BY, Uversky VN, Chait A. Analytical applications of partitioning in aqueous two-phase systems: Exploring protein structural changes and protein-partner interactions in vitro and in vivo by solvent interaction analysis method. Biochimica Et Biophysica Acta. 1864: 622-44. PMID 26923390 DOI: 10.1016/J.Bbapap.2016.02.017  0.388
2016 Stojanovski BM, Breydo L, Uversky VN, Ferreira GC. Murine erythroid 5-aminolevulinate synthase: Truncation of a disordered N-terminal extension is not detrimental for catalysis. Biochimica Et Biophysica Acta. 1864: 441-52. PMID 26854603 DOI: 10.1016/J.Bbapap.2016.02.002  0.661
2016 Uversky VN. Dancing Protein Clouds: The Strange Biology and Chaotic Physics of Intrinsically Disordered Proteins. The Journal of Biological Chemistry. 291: 6681-8. PMID 26851286 DOI: 10.1074/Jbc.R115.685859  0.505
2016 Platonov ME, Svetoch TE, Evseeva VV, Knyazeva AI, Dentovskaya SV, Motin VL, Uversky VN, Anisimov AP. Polymorphism of the Cysteine Protease YopT from Yersinia pestis. Protein and Peptide Letters. 23: 379-85. PMID 26845766 DOI: 10.2174/0929866523666160204124259  0.303
2016 Klionsky DJ, Abdelmohsen K, Abe A, Abedin MJ, Abeliovich H, Acevedo Arozena A, Adachi H, Adams CM, Adams PD, Adeli K, Adhihetty PJ, Adler SG, Agam G, Agarwal R, Aghi MK, ... ... Uversky VN, et al. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). Autophagy. 12: 1-222. PMID 26799652 DOI: 10.1080/15548627.2015.1100356  0.311
2016 Kazakov AS, Sokolov AS, Vologzhannikova AA, Permyakova ME, Khorn PA, Ismailov RG, Denessiouk KA, Denesyuk AI, Rastrygina VA, Baksheeva VE, Zernii EY, Zinchenko DV, Glazatov VV, Uversky VN, Mirzabekov TA, et al. Interleukin-11 binds specific EF-hand proteins via their conserved structural motifs. Journal of Biomolecular Structure & Dynamics. 1-47. PMID 26726132 DOI: 10.1080/07391102.2015.1132392  0.312
2016 Ferreira LA, Povarova OI, Stepanenko OV, Sulatskaya AI, Madeira PP, Kuznetsova IM, Turoverov KK, Uversky VN, Zaslavsky BY. Effects of low urea concentrations on protein-water interactions. Journal of Biomolecular Structure & Dynamics. 1-33. PMID 26726130 DOI: 10.1080/07391102.2015.1135823  0.675
2016 DeForte S, Uversky VN. Resolving the ambiguity: Making sense of intrinsic disorder when PDB structures disagree. Protein Science : a Publication of the Protein Society. 25: 676-88. PMID 26683124 DOI: 10.1002/Pro.2864  0.817
2016 Mattar EH, Almehdar HA, Yacoub HA, Uversky VN, Redwan EM. Antimicrobial potentials and structural disorder of human and animal defensins. Cytokine & Growth Factor Reviews. 28: 95-111. PMID 26598808 DOI: 10.1016/J.Cytogfr.2015.11.002  0.347
2016 Kuznetsova IM, Povarova OI, Uversky VN, Turoverov KK. Native globular actin has a thermodynamically unstable quasi-stationary structure with elements of intrinsic disorder. The Febs Journal. 283: 438-45. PMID 26460158 DOI: 10.1111/Febs.13548  0.437
2016 Almehdar HA, El-Fakharany EM, Uversky VN, Redwan EM. Disorder in milk proteins: structure, functional disorder, and biocidal potentials of lactoperoxidase. Current Protein & Peptide Science. 16: 352-65. PMID 25772156 DOI: 10.2174/1389203716666150316114956  0.487
2016 Uversky VN. Under-folded proteins: Conformational ensembles and their roles in protein folding, function, and pathogenesis. Biopolymers. 99: 870-87. PMID 23754493 DOI: 10.1002/Bip.22298  0.486
2016 Melnik BS, Povarnitsyna TV, Glukhov AS, Melnik TN, Uversky VN, Sarma RH. SS-Stabilizing Proteins Rationally: Intrinsic Disorder-Based Design of Stabilizing Disulphide Bridges in GFP. Journal of Biomolecular Structure & Dynamics. 29: 815-24. PMID 22591018 DOI: 10.1080/07391102.2012.10507414  0.423
2016 Carmell MA, Dokshin GA, Skaletsky H, Hu Y, Wolfswinkel JCv, Igarashi KJ, Bellott DW, Nefedov M, Reddien PW, Enders GC, Uversky VN, Mello CC, Page DC. Author response: A widely employed germ cell marker is an ancient disordered protein with reproductive functions in diverse eukaryotes Elife. DOI: 10.7554/Elife.19993.029  0.406
2016 Fonin AV, Uversky VN, Kuznetsova IM, Turoverov KK. Protein folding and stability in the presence of osmolytes Biophysics. 61: 185-192. DOI: 10.1134/S0006350916020056  0.433
2016 Stojanovski B, Breydo L, Uversky VN, Ferreira GC. Macromolecular crowders and osmolytes modulate the structural and catalytic properties of alkaline molten globular 5-aminolevulinate synthase Rsc Advances. 6: 114541-114552. DOI: 10.1039/C6Ra22533K  0.629
2016 Sales AE, Breydo L, Porto TS, Porto ALF, Uversky VN. Hydrophobicity-dependent effects of polymers on different protein conformations Rsc Advances. 6: 42971-42983. DOI: 10.1039/C6Ra07910E  0.688
2016 DeForte S, Uversky VN. Intrinsically disordered proteins in PubMed: what can the tip of the iceberg tell us about what lies below? Rsc Advances. 6: 11513-11521. DOI: 10.1039/C5Ra24866C  0.823
2016 Dezfooli SM, Uversky VN, Saleem M, Baharudin FS, Hitam SMS, Bachmann RT. A simplified method for the purification of an intrinsically disordered coagulant protein from defatted Moringa oleifera seeds Process Biochemistry. 51: 1085-1091. DOI: 10.1016/J.Procbio.2016.04.021  0.402
2016 Uversky VN. (Intrinsically disordered) splice variants in the proteome: implications for novel drug discovery Genes & Genomics. 38: 577-594. DOI: 10.1007/S13258-015-0384-0  0.418
2015 Frege T, Uversky VN. Intrinsically disordered proteins in the nucleus of human cells. Biochemistry and Biophysics Reports. 1: 33-51. PMID 29124132 DOI: 10.1016/J.Bbrep.2015.03.003  0.453
2015 DeForte S, Reddy KD, Uversky VN. Digested disorder, Quarterly intrinsic disorder digest (October-November-December, 2013). Intrinsically Disordered Proteins. 3: e984569. PMID 28293487 DOI: 10.4161/21690707.2014.984569  0.808
2015 Uversky VN. The intrinsic disorder alphabet. III. Dual personality of serine. Intrinsically Disordered Proteins. 3: e1027032. PMID 28232888 DOI: 10.1080/21690707.2015.1027032  0.324
2015 Uversky VN. Unreported intrinsic disorder in proteins: Disorder emergency room. Intrinsically Disordered Proteins. 3: e1010999. PMID 28232885 DOI: 10.1080/21690707.2015.1010999  0.352
2015 Meng F, Na I, Kurgan L, Uversky VN. Compartmentalization and Functionality of Nuclear Disorder: Intrinsic Disorder and Protein-Protein Interactions in Intra-Nuclear Compartments. International Journal of Molecular Sciences. 17. PMID 26712748 DOI: 10.3390/Ijms17010024  0.808
2015 Breydo L, Newland B, Zhang H, Rosser A, Werner C, Uversky VN, Wang W. A hyperbranched dopamine-containing PEG-based polymer for the inhibition of α-synuclein fibrillation. Biochemical and Biophysical Research Communications. PMID 26707645 DOI: 10.1016/J.Bbrc.2015.12.060  0.634
2015 Yan J, Dunker AK, Uversky VN, Kurgan L. Molecular recognition features (MoRFs) in three domains of life. Molecular Biosystems. PMID 26651072 DOI: 10.1039/C5Mb00640F  0.494
2015 da Silva NR, Ferreira LA, Madeira PP, Teixeira JA, Uversky VN, Zaslavsky BY. Effect of sodium chloride on solute-solvent interactions in aqueous polyethylene glycol-sodium sulfate two-phase systems. Journal of Chromatography. A. PMID 26615710 DOI: 10.1016/J.Chroma.2015.11.019  0.305
2015 Zaslavsky BY, Uversky VN, Chait A. Solvent interaction analysis as a proteomic approach to structure-based biomarker discovery and clinical diagnostics. Expert Review of Proteomics. 13: 9-17. PMID 26558960 DOI: 10.1586/14789450.2016.1116945  0.444
2015 Stepanenko OV, Povarova OI, Sulatskaya AI, Ferreira LA, Zaslavsky BY, Kuznetsova IM, Turioverov KK, Uversky VN. Protein unfolding in crowded milieu: What crowding can do to a protein undergoing unfolding? Journal of Biomolecular Structure & Dynamics. 1-0. PMID 26474212 DOI: 10.1080/07391102.2015.1109554  0.728
2015 Permyakov SE, Permyakov EA, Uversky VN. Intrinsically disordered caldesmon binds calmodulin via the "buttons on a string" mechanism. Peerj. 3: e1265. PMID 26417545 DOI: 10.7717/Peerj.1265  0.36
2015 Uversky VN. Biophysical Methods to Investigate Intrinsically Disordered Proteins: Avoiding an "Elephant and Blind Men" Situation. Advances in Experimental Medicine and Biology. 870: 215-60. PMID 26387104 DOI: 10.1007/978-3-319-20164-1_7  0.49
2015 da Silva NR, Ferreira LA, Madeira PP, Teixeira JA, Uversky VN, Zaslavsky BY. Analysis of partitioning of organic compounds and proteins in aqueous polyethylene glycol-sodium sulfate aqueous two-phase systems in terms of solute-solvent interactions. Journal of Chromatography. A. 1415: 1-10. PMID 26342872 DOI: 10.1016/J.Chroma.2015.08.053  0.319
2015 Uversky VN. Pliability of protein complexes and complexity of protein pliability. Febs Letters. 589: 2431-2432. PMID 26325593 DOI: 10.1016/J.Febslet.2015.08.035  0.362
2015 Fratz EJ, Clayton J, Hunter GA, Ducamp S, Breydo L, Uversky VN, Deybach JC, Gouya L, Puy H, Ferreira GC. Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release. Biochemistry. 54: 5617-31. PMID 26300302 DOI: 10.1021/Acs.Biochem.5B00407  0.651
2015 Wu Z, Hu G, Yang J, Peng Z, Uversky VN, Kurgan L. In various protein complexes, disordered protomers have large per-residue surface areas and area of protein-, DNA- and RNA-binding interfaces. Febs Letters. 589: 2561-9. PMID 26297830 DOI: 10.1016/J.Febslet.2015.08.014  0.458
2015 Huang F, Oldfield CJ, Xue B, Hsu WL, Meng J, Liu X, Shen L, Romero P, Uversky VN, Dunker AK. Erratum to: Improving protein order-disorder classification using charge-hydropathy plots. Bmc Bioinformatics. 16: 241. PMID 26227315 DOI: 10.1186/S12859-015-0646-5  0.322
2015 Hu G, Wu Z, Wang K, Uversky VN, Kurgan L. Untapped potential of disordered proteins in current druggable human proteome. Current Drug Targets. PMID 26201486 DOI: 10.2174/1389450116666150722141119  0.44
2015 Breydo L, Uversky VN. Structural, morphological, and functional diversity of amyloid oligomers. Febs Letters. 589: 2640-8. PMID 26188543 DOI: 10.1016/J.Febslet.2015.07.013  0.692
2015 El-Baky NA, Uversky VN, Redwan EM. Human consensus interferons: Bridging the natural and artificial cytokines with intrinsic disorder. Cytokine & Growth Factor Reviews. 26: 637-45. PMID 26169931 DOI: 10.1016/J.Cytogfr.2015.07.012  0.373
2015 Uversky VN. Protein Misfolding in Lipid-Mimetic Environments. Advances in Experimental Medicine and Biology. 855: 33-66. PMID 26149925 DOI: 10.1007/978-3-319-17344-3_2  0.368
2015 Meng F, Badierah RA, Almehdar HA, Redwan EM, Kurgan L, Uversky VN. Unstructural biology of the dengue virus proteins. The Febs Journal. PMID 26096987 DOI: 10.1111/Febs.13349  0.441
2015 Petrovich A, Borne A, Uversky VN, Xue B. Identifying Similar Patterns of Structural Flexibility in Proteins by Disorder Prediction and Dynamic Programming. International Journal of Molecular Sciences. 16: 13829-49. PMID 26086829 DOI: 10.3390/Ijms160613829  0.43
2015 Goh GK, Dunker AK, Uversky VN. Detection of links between Ebola nucleocapsid and virulence using disorder analysis. Molecular Biosystems. 11: 2337-44. PMID 26086270 DOI: 10.1039/C5Mb00240K  0.394
2015 Goh GK, Dunker AK, Uversky VN. Shell disorder, immune evasion and transmission behaviors among human and animal retroviruses. Molecular Biosystems. 11: 2312-23. PMID 26080321 DOI: 10.1039/C5Mb00277J  0.355
2015 Uversky VN. The multifaceted roles of intrinsic disorder in protein complexes. Febs Letters. 589: 2498-506. PMID 26073257 DOI: 10.1016/J.Febslet.2015.06.004  0.455
2015 Breydo L, Sales AE, Frege T, Howell MC, Zaslavsky BY, Uversky VN. Effects of Polymer Hydrophobicity on Protein Structure and Aggregation Kinetics in Crowded Milieu. Biochemistry. 54: 2957-66. PMID 25919930 DOI: 10.1021/Acs.Biochem.5B00116  0.716
2015 Breydo L, Morgan D, Uversky VN. Pseudocatalytic Antiaggregation Activity of Antibodies: Immunoglobulins can Influence α-Synuclein Aggregation at Substoichiometric Concentrations. Molecular Neurobiology. PMID 25833100 DOI: 10.1007/S12035-015-9148-8  0.658
2015 Uversky VN. Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders. Frontiers in Aging Neuroscience. 7: 18. PMID 25784874 DOI: 10.3389/Fnagi.2015.00018  0.344
2015 Sluchanko NN, Uversky VN. Hidden disorder propensity of the N-terminal segment of universal adapter protein 14-3-3 is manifested in its monomeric form: Novel insights into protein dimerization and multifunctionality. Biochimica Et Biophysica Acta. 1854: 492-504. PMID 25747569 DOI: 10.1016/J.Bbapap.2015.02.017  0.514
2015 Redwan EM, Xue B, Almehdar HA, Uversky VN. Disorder in milk proteins: caseins, intrinsically disordered colloids. Current Protein & Peptide Science. 16: 228-42. PMID 25714333 DOI: 10.2174/1389203716666150224145900  0.46
2015 Breydo L, Sales AE, Ferreira L, Fedotoff O, Shevelyova MP, Permyakov SE, Kroeck KG, Permyakov EA, Zaslavsky BY, Uversky VN. Effects of osmolytes on protein-solvent interactions in crowded environment: Analyzing the effect of TMAO on proteins in crowded solutions. Archives of Biochemistry and Biophysics. 570: 66-74. PMID 25712220 DOI: 10.1016/J.Abb.2015.02.021  0.704
2015 Ferreira LA, Madeira PP, Uversky AV, Uversky VN, Zaslavsky BY. Responses of proteins to different ionic environment are linearly interrelated. Journal of Chromatography. A. 1387: 32-41. PMID 25708470 DOI: 10.1016/J.Chroma.2015.02.006  0.443
2015 Polanco C, Samaniego JL, Uversky VN, Castañón-González JA, Buhse T, Leopold-Sordo M, Madero-Arteaga A, Morales-Reyes A, Tavera-Sierra L, González-Bernal JA, Arias-Estrada M. Identification of proteins associated with amyloidosis by polarity index method. Acta Biochimica Polonica. 62: 41-55. PMID 25669158 DOI: 10.18388/Abp.2014_755  0.445
2015 Uversky VN. Functional roles of transiently and intrinsically disordered regions within proteins Febs Journal. 282: 1182-1189. PMID 25631540 DOI: 10.1111/Febs.13202  0.517
2015 Ferreira LA, Madeira PP, Breydo L, Reichardt C, Uversky VN, Zaslavsky BY. Role of solvent properties of aqueous media in macromolecular crowding effects. Journal of Biomolecular Structure & Dynamics. 1-12. PMID 25616385 DOI: 10.1080/07391102.2015.1011235  0.633
2015 Lopes FC, Dobrovolska O, Real-Guerra R, Broll V, Zambelli B, Musiani F, Uversky VN, Carlini CR, Ciurli S. Pliable natural biocide: Jaburetox is an intrinsically disordered insecticidal and fungicidal polypeptide derived from jack bean urease Febs Journal. 282: 1043-1064. PMID 25605001 DOI: 10.1111/Febs.13201  0.446
2015 Kuznetsova IM, Zaslavsky BY, Breydo L, Turoverov KK, Uversky VN. Beyond the excluded volume effects: mechanistic complexity of the crowded milieu. Molecules (Basel, Switzerland). 20: 1377-409. PMID 25594347 DOI: 10.3390/Molecules20011377  0.709
2015 Malaney P, Uversky VN, Davé V. Identification of intrinsically disordered regions in PTEN and delineation of its function via a network approach. Methods (San Diego, Calif.). 77: 69-74. PMID 25449897 DOI: 10.1016/J.Ymeth.2014.10.005  0.491
2015 Uversky VN, Kuznetsova IM, Turoverov KK, Zaslavsky B. Intrinsically disordered proteins as crucial constituents of cellular aqueous two phase systems and coacervates. Febs Letters. 589: 15-22. PMID 25436423 DOI: 10.1016/J.Febslet.2014.11.028  0.364
2015 Dolan PT, Roth AP, Xue B, Sun R, Dunker AK, Uversky VN, LaCount DJ. Intrinsic disorder mediates hepatitis C virus core-host cell protein interactions. Protein Science : a Publication of the Protein Society. 24: 221-35. PMID 25424537 DOI: 10.1002/Pro.2608  0.42
2015 Uversky VN. Introduction to intrinsically disordered proteins (IDPs). Chemical Reviews. 114: 6557-60. PMID 25004990 DOI: 10.1021/Cr500288Y  0.46
2015 Peng Z, Yan J, Fan X, Mizianty MJ, Xue B, Wang K, Hu G, Uversky VN, Kurgan L. Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life. Cellular and Molecular Life Sciences : Cmls. 72: 137-51. PMID 24939692 DOI: 10.1007/S00018-014-1661-9  0.459
2015 Meng F, Na I, Kurgan L, Uversky VN. Compartmentalization and functionality of nuclear disorder: Intrinsic disorder and protein-protein interactions in intra-nuclear compartments International Journal of Molecular Sciences. 17. DOI: 10.3390/ijms17010024  0.799
2015 Ferreira LA, Fan X, Madeira PP, Kurgan L, Uversky VN, Zaslavsky BY. Analyzing the effects of protecting osmolytes on solute–water interactions by solvatochromic comparison method: II. Globular proteins Rsc Advances. 5: 59780-59791. DOI: 10.1039/C5Ra08612D  0.331
2015 Ferreira LA, Fedotoff O, Uversky VN, Zaslavsky BY. Effects of osmolytes on protein–solvent interactions in crowded environments: study of sucrose and trehalose effects on different proteins by solvent interaction analysis Rsc Advances. 5: 27154-27162. DOI: 10.1039/C5Ra02997J  0.369
2015 Reddy KD, Baker JD, Xue B, Deschenes RJ, Uversky VN. The Intrinsically Disordered Termini of zDHHC S-Palmitoyltransferases Facilitate Multiple Regulatory Functions Biophysical Journal. 108: 387a. DOI: 10.1016/J.Bpj.2014.11.2123  0.668
2014 Reddy KD, DeForte S, Uversky VN. Digested disorder: Quarterly intrinsic disorder digest (July-August-September, 2013). Intrinsically Disordered Proteins. 2: e27833. PMID 28232877 DOI: 10.4161/idp.27833  0.811
2014 Uversky VN. Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators. Frontiers in Molecular Biosciences. 1: 6. PMID 25988147 DOI: 10.3389/Fmolb.2014.00006  0.43
2014 Huang F, Oldfield CJ, Xue B, Hsu WL, Meng J, Liu X, Shen L, Romero P, Uversky VN, Dunker A. Improving protein order-disorder classification using charge-hydropathy plots. Bmc Bioinformatics. 15: S4. PMID 25559583 DOI: 10.1186/1471-2105-15-S17-S4  0.392
2014 Portillo A, Hashemi M, Zhang Y, Breydo L, Uversky VN, Lyubchenko YL. Role of monomer arrangement in the amyloid self-assembly. Biochimica Et Biophysica Acta. 1854: 218-28. PMID 25542374 DOI: 10.1016/J.Bbapap.2014.12.009  0.671
2014 Kuznetsova IM, Turoverov KK, Uversky VN. What macromolecular crowding can do to a protein. International Journal of Molecular Sciences. 15: 23090-140. PMID 25514413 DOI: 10.3390/Ijms151223090  0.442
2014 Uversky VN. Proteins without unique 3D structures: biotechnological applications of intrinsically unstable/disordered proteins. Biotechnology Journal. 10: 356-66. PMID 25287424 DOI: 10.1002/Biot.201400374  0.466
2014 Albar AH, Almehdar HA, Uversky VN, Redwan EM. Structural heterogeneity and multifunctionality of lactoferrin. Current Protein & Peptide Science. 15: 778-97. PMID 25245670 DOI: 10.2174/1389203715666140919124530  0.326
2014 Stojanovski BM, Breydo L, Hunter GA, Uversky VN, Ferreira GC. Catalytically active alkaline molten globular enzyme: Effect of pH and temperature on the structural integrity of 5-aminolevulinate synthase. Biochimica Et Biophysica Acta. 1844: 2145-2154. PMID 25240868 DOI: 10.1016/J.Bbapap.2014.09.013  0.624
2014 Kathiriya JJ, Pathak RR, Clayman E, Xue B, Uversky VN, Davé V. Presence and utility of intrinsically disordered regions in kinases Molecular Biosystems. 10: 2876-2888. PMID 25099472 DOI: 10.1039/C4Mb00224E  0.314
2014 Sun X, Greenwood DR, Templeton MD, Libich DS, McGhie TK, Xue B, Yoon M, Cui W, Kirk CA, Jones WT, Uversky VN, Rikkerink EH. The intrinsically disordered structural platform of the plant defence hub protein RPM1-interacting protein 4 provides insights into its mode of action in the host-pathogen interface and evolution of the nitrate-induced domain protein family. The Febs Journal. 281: 3955-79. PMID 25039985 DOI: 10.1111/Febs.12937  0.462
2014 Angelani CR, Curto LM, Cabanas IS, Caramelo JJ, Uversky VN, Delfino JM. Toward a common aggregation mechanism for a β-barrel protein family: insights derived from a stable dimeric species. Biochimica Et Biophysica Acta. 1844: 1599-607. PMID 24929115 DOI: 10.1016/J.Bbapap.2014.06.002  0.448
2014 Pejaver V, Hsu WL, Xin F, Dunker AK, Uversky VN, Radivojac P. The structural and functional signatures of proteins that undergo multiple events of post-translational modification. Protein Science : a Publication of the Protein Society. 23: 1077-93. PMID 24888500 DOI: 10.1002/Pro.2494  0.434
2014 Popelka H, Uversky VN, Klionsky DJ. Identification of Atg3 as an intrinsically disordered polypeptide yields insights into the molecular dynamics of autophagy-related proteins in yeast. Autophagy. 10: 1093-104. PMID 24879155 DOI: 10.4161/Auto.28616  0.499
2014 Kovacs GG, Breydo L, Green R, Kis V, Puska G, LÅ‘rincz P, Perju-Dumbrava L, Giera R, Pirker W, Lutz M, Lachmann I, Budka H, Uversky VN, Molnár K, László L. Intracellular processing of disease-associated α-synuclein in the human brain suggests prion-like cell-to-cell spread. Neurobiology of Disease. 69: 76-92. PMID 24878508 DOI: 10.1016/J.Nbd.2014.05.020  0.644
2014 Butler CL, Lucas O, Wuchty S, Xue B, Uversky VN, White M. Identifying novel cell cycle proteins in Apicomplexa parasites through co-expression decision analysis. Plos One. 9: e97625. PMID 24841368 DOI: 10.1371/Journal.Pone.0097625  0.378
2014 Uversky VN, Davé V, Iakoucheva LM, Malaney P, Metallo SJ, Pathak RR, Joerger AC. Pathological unfoldomics of uncontrolled chaos: Intrinsically disordered proteins and human diseases Chemical Reviews. 114: 6844-6879. PMID 24830552 DOI: 10.1021/Cr400713R  0.52
2014 van der Lee R, Buljan M, Lang B, Weatheritt RJ, Daughdrill GW, Dunker AK, Fuxreiter M, Gough J, Gsponer J, Jones DT, Kim PM, Kriwacki RW, Oldfield CJ, Pappu RV, Tompa P, ... Uversky VN, et al. Classification of intrinsically disordered regions and proteins. Chemical Reviews. 114: 6589-631. PMID 24773235 DOI: 10.1021/Cr400525M  0.4
2014 Fan X, Xue B, Dolan PT, LaCount DJ, Kurgan L, Uversky VN. The intrinsic disorder status of the human hepatitis C virus proteome. Molecular Biosystems. 10: 1345-63. PMID 24752801 DOI: 10.1039/C4Mb00027G  0.424
2014 Habchi J, Tompa P, Longhi S, Uversky VN. Introducing protein intrinsic disorder. Chemical Reviews. 114: 6561-88. PMID 24739139 DOI: 10.1021/Cr400514H  0.46
2014 Peng Z, Sakai Y, Kurgan L, Sokolowski B, Uversky V. Intrinsic disorder in the BK channel and its interactome. Plos One. 9: e94331. PMID 24727949 DOI: 10.1371/Journal.Pone.0094331  0.437
2014 Mizianty MJ, Uversky V, Kurgan L. Prediction of intrinsic disorder in proteins using MFDp2. Methods in Molecular Biology (Clifton, N.J.). 1137: 147-62. PMID 24573480 DOI: 10.1007/978-1-4939-0366-5_11  0.427
2014 Na I, Reddy KD, Breydo L, Xue B, Uversky VN. A putative role of the Sup35p C-terminal domain in the cytoskeleton organization during yeast mitosis. Molecular Biosystems. 10: 925-40. PMID 24549315 DOI: 10.1039/C3Mb70515C  0.809
2014 Jakob U, Kriwacki R, Uversky VN. Conditionally and transiently disordered proteins: Awakening cryptic disorder to regulate protein function Chemical Reviews. 114: 6779-6805. PMID 24502763 DOI: 10.1021/Cr400459C  0.459
2014 Ferreira L, Fan X, Mikheeva LM, Madeira PP, Kurgan L, Uversky VN, Zaslavsky BY. Structural features important for differences in protein partitioning in aqueous dextran-polyethylene glycol two-phase systems of different ionic compositions. Biochimica Et Biophysica Acta. 1844: 694-704. PMID 24486798 DOI: 10.1016/J.Bbapap.2014.01.016  0.444
2014 Uversky VN. The triple power of D³: protein intrinsic disorder in degenerative diseases. Frontiers in Bioscience (Landmark Edition). 19: 181-258. PMID 24389181 DOI: 10.2741/4204  0.455
2014 Lee C, Kalmar L, Xue B, Tompa P, Daughdrill GW, Uversky VN, Han KH. Contribution of proline to the pre-structuring tendency of transient helical secondary structure elements in intrinsically disordered proteins. Biochimica Et Biophysica Acta. 1840: 993-1003. PMID 24211251 DOI: 10.1016/J.Bbagen.2013.10.042  0.405
2014 Xue B, Uversky VN. Intrinsic disorder in proteins involved in the innate antiviral immunity: another flexible side of a molecular arms race. Journal of Molecular Biology. 426: 1322-50. PMID 24184279 DOI: 10.1016/J.Jmb.2013.10.030  0.419
2014 Varadi M, Kosol S, Lebrun P, Valentini E, Blackledge M, Dunker AK, Felli IC, Forman-Kay JD, Kriwacki RW, Pierattelli R, Sussman J, Svergun DI, Uversky VN, Vendruscolo M, Wishart D, et al. pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins. Nucleic Acids Research. 42: D326-35. PMID 24174539 DOI: 10.1093/Nar/Gkt960  0.419
2014 Malaney P, Uversky VN, Davé V. The PTEN Long N-tail is intrinsically disordered: increased viability for PTEN therapy. Molecular Biosystems. 9: 2877-88. PMID 24056727 DOI: 10.1039/C3Mb70267G  0.329
2014 Peng Z, Oldfield CJ, Xue B, Mizianty MJ, Dunker AK, Kurgan L, Uversky VN. A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome. Cellular and Molecular Life Sciences : Cmls. 71: 1477-504. PMID 23942625 DOI: 10.1007/S00018-013-1446-6  0.486
2014 Xue B, Ganti K, Rabionet A, Banks L, Uversky VN. Disordered interactome of human papillomavirus. Current Pharmaceutical Design. 20: 1274-92. PMID 23713779 DOI: 10.2174/13816128113199990072  0.412
2013 DeForte S, Reddy KD, Uversky VN. Digested disorder: Quarterly intrinsic disorder digest (April-May-June, 2013). Intrinsically Disordered Proteins. 1: e27454. PMID 28516028 DOI: 10.4161/idp.27454  0.811
2013 Uversky VN. Disorder in the lifetime of a protein. Intrinsically Disordered Proteins. 1: e26782. PMID 28516024 DOI: 10.4161/idp.26782  0.358
2013 Uversky VN. Hypothesis: The unfolding power of protein dielectricity. Intrinsically Disordered Proteins. 1: e25725. PMID 28516018 DOI: 10.4161/idp.25725  0.32
2013 Uversky VN. Digested disorder: Quarterly intrinsic disorder digest (January/February/March, 2013). Intrinsically Disordered Proteins. 1: e25496. PMID 28516015 DOI: 10.4161/idp.25496  0.311
2013 Uversky VN. The alphabet of intrinsic disorder: II. Various roles of glutamic acid in ordered and intrinsically disordered proteins. Intrinsically Disordered Proteins. 1: e24684. PMID 28516010 DOI: 10.4161/idp.24684  0.345
2013 Theillet FX, Kalmar L, Tompa P, Han KH, Selenko P, Dunker AK, Daughdrill GW, Uversky VN. The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins. Intrinsically Disordered Proteins. 1: e24360. PMID 28516008 DOI: 10.4161/idp.24360  0.346
2013 Dunker AK, Babu MM, Barbar E, Blackledge M, Bondos SE, Dosztányi Z, Dyson HJ, Forman-Kay J, Fuxreiter M, Gsponer J, Han KH, Jones DT, Longhi S, Metallo SJ, Nishikawa K, ... ... Uversky VN, et al. What's in a name? Why these proteins are intrinsically disordered: Why these proteins are intrinsically disordered. Intrinsically Disordered Proteins. 1: e24157. PMID 28516007 DOI: 10.4161/idp.24157  0.37
2013 Uversky AV, Xue B, Peng Z, Kurgan L, Uversky VN. On the intrinsic disorder status of the major players in programmed cell death pathways. F1000research. 2: 190. PMID 24358900 DOI: 10.12688/F1000Research.2-190.V1  0.419
2013 Goh GK, Dunker AK, Uversky V. Prediction of Intrinsic Disorder in MERS-CoV/HCoV-EMC Supports a High Oral-Fecal Transmission. Plos Currents. 5. PMID 24270586 DOI: 10.1371/Currents.Outbreaks.22254B58675Cdebc256Dbe3C5Aa6498B  0.344
2013 Breydo L, Reddy KD, Piai A, Felli IC, Pierattelli R, Uversky VN. The crowd you're in with: effects of different types of crowding agents on protein aggregation. Biochimica Et Biophysica Acta. 1844: 346-57. PMID 24252314 DOI: 10.1016/J.Bbapap.2013.11.004  0.777
2013 Breydo L, Mikheeva LM, Madeira PP, Zaslavsky BY, Uversky VN. Solvent interaction analysis of intrinsically disordered proteins in aqueous two-phase systems. Molecular Biosystems. 9: 3068-79. PMID 24072065 DOI: 10.1039/C3Mb70329K  0.694
2013 Marín M, Uversky VN, Ott T. Intrinsic disorder in pathogen effectors: protein flexibility as an evolutionary hallmark in a molecular arms race. The Plant Cell. 25: 3153-7. PMID 24038649 DOI: 10.1105/Tpc.113.116319  0.434
2013 Na I, Redmon D, Kopa M, Qin Y, Xue B, Uversky VN. Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology. Plos One. 8: e73476. PMID 24014171 DOI: 10.1371/Journal.Pone.0073476  0.821
2013 Blair LJ, Nordhues BA, Hill SE, Scaglione KM, O'Leary JC, Fontaine SN, Breydo L, Zhang B, Li P, Wang L, Cotman C, Paulson HL, Muschol M, Uversky VN, Klengel T, et al. Accelerated neurodegeneration through chaperone-mediated oligomerization of tau. The Journal of Clinical Investigation. 123: 4158-69. PMID 23999428 DOI: 10.1172/Jci69003  0.64
2013 Ferreira L, Madeira PP, Mikheeva L, Uversky VN, Zaslavsky B. Effect of salt additives on protein partition in polyethylene glycol-sodium sulfate aqueous two-phase systems. Biochimica Et Biophysica Acta. 1834: 2859-66. PMID 23920121 DOI: 10.1016/J.Bbapap.2013.07.014  0.406
2013 Uversky VN. The UBE2E proteins as conjugating dispersers: extending function with extended extensions. Journal of Molecular Biology. 425: 4067-70. PMID 23871835 DOI: 10.1016/J.Jmb.2013.07.024  0.476
2013 Shivu B, Seshadri S, Li J, Oberg KA, Uversky VN, Fink AL. Distinct β-sheet structure in protein aggregates determined by ATR-FTIR spectroscopy. Biochemistry. 52: 5176-83. PMID 23837615 DOI: 10.1021/Bi400625V  0.431
2013 Malaney P, Pathak RR, Xue B, Uversky VN, Davé V. Intrinsic disorder in PTEN and its interactome confers structural plasticity and functional versatility. Scientific Reports. 3: 2035. PMID 23783762 DOI: 10.1038/Srep02035  0.426
2013 Choi UB, Kazi R, Stenzoski N, Wollmuth LP, Uversky VN, Bowen ME. Modulating the intrinsic disorder in the cytoplasmic domain alters the biological activity of the N-methyl-D-aspartate-sensitive glutamate receptor. The Journal of Biological Chemistry. 288: 22506-15. PMID 23782697 DOI: 10.1074/Jbc.M113.477810  0.342
2013 Peng Z, Xue B, Kurgan L, Uversky VN. Resilience of death: intrinsic disorder in proteins involved in the programmed cell death. Cell Death and Differentiation. 20: 1257-67. PMID 23764774 DOI: 10.1038/Cdd.2013.65  0.444
2013 Yan J, Mizianty MJ, Filipow PL, Uversky VN, Kurgan L. RAPID: fast and accurate sequence-based prediction of intrinsic disorder content on proteomic scale. Biochimica Et Biophysica Acta. 1834: 1671-80. PMID 23732563 DOI: 10.1016/J.Bbapap.2013.05.022  0.395
2013 Uversky VN. The most important thing is the tail: multitudinous functionalities of intrinsically disordered protein termini. Febs Letters. 587: 1891-901. PMID 23665034 DOI: 10.1016/J.Febslet.2013.04.042  0.477
2013 Coelho Ribeiro Mde L, Espinosa J, Islam S, Martinez O, Thanki JJ, Mazariegos S, Nguyen T, Larina M, Xue B, Uversky VN. Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome. Peerj. 1: e2. PMID 23638354 DOI: 10.7717/Peerj.2  0.497
2013 Xue B, Romero PR, Noutsou M, Maurice MM, Rüdiger SG, William AM, Mizianty MJ, Kurgan L, Uversky VN, Dunker AK. Stochastic machines as a colocalization mechanism for scaffold protein function. Febs Letters. 587: 1587-91. PMID 23603389 DOI: 10.1016/J.Febslet.2013.04.006  0.369
2013 Uversky VN. A decade and a half of protein intrinsic disorder: biology still waits for physics. Protein Science : a Publication of the Protein Society. 22: 693-724. PMID 23553817 DOI: 10.1002/Pro.2261  0.478
2013 Kutyshenko VP, Prokhorov DA, Molochkov NV, Sharapov MG, Kolesnikov I, Uversky VN. Dancing retro: solution structure and micelle interactions of the retro-SH3-domain, retro-SHH-'Bergerac'. Journal of Biomolecular Structure & Dynamics. 32: 257-72. PMID 23527530 DOI: 10.1080/07391102.2012.762724  0.421
2013 Wood M, Rae GM, Wu RM, Walton EF, Xue B, Hellens RP, Uversky VN. Actinidia DRM1--an intrinsically disordered protein whose mRNA expression is inversely correlated with spring budbreak in kiwifruit. Plos One. 8: e57354. PMID 23516402 DOI: 10.1371/Journal.Pone.0057354  0.459
2013 Uversky VN. MultIDIMensionality of IDIMs: intrinsic disorder in autoinhibition. Structure (London, England : 1993). 21: 315-6. PMID 23473663 DOI: 10.1016/J.Str.2013.02.009  0.467
2013 Ortiz JF, MacDonald ML, Masterson P, Uversky VN, Siltberg-Liberles J. Rapid evolutionary dynamics of structural disorder as a potential driving force for biological divergence in flaviviruses Genome Biology and Evolution. 5: 504-513. PMID 23418179 DOI: 10.1093/Gbe/Evt026  0.461
2013 Xue B, Jeffers V, Sullivan WJ, Uversky VN. Protein intrinsic disorder in the acetylome of intracellular and extracellular Toxoplasma gondii. Molecular Biosystems. 9: 645-57. PMID 23403842 DOI: 10.1039/C3Mb25517D  0.435
2013 Sun X, Rikkerink EH, Jones WT, Uversky VN. Multifarious roles of intrinsic disorder in proteins illustrate its broad impact on plant biology. The Plant Cell. 25: 38-55. PMID 23362206 DOI: 10.1105/Tpc.112.106062  0.392
2013 Uversky VN, Dunker AK. The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure. F1000 Biology Reports. 5: 1. PMID 23361308 DOI: 10.3410/B5-1  0.4
2013 Xue B, Brown CJ, Dunker AK, Uversky VN. Intrinsically disordered regions of p53 family are highly diversified in evolution. Biochimica Et Biophysica Acta. 1834: 725-38. PMID 23352836 DOI: 10.1016/J.Bbapap.2013.01.012  0.397
2013 Jinwal UK, Akoury E, Abisambra JF, O'Leary JC, Thompson AD, Blair LJ, Jin Y, Bacon J, Nordhues BA, Cockman M, Zhang J, Li P, Zhang B, Borysov S, Uversky VN, et al. Imbalance of Hsp70 family variants fosters tau accumulation. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 27: 1450-9. PMID 23271055 DOI: 10.1096/Fj.12-220889  0.319
2013 Hsu WL, Oldfield CJ, Xue B, Meng J, Huang F, Romero P, Uversky VN, Dunker AK. Exploring the binding diversity of intrinsically disordered proteins involved in one-to-many binding. Protein Science : a Publication of the Protein Society. 22: 258-73. PMID 23233352 DOI: 10.1002/Pro.2207  0.44
2013 Oldfield CJ, Xue B, Van YY, Ulrich EL, Markley JL, Dunker AK, Uversky VN. Utilization of protein intrinsic disorder knowledge in structural proteomics. Biochimica Et Biophysica Acta. 1834: 487-98. PMID 23232152 DOI: 10.1016/J.Bbapap.2012.12.003  0.47
2013 Oates ME, Romero P, Ishida T, Ghalwash M, Mizianty MJ, Xue B, Dosztányi Z, Uversky VN, Obradovic Z, Kurgan L, Dunker AK, Gough J. D²P²: database of disordered protein predictions. Nucleic Acids Research. 41: D508-16. PMID 23203878 DOI: 10.1093/Nar/Gks1226  0.405
2013 Zaslavsky A, Madeira P, Breydo L, Uversky VN, Chait A, Zaslavsky B. High throughput characterization of structural differences between closely related proteins in solution. Biochimica Et Biophysica Acta. 1834: 583-92. PMID 23174655 DOI: 10.1016/J.Bbapap.2012.11.004  0.704
2013 Uversky VN. Intrinsic disorder-based protein interactions and their modulators. Current Pharmaceutical Design. 19: 4191-213. PMID 23170892 DOI: 10.2174/1381612811319230005  0.471
2013 Silva BA, Breydo L, Uversky VN. Targeting the chameleon: a focused look at α-synuclein and its roles in neurodegeneration. Molecular Neurobiology. 47: 446-59. PMID 22940885 DOI: 10.1007/S12035-012-8334-1  0.599
2013 Silva BA, Breydo L, Fink AL, Uversky VN. Agrochemicals, α-synuclein, and Parkinson's disease. Molecular Neurobiology. 47: 598-612. PMID 22933040 DOI: 10.1007/S12035-012-8333-2  0.665
2013 Blair L, Nordhues B, Hill S, Scaglione KM, O'Leary J, Breydo L, Bo Z, Li P, Wang L, Cotman C, Paulson H, Muschol M, Uversky V, Klengel T, Binder E, et al. The Hsp90 co-chaperone FKBP51 produces neurotoxic tau oligomers: Implication for aging and Alzheimer's disease Alzheimers & Dementia. 9: 173. DOI: 10.1016/J.Jalz.2013.05.279  0.612
2012 Uversky VN. Unusual biophysics of intrinsically disordered proteins. Biochimica Et Biophysica Acta. 1834: 932-51. PMID 23269364 DOI: 10.1016/J.Bbapap.2012.12.008  0.52
2012 Kirilyuk A, Shimoji M, Catania J, Sahu G, Pattabiraman N, Giordano A, Albanese C, Mocchetti I, Toretsky JA, Uversky VN, Avantaggiati ML. An intrinsically disordered region of the acetyltransferase p300 with similarity to prion-like domains plays a role in aggregation. Plos One. 7: e48243. PMID 23133622 DOI: 10.1371/Journal.Pone.0048243  0.44
2012 Goh GK, Dunker AK, Uversky VN. Understanding Viral Transmission Behavior via Protein Intrinsic Disorder Prediction: Coronaviruses. Journal of Pathogens. 2012: 738590. PMID 23097708 DOI: 10.1155/2012/738590  0.313
2012 Vacic V, Markwick PR, Oldfield CJ, Zhao X, Haynes C, Uversky VN, Iakoucheva LM. Disease-associated mutations disrupt functionally important regions of intrinsic protein disorder. Plos Computational Biology. 8: e1002709. PMID 23055912 DOI: 10.1371/Journal.Pcbi.1002709  0.368
2012 Santner AA, Croy CH, Vasanwala FH, Uversky VN, Van YY, Dunker AK. Sweeping away protein aggregation with entropic bristles: intrinsically disordered protein fusions enhance soluble expression. Biochemistry. 51: 7250-62. PMID 22924672 DOI: 10.1021/Bi300653M  0.496
2012 Neyroz P, Ciurli S, Uversky VN. Denaturant-induced conformational transitions in intrinsically disordered proteins Methods in Molecular Biology. 896: 197-213. PMID 22821525 DOI: 10.1007/978-1-4614-3704-8_12  0.437
2012 Uversky VN. Size-exclusion chromatography in structural analysis of intrinsically disordered proteins. Methods in Molecular Biology (Clifton, N.J.). 896: 179-94. PMID 22821524 DOI: 10.1007/978-1-4614-3704-8_11  0.445
2012 Sulatskaya AI, Povarova OI, Kuznetsova IM, Uversky VN, Turoverov KK. Binding stoichiometry and affinity of fluorescent dyes to proteins in different structural states. Methods in Molecular Biology (Clifton, N.J.). 895: 441-60. PMID 22760333 DOI: 10.1007/978-1-61779-927-3_26  0.333
2012 Xue B, Dunker AK, Uversky VN. Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life. Journal of Biomolecular Structure & Dynamics. 30: 137-49. PMID 22702725 DOI: 10.1080/07391102.2012.675145  0.424
2012 Disfani FM, Hsu WL, Mizianty MJ, Oldfield CJ, Xue B, Dunker AK, Uversky VN, Kurgan L. MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins. Bioinformatics (Oxford, England). 28: i75-83. PMID 22689782 DOI: 10.1093/Bioinformatics/Bts209  0.379
2012 Hervás R, Oroz J, Galera-Prat A, Goñi O, Valbuena A, Vera AM, Gómez-Sicilia A, Losada-Urzáiz F, Uversky VN, Menéndez M, Laurents DV, Bruix M, Carrión-Vázquez M. Common features at the start of the neurodegeneration cascade. Plos Biology. 10: e1001335. PMID 22666178 DOI: 10.1371/Journal.Pbio.1001335  0.41
2012 Johnson DE, Xue B, Sickmeier MD, Meng J, Cortese MS, Oldfield CJ, Le Gall T, Dunker AK, Uversky VN. High-throughput characterization of intrinsic disorder in proteins from the Protein Structure Initiative. Journal of Structural Biology. 180: 201-15. PMID 22651963 DOI: 10.1016/J.Jsb.2012.05.013  0.483
2012 Kuznetsova IM, Sulatskaya AI, Uversky VN, Turoverov KK. A new trend in the experimental methodology for the analysis of the thioflavin T binding to amyloid fibrils. Molecular Neurobiology. 45: 488-98. PMID 22592269 DOI: 10.1007/S12035-012-8272-Y  0.321
2012 Uversky VN. Intrinsically disordered proteins and novel strategies for drug discovery. Expert Opinion On Drug Discovery. 7: 475-88. PMID 22559227 DOI: 10.1517/17460441.2012.686489  0.491
2012 Ahmadi Adl A, Nowzari-Dalini A, Xue B, Uversky VN, Qian X. Accurate prediction of protein structural classes using functional domains and predicted secondary structure sequences. Journal of Biomolecular Structure & Dynamics. 29: 623-33. PMID 22545993 DOI: 10.1080/07391102.2011.672626  0.38
2012 Peng Z, Mizianty MJ, Xue B, Kurgan L, Uversky VN. More than just tails: intrinsic disorder in histone proteins. Molecular Biosystems. 8: 1886-901. PMID 22543956 DOI: 10.1039/C2Mb25102G  0.465
2012 Xu K, Uversky VN, Xue B. Local flexibility facilitates oxidization of buried methionine residues. Protein and Peptide Letters. 19: 688-97. PMID 22519542 DOI: 10.2174/092986612800494084  0.305
2012 Sikirzhytski V, Topilina NI, Takor GA, Higashiya S, Welch JT, Uversky VN, Lednev IK. Fibrillation mechanism of a model intrinsically disordered protein revealed by 2D correlation deep UV resonance Raman spectroscopy. Biomacromolecules. 13: 1503-9. PMID 22515261 DOI: 10.1021/Bm300193F  0.439
2012 Singh VK, Rahman MN, Munro K, Uversky VN, Smith SP, Jia Z. Free cysteine modulates the conformation of human C/EBP homologous protein. Plos One. 7: e34680. PMID 22496840 DOI: 10.1371/Journal.Pone.0034680  0.454
2012 Uversky VN. Editorial [Hot Topic: Intrinsically Disordered Proteins: A Focused Look at Fuzzy Subjects (Guest Editor: Vladimir N. Uversky)] Current Protein & Peptide Science. 13: 2-5. PMID 22455660 DOI: 10.2174/138920312799278018  0.365
2012 Tipparaju SM, Li XP, Kilfoil PJ, Xue B, Uversky VN, Bhatnagar A, Barski OA. Interactions between the C-terminus of Kv1.5 and Kvβ regulate pyridine nucleotide-dependent changes in channel gating. PflüGers Archiv : European Journal of Physiology. 463: 799-818. PMID 22426702 DOI: 10.1007/S00424-012-1093-Z  0.331
2012 Kuznetsova IM, Sulatskaya AI, Uversky VN, Turoverov KK. Analyzing thioflavin T binding to amyloid fibrils by an equilibrium microdialysis-based technique. Plos One. 7: e30724. PMID 22383971 DOI: 10.1371/Journal.Pone.0030724  0.313
2012 Uversky VN. Disordered competitive recruiter: fast and foldable. Journal of Molecular Biology. 418: 267-8. PMID 22381408 DOI: 10.1016/J.Jmb.2012.02.034  0.337
2012 Fedotoff O, Mikheeva LM, Chait A, Uversky VN, Zaslavsky BY. Influence of serum proteins on conformation of prostate-specific antigen. Journal of Biomolecular Structure & Dynamics. 29: 1051-64. PMID 22292959 DOI: 10.1080/073911012010525030  0.453
2012 Xue B, Dunker AK, Uversky VN. The roles of intrinsic disorder in orchestrating the Wnt-pathway. Journal of Biomolecular Structure & Dynamics. 29: 843-61. PMID 22292947 DOI: 10.1080/073911012010525024  0.439
2012 Uversky VN, Dunker AK. Multiparametric analysis of intrinsically disordered proteins: looking at intrinsic disorder through compound eyes. Analytical Chemistry. 84: 2096-104. PMID 22242801 DOI: 10.1021/Ac203096K  0.459
2012 Ahmad A, Burns CS, Fink AL, Uversky VN. Peculiarities of copper binding to alpha-synuclein. Journal of Biomolecular Structure & Dynamics. 29: 825-42. PMID 22208282 DOI: 10.1080/073911012010525023  0.316
2012 Zhang T, Faraggi E, Xue B, Dunker AK, Uversky VN, Zhou Y. SPINE-D: accurate prediction of short and long disordered regions by a single neural-network based method. Journal of Biomolecular Structure & Dynamics. 29: 799-813. PMID 22208280 DOI: 10.1080/073911012010525022  0.378
2012 Huang F, Oldfield C, Meng J, Hsu WL, Xue B, Uversky VN, Romero P, Dunker AK. Subclassifying disordered proteins by the CH-CDF plot method. Pacific Symposium On Biocomputing. Pacific Symposium On Biocomputing. 128-39. PMID 22174269 DOI: 10.7490/F1000Research.1089774.1  0.386
2012 Hsu WL, Oldfield C, Meng J, Huang F, Xue B, Uversky VN, Romero P, Dunker AK. Intrinsic protein disorder and protein-protein interactions. Pacific Symposium On Biocomputing. Pacific Symposium On Biocomputing. 116-27. PMID 22174268 DOI: 10.7490/F1000Research.1090909.1  0.451
2012 Uversky VN, Santambrogio C, Brocca S, Grandori R. Length-dependent compaction of intrinsically disordered proteins. Febs Letters. 586: 70-3. PMID 22138473 DOI: 10.1016/J.Febslet.2011.11.026  0.367
2012 Westerheide SD, Raynes R, Powell C, Xue B, Uversky VN. HSF transcription factor family, heat shock response, and protein intrinsic disorder. Current Protein & Peptide Science. 13: 86-103. PMID 22044151 DOI: 10.2174/138920312799277956  0.358
2012 Breydo L, Wu JW, Uversky VN. Α-synuclein misfolding and Parkinson's disease. Biochimica Et Biophysica Acta. 1822: 261-85. PMID 22024360 DOI: 10.1016/J.Bbadis.2011.10.002  0.668
2012 Zambelli B, Cremades N, Neyroz P, Turano P, Uversky VN, Ciurli S. Insights in the (un)structural organization of Bacillus pasteurii UreG, an intrinsically disordered GTPase enzyme Molecular Biosystems. 8: 220-228. PMID 21922108 DOI: 10.1039/C1Mb05227F  0.448
2012 Xue B, Oldfield CJ, Van YY, Dunker AK, Uversky VN. Protein intrinsic disorder and induced pluripotent stem cells. Molecular Biosystems. 8: 134-50. PMID 21761058 DOI: 10.1039/C1Mb05163F  0.391
2012 Oates M, Romero P, Ishida T, Ghalwash M, Uversky V, Xue B, Obradovic Z, Dunker K, Gough J. A community resource for analysis and understanding of intrinsic disorder in proteins of fully sequenced genomes F1000research. 3. DOI: 10.7490/F1000Research.1092160.1  0.351
2012 Zambelli B, Cremades N, Neyroz P, Turano P, Uversky V, Ciurli S. The conformational flexibility of UreG, an intrinsically disordered GTPase enzyme F1000research. 3. DOI: 10.7490/F1000Research.1090033.1  0.341
2012 HOWELL M, GREEN R, KILLEEN A, WEDDERBURN L, PICASCIO V, RABIONET A, PENG Z, LARINA M, XUE B, KURGAN L, UVERSKY VN. NOT THAT RIGID MIDGETS AND NOT SO FLEXIBLE GIANTS: ON THE ABUNDANCE AND ROLES OF INTRINSIC DISORDER IN SHORT AND LONG PROTEINS Journal of Biological Systems. 20: 471-511. DOI: 10.1142/S0218339012400086  0.471
2012 Hervás R, Oroz J, Galera A, Goñi O, Valbuena A, Vera AM, Gómez-Sicilia A, Uversky VN, Menéndez M, Laurents DV, Bruix M, Carrión-Vázquez M. The Nanomechanics of Neurotoxic Proteins Reveals Common Features at the Start of the Neurodegeneration Cascade Biophysical Journal. 102: 633a. DOI: 10.1016/J.Bpj.2011.11.3448  0.426
2012 Rexach M, Colvin M, Gopinathan A, Krishnan K, Lau E, Newsam S, Phillips J, Uversky V, Yamada J. Sorting with Disorder at Nuclear Pores Biophysical Journal. 102: 2a. DOI: 10.1016/J.Bpj.2011.11.024  0.424
2011 Xue B, Mizianty MJ, Kurgan L, Uversky VN. Protein intrinsic disorder as a flexible armor and a weapon of HIV-1. Cellular and Molecular Life Sciences : Cmls. 69: 1211-59. PMID 22033837 DOI: 10.1007/S00018-011-0859-3  0.462
2011 Peysselon F, Xue B, Uversky VN, Ricard-Blum S. Intrinsic disorder of the extracellular matrix. Molecular Biosystems. 7: 3353-65. PMID 22009114 DOI: 10.1039/C1Mb05316G  0.442
2011 Breydo L, Uversky VN. Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases. Metallomics : Integrated Biometal Science. 3: 1163-80. PMID 21869995 DOI: 10.1039/C1Mt00106J  0.701
2011 Melnik TN, Povarnitsyna TV, Glukhov AS, Uversky VN, Melnik BS. Sequential melting of two hydrophobic clusters within the green fluorescent protein GFP-cycle3. Biochemistry. 50: 7735-44. PMID 21823681 DOI: 10.1021/Bi2006674  0.333
2011 Melnik BS, Molochkov NV, Prokhorov DA, Uversky VN, Kutyshenko VP. Molecular mechanisms of the anomalous thermal aggregation of green fluorescent protein. Biochimica Et Biophysica Acta. 1814: 1930-9. PMID 21816236 DOI: 10.1016/J.Bbapap.2011.07.017  0.386
2011 Xue B, Soeria-Atmadja D, Gustafsson MG, Hammerling U, Dunker AK, Uversky VN. Abundance and functional roles of intrinsic disorder in allergenic proteins and allergen representative peptides. Proteins. 79: 2595-606. PMID 21732419 DOI: 10.1002/Prot.23077  0.461
2011 Sun X, Xue B, Jones WT, Rikkerink E, Dunker AK, Uversky VN. A functionally required unfoldome from the plant kingdom: intrinsically disordered N-terminal domains of GRAS proteins are involved in molecular recognition during plant development. Plant Molecular Biology. 77: 205-23. PMID 21732203 DOI: 10.1007/S11103-011-9803-Z  0.431
2011 Mizianty MJ, Zhang T, Xue B, Zhou Y, Dunker AK, Uversky VN, Kurgan L. In-silico prediction of disorder content using hybrid sequence representation. Bmc Bioinformatics. 12: 245. PMID 21682902 DOI: 10.1186/1471-2105-12-245  0.416
2011 Uversky VN, Shah SP, Gritsyna Y, Hitchcock-DeGregori SE, Kostyukova AS. Systematic analysis of tropomodulin/tropomyosin interactions uncovers fine-tuned binding specificity of intrinsically disordered proteins. Journal of Molecular Recognition : Jmr. 24: 647-55. PMID 21584876 DOI: 10.1002/Jmr.1093  0.389
2011 Permyakov SE, Ismailov RG, Xue B, Denesyuk AI, Uversky VN, Permyakov EA. Intrinsic disorder in S100 proteins. Molecular Biosystems. 7: 2164-80. PMID 21528128 DOI: 10.1039/C0Mb00305K  0.464
2011 Uversky VN. Intrinsically disordered proteins from A to Z. The International Journal of Biochemistry & Cell Biology. 43: 1090-103. PMID 21501695 DOI: 10.1016/J.Biocel.2011.04.001  0.451
2011 Uversky VN. Intrinsically disordered proteins may escape unwanted interactions via functional misfolding. Biochimica Et Biophysica Acta. 1814: 693-712. PMID 21440685 DOI: 10.1016/J.Bbapap.2011.03.010  0.401
2011 Rochman M, Taher L, Kurahashi T, Cherukuri S, Uversky VN, Landsman D, Ovcharenko I, Bustin M. Effects of HMGN variants on the cellular transcription profile. Nucleic Acids Research. 39: 4076-87. PMID 21278158 DOI: 10.1093/Nar/Gkq1343  0.387
2011 Dixon SE, Bhatti MM, Uversky VN, Dunker AK, Sullivan WJ. Regions of intrinsic disorder help identify a novel nuclear localization signal in Toxoplasma gondii histone acetyltransferase TgGCN5-B. Molecular and Biochemical Parasitology. 175: 192-5. PMID 21055425 DOI: 10.1016/J.Molbiopara.2010.10.009  0.351
2011 Hong DP, Han S, Fink AL, Uversky VN. Characterization of the non-fibrillar α-synuclein oligomers. Protein and Peptide Letters. 18: 230-40. PMID 20858207 DOI: 10.2174/092986611794578332  0.406
2011 Uversky VN. Seven lessons from one IDP structural analysis. Structure (London, England : 1993). 18: 1069-71. PMID 20826332 DOI: 10.1016/J.Str.2010.08.003  0.404
2011 Xue B, Dunker AK, Uversky VN. Prediction of intrinsic disorder: From general to specific F1000research. 2. DOI: 10.7490/F1000Research.764.1  0.321
2011 Hsu W, Oldfield CJ, Xue B, Wagle M, Meng J, Huang F, Morales C, Uversky VN, Dunker AK. Exploring the binding diversity of intrinsically disordered proteins F1000research. 2. DOI: 10.7490/F1000Research.2156.1  0.438
2011 Williams RW, Xue B, Uversky V, Dunker AK. Natural Selection of 100% Intrinsically Disordered Biologically Functional Disease Related Pfam Protein Domains Biophysical Journal. 100: 62a. DOI: 10.1016/J.Bpj.2010.12.537  0.391
2010 Xue B, Dunker AK, Uversky VN. Retro-MoRFs: identifying protein binding sites by normal and reverse alignment and intrinsic disorder prediction. International Journal of Molecular Sciences. 11: 3725-47. PMID 21152297 DOI: 10.3390/Ijms11103725  0.464
2010 Uversky VN. Flexible nets of malleable guardians: intrinsically disordered chaperones in neurodegenerative diseases. Chemical Reviews. 111: 1134-66. PMID 21086986 DOI: 10.1021/Cr100186D  0.358
2010 Uversky VN. Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes. Chemical Society Reviews. 40: 1623-34. PMID 21049125 DOI: 10.1039/C0Cs00057D  0.481
2010 Meng X, Munishkina LA, Fink AL, Uversky VN. Effects of Various Flavonoids on the α-Synuclein Fibrillation Process. Parkinson's Disease. 2010: 650794. PMID 20976092 DOI: 10.4061/2010/650794  0.776
2010 Dunker AK, Uversky VN. Drugs for 'protein clouds': targeting intrinsically disordered transcription factors. Current Opinion in Pharmacology. 10: 782-8. PMID 20889377 DOI: 10.1016/J.Coph.2010.09.005  0.445
2010 Uversky VN. Targeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: another illustration of the D(2) concept. Expert Review of Proteomics. 7: 543-64. PMID 20653509 DOI: 10.1586/Epr.10.36  0.483
2010 Jorda J, Xue B, Uversky VN, Kajava AV. Protein tandem repeats - the more perfect, the less structured. The Febs Journal. 277: 2673-82. PMID 20553501 DOI: 10.1111/J.1742-464X.2010.07684.X  0.471
2010 Erkizan HV, Uversky VN, Toretsky JA. Oncogenic partnerships: EWS-FLI1 protein interactions initiate key pathways of Ewing's sarcoma. Clinical Cancer Research : An Official Journal of the American Association For Cancer Research. 16: 4077-83. PMID 20547696 DOI: 10.1158/1078-0432.Ccr-09-2261  0.387
2010 Uversky VN. Mysterious oligomerization of the amyloidogenic proteins. The Febs Journal. 277: 2940-53. PMID 20546306 DOI: 10.1111/J.1742-4658.2010.07721.X  0.41
2010 Xue B, Williams RW, Oldfield CJ, Dunker AK, Uversky VN. Archaic chaos: intrinsically disordered proteins in Archaea. Bmc Systems Biology. 4: S1. PMID 20522251 DOI: 10.1186/1752-0509-4-S1-S1  0.459
2010 Dagkessamanskaia A, Durand F, Uversky VN, Binda M, Lopez F, El Azzouzi K, Francois JM, Martin-Yken H. Functional dissection of an intrinsically disordered protein: understanding the roles of different domains of Knr4 protein in protein-protein interactions. Protein Science : a Publication of the Protein Society. 19: 1376-85. PMID 20506404 DOI: 10.1002/Pro.418  0.466
2010 Xue B, Williams RW, Oldfield CJ, Goh GK, Dunker AK, Uversky VN. Viral disorder or disordered viruses: do viral proteins possess unique features? Protein and Peptide Letters. 17: 932-51. PMID 20450483 DOI: 10.2174/092986610791498984  0.484
2010 Ghosh RP, Nikitina T, Horowitz-Scherer RA, Gierasch LM, Uversky VN, Hite K, Hansen JC, Woodcock CL. Unique physical properties and interactions of the domains of methylated DNA binding protein 2. Biochemistry. 49: 4395-410. PMID 20405910 DOI: 10.1021/Bi9019753  0.382
2010 Yamada J, Phillips JL, Patel S, Goldfien G, Calestagne-Morelli A, Huang H, Reza R, Acheson J, Krishnan VV, Newsam S, Gopinathan A, Lau EY, Colvin ME, Uversky VN, Rexach MF. A bimodal distribution of two distinct categories of intrinsically disordered structures with separate functions in FG nucleoporins. Molecular & Cellular Proteomics : McP. 9: 2205-24. PMID 20368288 DOI: 10.1074/Mcp.M000035-Mcp201  0.357
2010 Uversky VN, Dunker AK. Understanding protein non-folding. Biochimica Et Biophysica Acta. 1804: 1231-64. PMID 20117254 DOI: 10.1016/J.Bbapap.2010.01.017  0.506
2010 Sun X, Jones WT, Harvey D, Edwards PJ, Pascal SM, Kirk C, Considine T, Sheerin DJ, Rakonjac J, Oldfield CJ, Xue B, Dunker AK, Uversky VN. N-terminal domains of DELLA proteins are intrinsically unstructured in the absence of interaction with GID1/gibberellic acid receptors. The Journal of Biological Chemistry. 285: 11557-71. PMID 20103592 DOI: 10.1074/Jbc.M109.027011  0.367
2010 Xue B, Dunbrack RL, Williams RW, Dunker AK, Uversky VN. PONDR-FIT: a meta-predictor of intrinsically disordered amino acids. Biochimica Et Biophysica Acta. 1804: 996-1010. PMID 20100603 DOI: 10.1016/J.Bbapap.2010.01.011  0.414
2010 Turoverov KK, Kuznetsova IM, Uversky VN. The protein kingdom extended: ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation. Progress in Biophysics and Molecular Biology. 102: 73-84. PMID 20097220 DOI: 10.1016/J.Pbiomolbio.2010.01.003  0.515
2010 Posokhova E, Uversky V, Martemyanov KA. Proteomic identification of Hsc70 as a mediator of RGS9-2 degradation by in vivo interactome analysis. Journal of Proteome Research. 9: 1510-21. PMID 20095651 DOI: 10.1021/Pr901022M  0.387
2010 Zhou W, Long C, Reaney SH, Di Monte DA, Fink AL, Uversky VN. Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions. Biochimica Et Biophysica Acta. 1802: 322-30. PMID 20026206 DOI: 10.1016/J.Bbadis.2009.12.004  0.358
2010 Uversky VN. The mysterious unfoldome: structureless, underappreciated, yet vital part of any given proteome. Journal of Biomedicine & Biotechnology. 2010: 568068. PMID 20011072 DOI: 10.1155/2010/568068  0.471
2010 Frimpong AK, Abzalimov RR, Uversky VN, Kaltashov IA. Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: conformational heterogeneity of alpha-synuclein. Proteins. 78: 714-22. PMID 19847913 DOI: 10.1002/Prot.22604  0.411
2010 Uversky VN. Intrinsically disordered proteins and their environment: effects of strong denaturants, temperature, pH, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding. The Protein Journal. 28: 305-25. PMID 19768526 DOI: 10.1007/S10930-009-9201-4  0.436
2010 Uversky VN, Goto Y. Acid denaturation and anion-induced folding of globular proteins: multitude of equilibium partially folded intermediates. Current Protein & Peptide Science. 10: 447-55. PMID 19538151 DOI: 10.2174/138920309789352029  0.452
2010 Kuznetsova IM, Biktashev AG, Khaitlina SY, Vassilenko KS, Turoverov KK, Uversky VN. Effect of self-association on the structural organization of partially folded proteins: inactivated actin. Biophysical Journal. 77: 2788-800. PMID 10545377 DOI: 10.1016/S0006-3495(99)77111-0  0.436
2010 Zhou W, Long C, Fink A, Uversky V. Calbindin-D28K acts as a calcium-dependent chaperone suppressing α-synuclein fibrillation in vitro Open Life Sciences. 5: 11-20. DOI: 10.2478/S11535-009-0071-8  0.373
2010 Zhou W, Long C, Fink AL, Uversky VN. 3, 4-Dihydroxyphenylacetic Acid (DOPAC) Impairs α-Synuclein Interaction with Lipids The Open Proteomics Journal. 3: 1-7. DOI: 10.2174/1875039701003010001  0.336
2010 Jorda J, Xue B, Uversky VN, Kajava AV. Protein tandem repeats - the more perfect, the less structured Febs Journal. 277: 2673-2682. DOI: 10.1111/j.1742-4658.2010.07684.x  0.309
2010 Yamin G, Munishkina LA, Karymov MA, Lyubchenko YL, Uversky VN, Fink AL. Correction to forcing nonamyloidogenic β-synuclein to fibrillate (Biochemistry (2005) 44, (9096) DOI: 10.1021/ bi048778a) Biochemistry. 49: 247. DOI: 10.1021/Bi8016685  0.735
2010 Uversky VN, Dunker AK, Xue B, Oldfield CJ. Searching for the Native Molten Globules Biophysical Journal. 98: 256a. DOI: 10.1016/J.Bpj.2009.12.1393  0.519
2010 Xue B, Oldfield CJ, Hsu W, Uversky V, Dunker A. Development of New Predictors of Intrinsically Disordered Proteins and Residues Biophysical Journal. 98: 256a. DOI: 10.1016/J.Bpj.2009.12.1391  0.352
2009 Midic U, Oldfield CJ, Dunker AK, Obradovic Z, Uversky VN. Unfoldomics of human genetic diseases: illustrative examples of ordered and intrinsically disordered members of the human diseasome. Protein and Peptide Letters. 16: 1533-47. PMID 20001916 DOI: 10.2174/092986609789839377  0.385
2009 Kutyshenko VP, Prokhorov DA, Timchenko MA, Kudrevatykh YA, Gushchina LV, Khristoforov VS, Filimonov VV, Uversky VN. Solution structure and dynamics of the chimeric SH3 domains, SHH- and SHA-"Bergeracs". Biochimica Et Biophysica Acta. 1794: 1813-22. PMID 19732853 DOI: 10.1016/J.Bbapap.2009.08.021  0.371
2009 Mohan A, Uversky VN, Radivojac P. Influence of sequence changes and environment on intrinsically disordered proteins. Plos Computational Biology. 5: e1000497. PMID 19730682 DOI: 10.1371/Journal.Pcbi.1000497  0.474
2009 Permyakov SE, Bakunts AG, Permyakova ME, Denesyuk AI, Uversky VN, Permyakov EA. Metal-controlled interdomain cooperativity in parvalbumins. Cell Calcium. 46: 163-75. PMID 19651438 DOI: 10.1016/J.Ceca.2009.07.001  0.36
2009 Meng X, Munishkina LA, Fink AL, Uversky VN. Molecular mechanisms underlying the flavonoid-induced inhibition of alpha-synuclein fibrillation. Biochemistry. 48: 8206-24. PMID 19634918 DOI: 10.1021/Bi900506B  0.771
2009 He B, Wang K, Liu Y, Xue B, Uversky VN, Dunker AK. Predicting intrinsic disorder in proteins: an overview. Cell Research. 19: 929-49. PMID 19597536 DOI: 10.1038/Cr.2009.87  0.457
2009 Uversky VN, Oldfield CJ, Midic U, Xie H, Xue B, Vucetic S, Iakoucheva LM, Obradovic Z, Dunker AK. Unfoldomics of human diseases: linking protein intrinsic disorder with diseases. Bmc Genomics. 10: S7. PMID 19594884 DOI: 10.1186/1471-2164-10-S1-S7  0.4
2009 Midic U, Oldfield CJ, Dunker AK, Obradovic Z, Uversky VN. Protein disorder in the human diseasome: unfoldomics of human genetic diseases. Bmc Genomics. 10: S12. PMID 19594871 DOI: 10.1186/1471-2164-10-S1-S12  0.443
2009 Xue B, Li L, Meroueh SO, Uversky VN, Dunker AK. Analysis of structured and intrinsically disordered regions of transmembrane proteins. Molecular Biosystems. 5: 1688-1702. PMID 19585006 DOI: 10.1039/B905913J  0.453
2009 Seshadri S, Oberg KA, Uversky VN. Mechanisms and consequences of protein aggregation: the role of folding intermediates. Current Protein & Peptide Science. 10: 456-63. PMID 19538148 DOI: 10.2174/138920309789351976  0.453
2009 Uversky VN, Eliezer D. Biophysics of Parkinson's disease: structure and aggregation of alpha-synuclein. Current Protein & Peptide Science. 10: 483-99. PMID 19538146 DOI: 10.2174/138920309789351921  0.372
2009 Munishkina LA, Fink AL, Uversky VN. Accelerated fibrillation of alpha-synuclein induced by the combined action of macromolecular crowding and factors inducing partial folding. Current Alzheimer Research. 6: 252-60. PMID 19519306 DOI: 10.2174/156720509788486491  0.767
2009 Uversky VN. Intrinsic Disorder in Proteins Associated with Neurodegenerative Diseases Frontiers in Bioscience. 14: 5188-5238. PMID 19482612 DOI: 10.2741/3594  0.408
2009 Xue B, Oldfield CJ, Dunker AK, Uversky VN. CDF it all: consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions. Febs Letters. 583: 1469-74. PMID 19351533 DOI: 10.1016/J.Febslet.2009.03.070  0.442
2009 Zhou W, Gallagher A, Hong DP, Long C, Fink AL, Uversky VN. At low concentrations, 3,4-dihydroxyphenylacetic acid (DOPAC) binds non-covalently to alpha-synuclein and prevents its fibrillation. Journal of Molecular Biology. 388: 597-610. PMID 19328209 DOI: 10.1016/J.Jmb.2009.03.053  0.333
2009 Brocca S, Samalíková M, Uversky VN, Lotti M, Vanoni M, Alberghina L, Grandori R. Order propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1. Proteins. 76: 731-46. PMID 19280601 DOI: 10.1002/Prot.22385  0.445
2009 Tompa P, Fuxreiter M, Oldfield CJ, Simon I, Dunker AK, Uversky VN. Close encounters of the third kind: disordered domains and the interactions of proteins. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 31: 328-35. PMID 19260013 DOI: 10.1002/Bies.200800151  0.457
2009 Hébrard E, Bessin Y, Michon T, Longhi S, Uversky VN, Delalande F, Van Dorsselaer A, Romero P, Walter J, Declerck N, Fargette D. Intrinsic disorder in Viral Proteins Genome-Linked: experimental and predictive analyses. Virology Journal. 6: 23. PMID 19220875 DOI: 10.1186/1743-422X-6-23  0.392
2009 Liang S, Li L, Hsu WL, Pilcher MN, Uversky V, Zhou Y, Dunker AK, Meroueh SO. Exploring the molecular design of protein interaction sites with molecular dynamics simulations and free energy calculations. Biochemistry. 48: 399-414. PMID 19113835 DOI: 10.1021/Bi8017043  0.412
2009 Tokuriki N, Oldfield CJ, Uversky VN, Berezovsky IN, Tawfik DS. Do viral proteins possess unique biophysical features? Trends in Biochemical Sciences. 34: 53-9. PMID 19062293 DOI: 10.1016/J.Tibs.2008.10.009  0.435
2009 Durand F, Dagkessamanskaia A, Martin-Yken H, Graille M, Van Tilbeurgh H, Uversky VN, François JM. Structure-function analysis of Knr4/Smi1, a newly member of intrinsically disordered proteins family, indispensable in the absence of a functional PKC1-SLT2 pathway in Saccharomyces cerevisiae. Yeast (Chichester, England). 25: 563-76. PMID 18668512 DOI: 10.1002/Yea.1608  0.446
2009 Johnson DE, Sickmeier MD, Meng J, Le Gall T, Uversky V, Dunker AK. High-throughput Characterization of Intrinsically Disordered Proteins from the Protein Structure Initiative Biophysical Journal. 96: 220a. DOI: 10.1016/J.Bpj.2008.12.1919  0.478
2009 Oldfield CJ, Uversky VN, Dunker AK. Bioinformatic Analysis of the Role of Intrinsic Disorder in Multiple Specificity Biophysical Journal. 96: 220a. DOI: 10.1016/J.Bpj.2008.12.1918  0.489
2009 Midic U, Oldfield C, Dunker A, Obradovic Z, Uversky V. Unfoldomics of Human Genetic Diseases Biophysical Journal. 96: 318a. DOI: 10.1016/J.Bpj.2008.12.1594  0.436
2009 Dunker A, Chan W, Karn S, Uversky V, Brooks D, Oldfield C, White J, Perumal N, Romero P. Protein Folding as a Transition Step from Ancient to the Modern Life Forms Biophysical Journal. 96: 318a. DOI: 10.1016/J.Bpj.2008.12.1591  0.433
2008 Xu M, Ermolenkov VV, Uversky VN, Lednev IK. Hen egg white lysozyme fibrillation: a deep-UV resonance Raman spectroscopic study. Journal of Biophotonics. 1: 215-29. PMID 19412971 DOI: 10.1002/Jbio.200710013  0.362
2008 Tóth-Petróczy A, Oldfield CJ, Simon I, Takagi Y, Dunker AK, Uversky VN, Fuxreiter M. Malleable machines in transcription regulation: the mediator complex. Plos Computational Biology. 4: e1000243. PMID 19096501 DOI: 10.1371/Journal.Pcbi.1000243  0.4
2008 Munishkina LA, Fink AL, Uversky VN. Concerted action of metals and macromolecular crowding on the fibrillation of alpha-synuclein. Protein and Peptide Letters. 15: 1079-85. PMID 19075819 DOI: 10.2174/092986608786071102  0.748
2008 Fuxreiter M, Tompa P, Simon I, Uversky VN, Hansen JC, Asturias FJ. Malleable machines take shape in eukaryotic transcriptional regulation. Nature Chemical Biology. 4: 728-37. PMID 19008886 DOI: 10.1038/Nchembio.127  0.362
2008 Campen A, Williams RM, Brown CJ, Meng J, Uversky VN, Dunker AK. TOP-IDP-scale: a new amino acid scale measuring propensity for intrinsic disorder. Protein and Peptide Letters. 15: 956-63. PMID 18991772 DOI: 10.2174/092986608785849164  0.35
2008 Dunker AK, Silman I, Uversky VN, Sussman JL. Function and structure of inherently disordered proteins Current Opinion in Structural Biology. 18: 756-764. PMID 18952168 DOI: 10.1016/J.Sbi.2008.10.002  0.466
2008 Goh GK, Dunker AK, Uversky VN. A comparative analysis of viral matrix proteins using disorder predictors. Virology Journal. 5: 126. PMID 18947403 DOI: 10.1186/1743-422X-5-126  0.397
2008 Uversky VN. Alpha-synuclein misfolding and neurodegenerative diseases. Current Protein & Peptide Science. 9: 507-40. PMID 18855701 DOI: 10.2174/138920308785915218  0.377
2008 Goh GK, Dunker AK, Uversky VN. Protein intrinsic disorder toolbox for comparative analysis of viral proteins. Bmc Genomics. 9: S4. PMID 18831795 DOI: 10.1186/1471-2164-9-S2-S4  0.444
2008 Ren S, Uversky VN, Chen Z, Dunker AK, Obradovic Z. Short Linear Motifs recognized by SH2, SH3 and Ser/Thr Kinase domains are conserved in disordered protein regions. Bmc Genomics. 9: S26. PMID 18831792 DOI: 10.1186/1471-2164-9-S2-S26  0.448
2008 Dunker AK, Oldfield CJ, Meng J, Romero P, Yang JY, Chen JW, Vacic V, Obradovic Z, Uversky VN. The unfoldomics decade: an update on intrinsically disordered proteins. Bmc Genomics. 9: S1. PMID 18831774 DOI: 10.1186/1471-2164-9-S2-S1  0.491
2008 Hong DP, Fink AL, Uversky VN. Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein. Journal of Molecular Biology. 383: 214-23. PMID 18775438 DOI: 10.1016/J.Jmb.2008.08.039  0.337
2008 Stepanenko OV, Verkhusha VV, Kuznetsova IM, Uversky VN, Turoverov KK. Fluorescent proteins as biomarkers and biosensors: throwing color lights on molecular and cellular processes. Current Protein & Peptide Science. 9: 338-69. PMID 18691124 DOI: 10.2174/138920308785132668  0.69
2008 Munishkina LA, Ahmad A, Fink AL, Uversky VN. Guiding protein aggregation with macromolecular crowding. Biochemistry. 47: 8993-9006. PMID 18665616 DOI: 10.1021/Bi8008399  0.809
2008 Hu D, Qin Z, Xue B, Fink AL, Uversky VN. Effect of methionine oxidation on the structural properties, conformational stability, and aggregation of immunoglobulin light chain LEN. Biochemistry. 47: 8665-77. PMID 18652490 DOI: 10.1021/Bi800806D  0.309
2008 Cortese MS, Uversky VN, Dunker AK. Intrinsic disorder in scaffold proteins: getting more from less. Progress in Biophysics and Molecular Biology. 98: 85-106. PMID 18619997 DOI: 10.1016/J.Pbiomolbio.2008.05.007  0.443
2008 Uversky VN, Oldfield CJ, Dunker AK. Intrinsically disordered proteins in human diseases: introducing the D2 concept. Annual Review of Biophysics. 37: 215-46. PMID 18573080 DOI: 10.1146/Annurev.Biophys.37.032807.125924  0.485
2008 Uversky VN. Amyloidogenesis of natively unfolded proteins. Current Alzheimer Research. 5: 260-87. PMID 18537543 DOI: 10.2174/156720508784533312  0.478
2008 Singh VK, Pacheco I, Uversky VN, Smith SP, MacLeod RJ, Jia Z. Intrinsically disordered human C/EBP homologous protein regulates biological activity of colon cancer cells during calcium stress. Journal of Molecular Biology. 380: 313-26. PMID 18534616 DOI: 10.1016/J.Jmb.2008.04.069  0.468
2008 Rantalainen KI, Uversky VN, Permi P, Kalkkinen N, Dunker AK, Mäkinen K. Potato virus A genome-linked protein VPg is an intrinsically disordered molten globule-like protein with a hydrophobic core. Virology. 377: 280-8. PMID 18533220 DOI: 10.1016/J.Virol.2008.04.025  0.468
2008 Stepanenko OV, Verkhusha VV, Shavlovsky MM, Kuznetsova IM, Uversky VN, Turoverov KK. Understanding the role of Arg96 in structure and stability of green fluorescent protein. Proteins. 73: 539-51. PMID 18470931 DOI: 10.1002/Prot.22089  0.672
2008 Paliy O, Gargac SM, Cheng Y, Uversky VN, Dunker AK. Protein disorder is positively correlated with gene expression in Escherichia coli. Journal of Proteome Research. 7: 2234-45. PMID 18465893 DOI: 10.1021/Pr800055R  0.398
2008 De Biasio A, Guarnaccia C, Popovic M, Uversky VN, Pintar A, Pongor S. Prevalence of intrinsic disorder in the intracellular region of human single-pass type I proteins: the case of the notch ligand Delta-4. Journal of Proteome Research. 7: 2496-506. PMID 18435556 DOI: 10.1021/Pr800063U  0.459
2008 Oldfield CJ, Meng J, Yang JY, Yang MQ, Uversky VN, Dunker AK. Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners. Bmc Genomics. 9: S1. PMID 18366598 DOI: 10.1186/1471-2164-9-S1-S1  0.474
2008 Prokhorov DA, Timchenko AA, Uversky VN, Khristoforov VS, Kihara H, Kimura K, Kutyshenko VP. Dynamics of oligomer formation by denatured carbonic anhydrase II. Biochimica Et Biophysica Acta. 1784: 834-42. PMID 18359304 DOI: 10.1016/J.Bbapap.2008.02.012  0.43
2008 Mohan A, Sullivan WJ, Radivojac P, Dunker AK, Uversky VN. Intrinsic disorder in pathogenic and non-pathogenic microbes: discovering and analyzing the unfoldomes of early-branching eukaryotes. Molecular Biosystems. 4: 328-40. PMID 18354786 DOI: 10.1039/B719168E  0.439
2008 Dunker AK, Uversky VN. Signal transduction via unstructured protein conduits. Nature Chemical Biology. 4: 229-30. PMID 18347590 DOI: 10.1038/Nchembio0408-229  0.368
2008 Permyakov SE, Bakunts AG, Denesyuk AI, Knyazeva EL, Uversky VN, Permyakov EA. Apo-parvalbumin as an intrinsically disordered protein. Proteins. 72: 822-36. PMID 18260106 DOI: 10.1002/Prot.21974  0.433
2008 Toth-Petroczy A, Meszaros B, Simon I, Dunker AK, Uversky VN, Fuxreiter M. Assessing Conservation of Disordered Regions in Proteins The Open Proteomics Journal. 1: 46-53. DOI: 10.2174/1875039700801010046  0.412
2008 Uversky V. Protein Folding, Misfolding and Aggregation: Classical Themes and Novel Approaches. Edited by Victor Muñoz. Chembiochem. 9: 2750-2751. DOI: 10.1002/Cbic.200800645  0.402
2007 Uversky VN, Radivojac P, Iakoucheva LM, Obradovic Z, Dunker AK. Prediction of intrinsic disorder and its use in functional proteomics. Methods in Molecular Biology (Clifton, N.J.). 408: 69-92. PMID 18314578 DOI: 10.1007/978-1-59745-547-3_5  0.478
2007 Anderson GR, Lujan R, Semenov A, Pravetoni M, Posokhova EN, Song JH, Uversky V, Chen CK, Wickman K, Martemyanov KA. Expression and localization of RGS9-2/G 5/R7BP complex in vivo is set by dynamic control of its constitutive degradation by cellular cysteine proteases. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 27: 14117-27. PMID 18094251 DOI: 10.1523/Jneurosci.3884-07.2007  0.342
2007 Li L, Uversky VN, Dunker AK, Meroueh SO. A computational investigation of allostery in the catabolite activator protein. Journal of the American Chemical Society. 129: 15668-76. PMID 18041838 DOI: 10.1021/Ja076046A  0.327
2007 Uversky VN. Nanoimaging in protein-misfolding and -conformational diseases. Nanomedicine (London, England). 2: 615-43. PMID 17976024 DOI: 10.2217/17435889.2.5.615  0.453
2007 Cheng Y, Oldfield CJ, Meng J, Romero P, Uversky VN, Dunker AK. Mining alpha-helix-forming molecular recognition features with cross species sequence alignments. Biochemistry. 46: 13468-77. PMID 17973494 DOI: 10.1021/Bi7012273  0.382
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