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Peter Tompa - Publications

Affiliations: 
VIB-VUB Center for Structural Biology VIB-VUB Brussels Belgium 
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287 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2024 Jiao X, Di Sante G, Casimiro MC, Tantos A, Ashton AW, Li Z, Quach Y, Bhargava D, Di Rocco A, Pupo C, Crosariol M, Lazar T, Tompa P, Wang C, Yu Z, et al. A cyclin D1 intrinsically disordered domain accesses modified histone motifs to govern gene transcription. Oncogenesis. 13: 4. PMID 38191593 DOI: 10.1038/s41389-023-00502-1  0.781
2023 Ghafouri H, Lazar T, Del Conte A, Tenorio Ku LG, Tompa P, Tosatto SCE, Monzon AM. PED in 2024: improving the community deposition of structural ensembles for intrinsically disordered proteins. Nucleic Acids Research. PMID 37904608 DOI: 10.1093/nar/gkad947  0.826
2023 Lázár T, Tantos A, Tompa P, Schad E. Reply to "Intrinsic protein disorder uncouples affinity from binding specificity". Protein Science : a Publication of the Protein Society. 32: e4601. PMID 36808785 DOI: 10.1002/pro.4601  0.841
2022 Meszaros A, Ahmed J, Russo G, Tompa P, Lazar T. The evolution and polymorphism of mono-amino acid repeats in androgen receptor and their regulatory role in health and disease. Frontiers in Medicine. 9: 1019803. PMID 36388907 DOI: 10.3389/fmed.2022.1019803  0.794
2022 Mészáros A, Muwonge K, Janvier S, Ahmed J, Tompa P. A Novel Tandem-Tag Purification Strategy for Challenging Disordered Proteins. Biomolecules. 12. PMID 36358915 DOI: 10.3390/biom12111566  0.42
2022 Lazar T, Tantos A, Tompa P, Schad E. Intrinsic protein disorder uncouples affinity from binding specificity. Protein Science : a Publication of the Protein Society. 31: e4455. PMID 36305763 DOI: 10.1002/pro.4455  0.848
2022 Guharoy M, Lazar T, Macossay-Castillo M, Tompa P. Degron masking outlines degronons, co-degrading functional modules in the proteome. Communications Biology. 5: 445. PMID 35545699 DOI: 10.1038/s42003-022-03391-z  0.845
2022 Van Lindt J, Lazar T, Pakravan D, Demulder M, Meszaros A, Van Den Bosch L, Maes D, Tompa P. F/YGG-motif is an intrinsically disordered nucleic-acid binding motif. Rna Biology. 19: 622-635. PMID 35491929 DOI: 10.1080/15476286.2022.2066336  0.8
2021 Quaglia F, Mészáros B, Salladini E, Hatos A, Pancsa R, Chemes LB, Pajkos M, Lazar T, Peña-Díaz S, Santos J, Ács V, Farahi N, Fichó E, Aspromonte MC, Bassot C, ... ... Tompa P, et al. DisProt in 2022: improved quality and accessibility of protein intrinsic disorder annotation. Nucleic Acids Research. PMID 34850135 DOI: 10.1093/nar/gkab1082  0.85
2021 Quaglia F, Lazar T, Hatos A, Tompa P, Piovesan D, Tosatto SCE. Exploring Curated Conformational Ensembles of Intrinsically Disordered Proteins in the Protein Ensemble Database. Current Protocols. 1: e192. PMID 34252246 DOI: 10.1002/cpz1.192  0.839
2021 Quaglia F, Lazar T, Hatos A, Tompa P, Piovesan D, Tosatto SCE. Exploring Curated Conformational Ensembles of Intrinsically Disordered Proteins in the Protein Ensemble Database. Current Protocols. 1: e192. PMID 34252246 DOI: 10.1002/cpz1.192  0.839
2021 Murvai N, Kalmar L, Szabo B, Schad E, Micsonai A, Kardos J, Buday L, Han KH, Tompa P, Tantos A. Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14. International Journal of Molecular Sciences. 22. PMID 34201246 DOI: 10.3390/ijms22126190  0.846
2021 Murvai N, Kalmar L, Szabo B, Schad E, Micsonai A, Kardos J, Buday L, Han KH, Tompa P, Tantos A. Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14. International Journal of Molecular Sciences. 22. PMID 34201246 DOI: 10.3390/ijms22126190  0.846
2021 Ahmed J, Meszaros A, Lazar T, Tompa P. DNA-binding domain as the minimal region driving RNA-dependent liquid-liquid phase separation of androgen receptor. Protein Science : a Publication of the Protein Society. PMID 33938068 DOI: 10.1002/pro.4100  0.782
2021 Ahmed J, Meszaros A, Lazar T, Tompa P. DNA-binding domain as the minimal region driving RNA-dependent liquid-liquid phase separation of androgen receptor. Protein Science : a Publication of the Protein Society. PMID 33938068 DOI: 10.1002/pro.4100  0.782
2021 Farahi N, Lazar T, Wodak SJ, Tompa P, Pancsa R. Integration of Data from Liquid-Liquid Phase Separation Databases Highlights Concentration and Dosage Sensitivity of LLPS Drivers. International Journal of Molecular Sciences. 22. PMID 33809541 DOI: 10.3390/ijms22063017  0.82
2021 Farahi N, Lazar T, Wodak SJ, Tompa P, Pancsa R. Integration of Data from Liquid-Liquid Phase Separation Databases Highlights Concentration and Dosage Sensitivity of LLPS Drivers. International Journal of Molecular Sciences. 22. PMID 33809541 DOI: 10.3390/ijms22063017  0.82
2021 Van Lindt J, Bratek-Skicki A, Nguyen PN, Pakravan D, Durán-Armenta LF, Tantos A, Pancsa R, Van Den Bosch L, Maes D, Tompa P. Author Correction: A generic approach to study the kinetics of liquid-liquid phase separation under near-native conditions. Communications Biology. 4: 303. PMID 33654184 DOI: 10.1038/s42003-021-01853-4  0.762
2021 Van Lindt J, Bratek-Skicki A, Nguyen PN, Pakravan D, Durán-Armenta LF, Tantos A, Pancsa R, Van Den Bosch L, Maes D, Tompa P. A generic approach to study the kinetics of liquid-liquid phase separation under near-native conditions. Communications Biology. 4: 77. PMID 33469149 DOI: 10.1038/s42003-020-01596-8  0.814
2020 Lazar T, Martínez-Pérez E, Quaglia F, Hatos A, Chemes LB, Iserte JA, Méndez NA, Garrone NA, Saldaño TE, Marchetti J, Rueda AJV, Bernadó P, Blackledge M, Cordeiro TN, Fagerberg E, ... ... Tompa P, et al. PED in 2021: a major update of the protein ensemble database for intrinsically disordered proteins. Nucleic Acids Research. PMID 33305318 DOI: 10.1093/nar/gkaa1021  0.843
2020 Lazar T, Martínez-Pérez E, Quaglia F, Hatos A, Chemes LB, Iserte JA, Méndez NA, Garrone NA, Saldaño TE, Marchetti J, Rueda AJV, Bernadó P, Blackledge M, Cordeiro TN, Fagerberg E, ... ... Tompa P, et al. PED in 2021: a major update of the protein ensemble database for intrinsically disordered proteins. Nucleic Acids Research. PMID 33305318 DOI: 10.1093/nar/gkaa1021  0.843
2020 Iserte JA, Lazar T, Tosatto SCE, Tompa P, Marino-Buslje C. Chasing coevolutionary signals in intrinsically disordered proteins complexes. Scientific Reports. 10: 17962. PMID 33087759 DOI: 10.1038/s41598-020-74791-6  0.867
2020 Iserte JA, Lazar T, Tosatto SCE, Tompa P, Marino-Buslje C. Chasing coevolutionary signals in intrinsically disordered proteins complexes. Scientific Reports. 10: 17962. PMID 33087759 DOI: 10.1038/s41598-020-74791-6  0.867
2020 Murvai N, Kalmar L, Szalaine Agoston B, Szabo B, Tantos A, Csikos G, Micsonai A, Kardos J, Vertommen D, Nguyen PN, Hristozova N, Lang A, Kovacs D, Buday L, Han KH, ... ... Tompa P, et al. Interplay of Structural Disorder and Short Binding Elements in the Cellular Chaperone Function of Plant Dehydrin ERD14. Cells. 9. PMID 32784707 DOI: 10.3390/Cells9081856  0.844
2020 Murvai N, Kalmar L, Szalaine Agoston B, Szabo B, Tantos A, Csikos G, Micsonai A, Kardos J, Vertommen D, Nguyen PN, Hristozova N, Lang A, Kovacs D, Buday L, Han KH, ... ... Tompa P, et al. Interplay of Structural Disorder and Short Binding Elements in the Cellular Chaperone Function of Plant Dehydrin ERD14. Cells. 9. PMID 32784707 DOI: 10.3390/Cells9081856  0.844
2020 Nguyen HH, Ábrányi-Balogh P, Petri L, Mészáros A, Pauwels K, Vandenbussche G, Keserű GM, Tompa P. Targeting an Intrinsically Disordered Protein by Covalent Modification. Methods in Molecular Biology (Clifton, N.J.). 2141: 835-854. PMID 32696392 DOI: 10.1007/978-1-0716-0524-0_43  0.32
2020 Bokor M, Tantos Á, Tompa P, Han KH, Tompa K. WT and A53T α-Synuclein Systems: Melting Diagram and Its New Interpretation. International Journal of Molecular Sciences. 21. PMID 32503167 DOI: 10.3390/ijms21113997  0.806
2020 Lazar T, Guharoy M, Vranken W, Rauscher S, Wodak SJ, Tompa P. Distance-Based Metrics for Comparing Conformational Ensembles of Intrinsically Disordered Proteins. Biophysical Journal. 118: 2952-2965. PMID 32502383 DOI: 10.1016/J.Bpj.2020.05.015  0.853
2020 Lazar T, Guharoy M, Vranken W, Rauscher S, Wodak SJ, Tompa P. Distance-Based Metrics for Comparing Conformational Ensembles of Intrinsically Disordered Proteins. Biophysical Journal. 118: 2952-2965. PMID 32502383 DOI: 10.1016/J.Bpj.2020.05.015  0.853
2020 Bokor M, Tantos Á, Mészáros A, Jenei B, Haminda R, Tompa P, Tompa K. Molecular motions and interactions in aqueous solutions of thymosin-β4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 32469123 DOI: 10.1002/cphc.202000264  0.36
2020 Bokor M, Tantos Á, Mészáros A, Jenei B, Haminda R, Tompa P, Tompa K. Corrigendum: Molecular Motions and Interactions in Aqueous Solutions of Thymosin-β , Stabilin C-Terminal Domain (CTD) and Their 1:1 Complex Studied by H NMR Spectroscopy. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 21: 958. PMID 32374478 DOI: 10.1002/cphc.202000158  0.769
2020 Kosol S, Contreras-Martos S, Piai A, Varadi M, Lazar T, Bekesi A, Lebrun P, Felli IC, Pierattelli R, Tompa P. Interaction between the scaffold proteins CBP by IQGAP1 provides an interface between gene expression and cytoskeletal activity. Scientific Reports. 10: 5753. PMID 32238831 DOI: 10.1038/s41598-020-62069-w  0.843
2020 Kosol S, Contreras-Martos S, Piai A, Varadi M, Lazar T, Bekesi A, Lebrun P, Felli IC, Pierattelli R, Tompa P. Interaction between the scaffold proteins CBP by IQGAP1 provides an interface between gene expression and cytoskeletal activity. Scientific Reports. 10: 5753. PMID 32238831 DOI: 10.1038/s41598-020-62069-w  0.843
2019 Davey NE, Babu MM, Blackledge M, Bridge A, Capella-Gutierrez S, Dosztanyi Z, Drysdale R, Edwards RJ, Elofsson A, Felli IC, Gibson TJ, Gutmanas A, Hancock JM, Harrow J, Higgins D, ... ... Tompa P, et al. An intrinsically disordered proteins community for ELIXIR. F1000research. 8. PMID 31824649 DOI: 10.12688/F1000Research.20136.1  0.35
2019 Hatos A, Hajdu-Soltész B, Monzon AM, Palopoli N, Álvarez L, Aykac-Fas B, Bassot C, Benítez GI, Bevilacqua M, Chasapi A, Chemes L, Davey NE, Davidović R, Dunker AK, Elofsson A, ... ... Tompa P, et al. DisProt: intrinsic protein disorder annotation in 2020. Nucleic Acids Research. PMID 31713636 DOI: 10.1093/Nar/Gkz975  0.834
2019 Hatos A, Hajdu-Soltész B, Monzon AM, Palopoli N, Álvarez L, Aykac-Fas B, Bassot C, Benítez GI, Bevilacqua M, Chasapi A, Chemes L, Davey NE, Davidović R, Dunker AK, Elofsson A, ... ... Tompa P, et al. DisProt: intrinsic protein disorder annotation in 2020. Nucleic Acids Research. PMID 31713636 DOI: 10.1093/Nar/Gkz975  0.834
2019 Mészáros B, Erdős G, Szabó B, Schád É, Tantos Á, Abukhairan R, Horváth T, Murvai N, Kovács OP, Kovács M, Tosatto SCE, Tompa P, Dosztányi Z, Pancsa R. PhaSePro: the database of proteins driving liquid-liquid phase separation. Nucleic Acids Research. PMID 31612960 DOI: 10.1093/nar/gkz848  0.817
2019 Mészáros B, Erdős G, Szabó B, Schád É, Tantos Á, Abukhairan R, Horváth T, Murvai N, Kovács OP, Kovács M, Tosatto SCE, Tompa P, Dosztányi Z, Pancsa R. PhaSePro: the database of proteins driving liquid-liquid phase separation. Nucleic Acids Research. PMID 31612960 DOI: 10.1093/nar/gkz848  0.817
2019 Szabo B, Horvath T, Schad E, Murvai N, Tantos A, Kalmar L, Chemes LB, Han KH, Tompa P. Intrinsically Disordered Linkers Impart Processivity on Enzymes by Spatial Confinement of Binding Domains. International Journal of Molecular Sciences. 20. PMID 31032817 DOI: 10.3390/ijms20092119  0.824
2019 Szabo B, Horvath T, Schad E, Murvai N, Tantos A, Kalmar L, Chemes LB, Han KH, Tompa P. Intrinsically Disordered Linkers Impart Processivity on Enzymes by Spatial Confinement of Binding Domains. International Journal of Molecular Sciences. 20. PMID 31032817 DOI: 10.3390/ijms20092119  0.824
2019 Macossay-Castillo M, Marvelli G, Guharoy M, Jain A, Kihara D, Tompa P, Wodak SJ. The Balancing Act of Intrinsically Disordered Proteins: Enabling Functional Diversity while Minimizing Promiscuity. Journal of Molecular Biology. PMID 30878482 DOI: 10.1016/J.Jmb.2019.03.008  0.862
2019 Pancsa R, Schad E, Tantos A, Tompa P. Emergent functions of proteins in non-stoichiometric supramolecular assemblies. Biochimica Et Biophysica Acta. Proteins and Proteomics. 1867: 970-979. PMID 30826453 DOI: 10.1016/j.bbapap.2019.02.007  0.837
2019 Pancsa R, Schad E, Tantos A, Tompa P. Emergent functions of proteins in non-stoichiometric supramolecular assemblies. Biochimica Et Biophysica Acta. Proteins and Proteomics. 1867: 970-979. PMID 30826453 DOI: 10.1016/j.bbapap.2019.02.007  0.401
2019 Pancsa R, Kovacs D, Tompa P. Misprediction of Structural Disorder in Halophiles. Molecules (Basel, Switzerland). 24. PMID 30699990 DOI: 10.3390/molecules24030479  0.499
2019 Pancsa R, Kovacs D, Tompa P. Misprediction of Structural Disorder in Halophiles. Molecules (Basel, Switzerland). 24. PMID 30699990 DOI: 10.3390/molecules24030479  0.499
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  0.351
2018 Bekesi A, Abdellaoui S, Holroyd N, Van Delm W, Pardon E, Pauwels J, Gevaert K, Steyaert J, Derveaux S, Borysik A, Tompa P. Challenges in the Structural-Functional Characterization of Multidomain, Partially Disordered Proteins CBP and p300: Preparing Native Proteins and Developing Nanobody Tools. Methods in Enzymology. 611: 607-675. PMID 30471702 DOI: 10.1016/bs.mie.2018.09.032  0.469
2018 Bekesi A, Abdellaoui S, Holroyd N, Van Delm W, Pardon E, Pauwels J, Gevaert K, Steyaert J, Derveaux S, Borysik A, Tompa P. Challenges in the Structural-Functional Characterization of Multidomain, Partially Disordered Proteins CBP and p300: Preparing Native Proteins and Developing Nanobody Tools. Methods in Enzymology. 611: 607-675. PMID 30471702 DOI: 10.1016/bs.mie.2018.09.032  0.469
2018 Tompa K, Bokor M, Tompa P. The Melting Diagram of Protein Solutions and Its Thermodynamic Interpretation. International Journal of Molecular Sciences. 19. PMID 30424574 DOI: 10.3390/ijms19113571  0.402
2018 Pancsa R, Zsolyomi F, Tompa P. Co-Evolution of Intrinsically Disordered Proteins with Folded Partners Witnessed by Evolutionary Couplings. International Journal of Molecular Sciences. 19. PMID 30366362 DOI: 10.3390/ijms19113315  0.394
2018 Pancsa R, Zsolyomi F, Tompa P. Co-Evolution of Intrinsically Disordered Proteins with Folded Partners Witnessed by Evolutionary Couplings. International Journal of Molecular Sciences. 19. PMID 30366362 DOI: 10.3390/ijms19113315  0.394
2018 Contreras-Martos S, Nguyen HH, Nguyen PN, Hristozova N, Macossay-Castillo M, Kovacs D, Bekesi A, Oemig JS, Maes D, Pauwels K, Tompa P, Lebrun P. Quantification of Intrinsically Disordered Proteins: A Problem Not Fully Appreciated. Frontiers in Molecular Biosciences. 5: 83. PMID 30234128 DOI: 10.3389/fmolb.2018.00083  0.378
2018 Lazar T, Guharoy M, Schad E, Tompa P. Unique Physicochemical Patterns of Residues in Protein-Protein Interfaces. Journal of Chemical Information and Modeling. PMID 30212197 DOI: 10.1021/acs.jcim.8b00270  0.838
2018 Lazar T, Guharoy M, Schad E, Tompa P. Unique Physicochemical Patterns of Residues in Protein-Protein Interfaces. Journal of Chemical Information and Modeling. PMID 30212197 DOI: 10.1021/acs.jcim.8b00270  0.838
2018 Guharoy M, Lazar T, Tompa P. Disordered substrates of the 20S proteasome link degradation with phase separation. Proteomics. e1800276. PMID 30070766 DOI: 10.1002/pmic.201800276  0.844
2018 Guharoy M, Lazar T, Tompa P. Disordered substrates of the 20S proteasome link degradation with phase separation. Proteomics. e1800276. PMID 30070766 DOI: 10.1002/pmic.201800276  0.844
2018 Boeynaems S, Alberti S, Fawzi NL, Mittag T, Polymenidou M, Rousseau F, Schymkowitz J, Shorter J, Wolozin B, Van Den Bosch L, Tompa P, Fuxreiter M. Protein Phase Separation: A New Phase in Cell Biology. Trends in Cell Biology. PMID 29602697 DOI: 10.1016/J.Tcb.2018.02.004  0.335
2018 Boeynaems S, Alberti S, Fawzi NL, Mittag T, Polymenidou M, Rousseau F, Schymkowitz J, Shorter J, Wolozin B, Van Den Bosch L, Tompa P, Fuxreiter M. Protein Phase Separation: A New Phase in Cell Biology. Trends in Cell Biology. PMID 29602697 DOI: 10.1016/J.Tcb.2018.02.004  0.335
2018 Boeynaems S, Tompa P, Bosch LVD. Phasing in on the cell cycle. Cell Division. 13: 1-8. PMID 29416553 DOI: 10.1186/S13008-018-0034-4  0.314
2018 Boeynaems S, Tompa P, Bosch LVD. Phasing in on the cell cycle. Cell Division. 13: 1-8. PMID 29416553 DOI: 10.1186/S13008-018-0034-4  0.314
2018 Nguyen HH, Volkov AN, Vandenbussche G, Tompa P, Pauwels K. In vivo biotinylated calpastatin improves the affinity purification of human m-calpain. Protein Expression and Purification. PMID 29339216 DOI: 10.1016/j.pep.2018.01.002  0.41
2018 Nguyen HH, Volkov AN, Vandenbussche G, Tompa P, Pauwels K. In vivo biotinylated calpastatin improves the affinity purification of human m-calpain. Protein Expression and Purification. PMID 29339216 DOI: 10.1016/j.pep.2018.01.002  0.41
2018 Varadi M, De Baets G, Vranken WF, Tompa P, Pancsa R. AmyPro: a database of proteins with validated amyloidogenic regions. Nucleic Acids Research. 46: D387-D392. PMID 29040693 DOI: 10.1093/nar/gkx950  0.328
2018 Varadi M, De Baets G, Vranken WF, Tompa P, Pancsa R. AmyPro: a database of proteins with validated amyloidogenic regions. Nucleic Acids Research. 46: D387-D392. PMID 29040693 DOI: 10.1093/nar/gkx950  0.328
2018 Necci M, Piovesan D, Dosztányi Z, Tompa P, Tosatto SCE. A comprehensive assessment of long intrinsic protein disorder from the DisProt database. Bioinformatics (Oxford, England). 34: 445-452. PMID 28968848 DOI: 10.1093/bioinformatics/btx590  0.424
2018 Necci M, Piovesan D, Dosztányi Z, Tompa P, Tosatto SCE. A comprehensive assessment of long intrinsic protein disorder from the DisProt database. Bioinformatics (Oxford, England). 34: 445-452. PMID 28968848 DOI: 10.1093/bioinformatics/btx590  0.424
2018 Micsonai A, Murvai N, Bulyáki É, Szabó B, Wien F, Lee Y, Réfrégiers M, Goto Y, Tompa P, Han K, Tantos Á, Kardos J. Improved Structural Estimation of Disordered Proteins by CD Spectroscopy: Method Development and Application Biophysical Journal. 114. DOI: 10.1016/J.Bpj.2017.11.3213  0.308
2017 Bokor M, Tantos Á, Mészáros A, Jenei B, Haminda R, Tompa P, Tompa K. Molecular motions and interactions in aqueous solutions of thymosin-ß4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 29274195 DOI: 10.1002/cphc.201701187  0.835
2017 Piovesan D, Tabaro F, Paladin L, Necci M, Micetic I, Camilloni C, Davey N, Dosztányi Z, Mészáros B, Monzon AM, Parisi G, Schad E, Sormanni P, Tompa P, Vendruscolo M, et al. MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins. Nucleic Acids Research. PMID 29136219 DOI: 10.1093/Nar/Gkx1071  0.861
2017 Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P. Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. Scientific Reports. 7: 4676. PMID 28680062 DOI: 10.1038/s41598-017-04611-x  0.43
2017 Pauwels K, Lebrun P, Tompa P. To be disordered or not to be disordered: is that still a question for proteins in the cell? Cellular and Molecular Life Sciences : Cmls. PMID 28612216 DOI: 10.1007/s00018-017-2561-6  0.505
2017 Cedeño C, Pauwels K, Tompa P. Protein Delivery into Plant Cells: Toward Structural Biology. Frontiers in Plant Science. 8: 519. PMID 28469623 DOI: 10.3389/fpls.2017.00519  0.385
2017 Cedeño C, Pauwels K, Tompa P. Protein Delivery into Plant Cells: Toward Structural Biology. Frontiers in Plant Science. 8: 519. PMID 28469623 DOI: 10.3389/fpls.2017.00519  0.385
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  0.451
2017 Boeynaems S, Bogaert E, Kovacs D, Konijnenberg A, Timmerman E, Volkov A, Guharoy M, De Decker M, Jaspers T, Ryan VH, Janke AM, Baatsen P, Vercruysse T, Kolaitis RM, Daelemans D, ... ... Tompa P, et al. Phase Separation of C9orf72 Dipeptide Repeats Perturbs Stress Granule Dynamics. Molecular Cell. 65: 1044-1055.e5. PMID 28306503 DOI: 10.1016/J.Molcel.2017.02.013  0.795
2017 Cedeño C, Żerko S, Tompa P, Koźmiński W. H, N, C resonance assignment of plant dehydrin early response to dehydration 10 (ERD10). Biomolecular Nmr Assignments. 11: 127-131. PMID 28275980 DOI: 10.1007/s12104-017-9732-0  0.341
2017 Cedeño C, Żerko S, Tompa P, Koźmiński W. H, N, C resonance assignment of plant dehydrin early response to dehydration 10 (ERD10). Biomolecular Nmr Assignments. 11: 127-131. PMID 28275980 DOI: 10.1007/s12104-017-9732-0  0.341
2017 Tompa K, Bokor M, Ágner D, Iván D, Kovacs D, Verebélyi T, Tompa P. Hydrogen mobility and protein-water interaction in proteins of solid state. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 28066974 DOI: 10.1002/cphc.201601136  0.311
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, ... ... Tompa P, et al. DisProt 7.0: a major update of the database of disordered proteins. Nucleic Acids Research. PMID 27965415 DOI: 10.1093/Nar/Gkw1279  0.85
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, ... ... Tompa P, et al. DisProt 7.0: a major update of the database of disordered proteins. Nucleic Acids Research. PMID 27965415 DOI: 10.1093/Nar/Gkw1279  0.85
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, ... ... Tompa P, et al. DisProt 7.0: a major update of the database of disordered proteins. Nucleic Acids Research. PMID 27899601 DOI: 10.1093/Nar/Gkw1056  0.852
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, ... ... Tompa P, et al. DisProt 7.0: a major update of the database of disordered proteins. Nucleic Acids Research. PMID 27899601 DOI: 10.1093/Nar/Gkw1056  0.852
2016 Pancsa R, Tompa P. Coding Regions of Intrinsic Disorder Accommodate Parallel Functions. Trends in Biochemical Sciences. 41: 898-906. PMID 27647212 DOI: 10.1016/j.tibs.2016.08.009  0.405
2016 Pancsa R, Tompa P. Coding Regions of Intrinsic Disorder Accommodate Parallel Functions. Trends in Biochemical Sciences. 41: 898-906. PMID 27647212 DOI: 10.1016/j.tibs.2016.08.009  0.405
2016 Pancsa R, Tompa P. Essential functions linked with structural disorder in organisms of minimal genome. Biology Direct. 11: 45. PMID 27608806 DOI: 10.1186/s13062-016-0149-y  0.439
2016 Pancsa R, Tompa P. Essential functions linked with structural disorder in organisms of minimal genome. Biology Direct. 11: 45. PMID 27608806 DOI: 10.1186/s13062-016-0149-y  0.439
2016 Hristozova N, Tompa P, Kovacs D. A Novel Method for Assessing the Chaperone Activity of Proteins. Plos One. 11: e0161970. PMID 27564234 DOI: 10.1371/journal.pone.0161970  0.315
2016 Hristozova N, Tompa P, Kovacs D. A Novel Method for Assessing the Chaperone Activity of Proteins. Plos One. 11: e0161970. PMID 27564234 DOI: 10.1371/journal.pone.0161970  0.315
2016 Pancsa R, Macossay-Castillo M, Kosol S, Tompa P. Computational analysis of translational readthrough proteins in Drosophila and yeast reveals parallels to alternative splicing. Scientific Reports. 6: 32142. PMID 27561673 DOI: 10.1038/srep32142  0.455
2016 Pancsa R, Macossay-Castillo M, Kosol S, Tompa P. Computational analysis of translational readthrough proteins in Drosophila and yeast reveals parallels to alternative splicing. Scientific Reports. 6: 32142. PMID 27561673 DOI: 10.1038/srep32142  0.455
2016 Tompa P, Kim KH, Bokor M, Kamasa P, Tantos Á, Fritz B, Kim DH, Lee C, Verebélyi T, Tompa K. Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment. Bmb Reports. PMID 27418282 DOI: 10.5483/BMBRep.2016.49.9.037  0.817
2016 Braten O, Livneh I, Ziv T, Admon A, Kehat I, Caspi LH, Gonen H, Bercovich B, Godzik A, Jahandideh S, Jaroszewski L, Sommer T, Kwon YT, Guharoy M, Tompa P, et al. Numerous proteins with unique characteristics are degraded by the 26S proteasome following monoubiquitination. Proceedings of the National Academy of Sciences of the United States of America. PMID 27385826 DOI: 10.1073/Pnas.1608644113  0.821
2016 Lazar T, Schad E, Szabo B, Horvath T, Meszaros A, Tompa P, Tantos A. Intrinsic protein disorder in histone lysine methylation. Biology Direct. 11: 30. PMID 27356874 DOI: 10.1186/s13062-016-0129-2  0.849
2016 Lazar T, Schad E, Szabo B, Horvath T, Meszaros A, Tompa P, Tantos A. Intrinsic protein disorder in histone lysine methylation. Biology Direct. 11: 30. PMID 27356874 DOI: 10.1186/s13062-016-0129-2  0.849
2016 Smithers B, Oates ME, Tompa P, Gough J. Three reasons protein disorder analysis makes more sense in the light of collagen. Protein Science : a Publication of the Protein Society. 25: 1030-6. PMID 26941008 DOI: 10.1002/Pro.2913  0.465
2016 Guharoy M, Bhowmick P, Tompa P. Design Principles Involving Protein Disorder Facilitate Specific Substrate Selection and Degradation by the Ubiquitin-Proteasome System. The Journal of Biological Chemistry. 291: 6723-31. PMID 26851277 DOI: 10.1074/jbc.R115.692665  0.849
2016 Piai A, Calçada EO, Tarenzi T, Grande AD, Varadi M, Tompa P, Felli IC, Pierattelli R. Just a Flexible Linker? The Structural and Dynamic Properties of CBP-ID4 Revealed by NMR Spectroscopy. Biophysical Journal. 110: 372-381. PMID 26789760 DOI: 10.1016/j.bpj.2015.11.3516  0.426
2016 Piai A, Calçada EO, Tarenzi T, Grande AD, Varadi M, Tompa P, Felli IC, Pierattelli R. Just a Flexible Linker? The Structural and Dynamic Properties of CBP-ID4 Revealed by NMR Spectroscopy. Biophysical Journal. 110: 372-381. PMID 26789760 DOI: 10.1016/j.bpj.2015.11.3516  0.426
2016 Guharoy M, Bhowmick P, Sallam M, Tompa P. Tripartite degrons confer diversity and specificity on regulated protein degradation in the ubiquitin-proteasome system. Nature Communications. 7: 10239. PMID 26732515 DOI: 10.1038/ncomms10239  0.85
2016 Guharoy M, Bhowmick P, Sallam M, Tompa P. Tripartite degrons confer diversity and specificity on regulated protein degradation in the ubiquitin-proteasome system. Nature Communications. 7: 10239. PMID 26732515 DOI: 10.1038/ncomms10239  0.85
2016 Pancsa R, Varadi M, Tompa P, Vranken WF. Start2Fold: a database of hydrogen/deuterium exchange data on protein folding and stability. Nucleic Acids Research. 44: D429-34. PMID 26582925 DOI: 10.1093/nar/gkv1185  0.382
2016 Pancsa R, Varadi M, Tompa P, Vranken WF. Start2Fold: a database of hydrogen/deuterium exchange data on protein folding and stability. Nucleic Acids Research. 44: D429-34. PMID 26582925 DOI: 10.1093/nar/gkv1185  0.382
2015 Aouacheria A, Combet C, Tompa P, Hardwick JM. Redefining the BH3 Death Domain as a 'Short Linear Motif'. Trends in Biochemical Sciences. 40: 736-48. PMID 26541461 DOI: 10.1016/J.Tibs.2015.09.007  0.405
2015 Varadi M, Zsolyomi F, Guharoy M, Tompa P. Functional Advantages of Conserved Intrinsic Disorder in RNA-Binding Proteins. Plos One. 10: e0139731. PMID 26439842 DOI: 10.1371/journal.pone.0139731  0.85
2015 Varadi M, Zsolyomi F, Guharoy M, Tompa P. Functional Advantages of Conserved Intrinsic Disorder in RNA-Binding Proteins. Plos One. 10: e0139731. PMID 26439842 DOI: 10.1371/journal.pone.0139731  0.427
2015 Borysik AJ, Kovacs D, Guharoy M, Tompa P. Ensemble Methods Enable a New Definition for the Solution to Gas-Phase Transfer of Intrinsically Disordered Proteins. Journal of the American Chemical Society. 137: 13807-17. PMID 26437245 DOI: 10.1021/jacs.5b06027  0.816
2015 Tompa P, Schad E, Tantos A, Kalmar L. Intrinsically disordered proteins: emerging interaction specialists. Current Opinion in Structural Biology. 35: 49-59. PMID 26402567 DOI: 10.1016/j.sbi.2015.08.009  0.855
2015 Tompa P, Schad E, Tantos A, Kalmar L. Intrinsically disordered proteins: emerging interaction specialists. Current Opinion in Structural Biology. 35: 49-59. PMID 26402567 DOI: 10.1016/j.sbi.2015.08.009  0.486
2015 Varadi M, Tompa P. The Protein Ensemble Database. Advances in Experimental Medicine and Biology. 870: 335-49. PMID 26387108 DOI: 10.1007/978-3-319-20164-1_11  0.401
2015 Varadi M, Tompa P. The Protein Ensemble Database. Advances in Experimental Medicine and Biology. 870: 335-49. PMID 26387108 DOI: 10.1007/978-3-319-20164-1_11  0.401
2015 Bhowmick P, Guharoy M, Tompa P. Bioinformatics Approaches for Predicting Disordered Protein Motifs. Advances in Experimental Medicine and Biology. 870: 291-318. PMID 26387106 DOI: 10.1007/978-3-319-20164-1_9  0.85
2015 Varadi M, Vranken W, Guharoy M, Tompa P. Computational approaches for inferring the functions of intrinsically disordered proteins. Frontiers in Molecular Biosciences. 2: 45. PMID 26301226 DOI: 10.3389/fmolb.2015.00045  0.868
2015 Varadi M, Vranken W, Guharoy M, Tompa P. Computational approaches for inferring the functions of intrinsically disordered proteins. Frontiers in Molecular Biosciences. 2: 45. PMID 26301226 DOI: 10.3389/fmolb.2015.00045  0.498
2015 Tusnády GE, Dobson L, Tompa P. Disordered regions in transmembrane proteins. Biochimica Et Biophysica Acta. 1848: 2839-48. PMID 26275590 DOI: 10.1016/j.bbamem.2015.08.002  0.49
2015 Tusnády GE, Dobson L, Tompa P. Disordered regions in transmembrane proteins. Biochimica Et Biophysica Acta. 1848: 2839-48. PMID 26275590 DOI: 10.1016/j.bbamem.2015.08.002  0.49
2015 Guharoy M, Pauwels K, Tompa P. SnapShot: Intrinsic Structural Disorder. Cell. 161: 1230-1230.e1. PMID 26000490 DOI: 10.1016/j.cell.2015.05.024  0.87
2015 Guharoy M, Pauwels K, Tompa P. SnapShot: Intrinsic Structural Disorder. Cell. 161: 1230-1230.e1. PMID 26000490 DOI: 10.1016/j.cell.2015.05.024  0.506
2015 Tantos A, Kalmar L, Tompa P. The role of structural disorder in cell cycle regulation, related clinical proteomics, disease development and drug targeting. Expert Review of Proteomics. 12: 221-33. PMID 25976105 DOI: 10.1586/14789450.2015.1042866  0.837
2015 Tantos A, Kalmar L, Tompa P. The role of structural disorder in cell cycle regulation, related clinical proteomics, disease development and drug targeting. Expert Review of Proteomics. 12: 221-33. PMID 25976105 DOI: 10.1586/14789450.2015.1042866  0.384
2015 Varadi M, Guharoy M, Zsolyomi F, Tompa P. DisCons: a novel tool to quantify and classify evolutionary conservation of intrinsic protein disorder. Bmc Bioinformatics. 16: 153. PMID 25968230 DOI: 10.1186/s12859-015-0592-2  0.856
2015 Varadi M, Guharoy M, Zsolyomi F, Tompa P. DisCons: a novel tool to quantify and classify evolutionary conservation of intrinsic protein disorder. Bmc Bioinformatics. 16: 153. PMID 25968230 DOI: 10.1186/s12859-015-0592-2  0.452
2014 Macossay-Castillo M, Kosol S, Tompa P, Pancsa R. Synonymous constraint elements show a tendency to encode intrinsically disordered protein segments. Plos Computational Biology. 10: e1003607. PMID 24809503 DOI: 10.1371/journal.pcbi.1003607  0.423
2014 Macossay-Castillo M, Kosol S, Tompa P, Pancsa R. Synonymous constraint elements show a tendency to encode intrinsically disordered protein segments. Plos Computational Biology. 10: e1003607. PMID 24809503 DOI: 10.1371/journal.pcbi.1003607  0.423
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, et al. Classification of intrinsically disordered regions and proteins. Chemical Reviews. 114: 6589-631. PMID 24773235 DOI: 10.1021/Cr400525M  0.377
2014 Szöllősi D, Horváth T, Han KH, Dokholyan NV, Tompa P, Kalmár L, Hegedűs T. Discrete molecular dynamics can predict helical prestructured motifs in disordered proteins. Plos One. 9: e95795. PMID 24763499 DOI: 10.1371/journal.pone.0095795  0.778
2014 Habchi J, Tompa P, Longhi S, Uversky VN. Introducing protein intrinsic disorder. Chemical Reviews. 114: 6561-88. PMID 24739139 DOI: 10.1021/Cr400514H  0.49
2014 Cilia E, Pancsa R, Tompa P, Lenaerts T, Vranken WF. The DynaMine webserver: predicting protein dynamics from sequence. Nucleic Acids Research. 42: W264-70. PMID 24728994 DOI: 10.1093/nar/gku270  0.357
2014 Tompa P. Multisteric regulation by structural disorder in modular signaling proteins: an extension of the concept of allostery. Chemical Reviews. 114: 6715-32. PMID 24533462 DOI: 10.1021/cr4005082  0.426
2014 Tompa P. Multisteric regulation by structural disorder in modular signaling proteins: an extension of the concept of allostery. Chemical Reviews. 114: 6715-32. PMID 24533462 DOI: 10.1021/cr4005082  0.426
2014 Tompa P, Varadi M. Predicting the predictive power of IDP ensembles. Structure (London, England : 1993). 22: 177-8. PMID 24507778 DOI: 10.1016/j.str.2014.01.003  0.321
2014 Tompa P, Varadi M. Predicting the predictive power of IDP ensembles. Structure (London, England : 1993). 22: 177-8. PMID 24507778 DOI: 10.1016/j.str.2014.01.003  0.321
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  0.726
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, ... ... Tompa P, 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  0.388
2013 Tantos A, Szabo B, Lang A, Varga Z, Tsylonok M, Bokor M, Verebelyi T, Kamasa P, Tompa K, Perczel A, Buday L, Lee SH, Choo Y, Han KH, Tompa P. Multiple fuzzy interactions in the moonlighting function of thymosin-β4. Intrinsically Disordered Proteins. 1: e26204. PMID 28516021 DOI: 10.4161/idp.26204  0.831
2013 Tompa K, Bokor M, Han KH, Tompa P. Hydrogen skeleton, mobility and protein architecture. Intrinsically Disordered Proteins. 1: e25767. PMID 28516019 DOI: 10.4161/idp.25767  0.317
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  0.775
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  0.775
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, ... ... Tompa P, 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  0.498
2013 Cilia E, Pancsa R, Tompa P, Lenaerts T, Vranken WF. From protein sequence to dynamics and disorder with DynaMine. Nature Communications. 4: 2741. PMID 24225580 DOI: 10.1038/ncomms3741  0.477
2013 Song J, Ng SC, Tompa P, Lee KA, Chan HS. Polycation-π interactions are a driving force for molecular recognition by an intrinsically disordered oncoprotein family. Plos Computational Biology. 9: e1003239. PMID 24086122 DOI: 10.1371/Journal.Pcbi.1003239  0.378
2013 Kosol S, Contreras-Martos S, Cedeño C, Tompa P. Structural characterization of intrinsically disordered proteins by NMR spectroscopy. Molecules (Basel, Switzerland). 18: 10802-28. PMID 24008243 DOI: 10.3390/molecules180910802  0.373
2013 Pietrosemoli N, Pancsa R, Tompa P. Structural disorder provides increased adaptability for vesicle trafficking pathways. Plos Computational Biology. 9: e1003144. PMID 23874186 DOI: 10.1371/Journal.Pcbi.1003144  0.473
2013 Guharoy M, Szabo B, Contreras Martos S, Kosol S, Tompa P. Intrinsic structural disorder in cytoskeletal proteins. Cytoskeleton (Hoboken, N.J.). 70: 550-71. PMID 23761374 DOI: 10.1002/cm.21118  0.835
2013 Guharoy M, Szabo B, Contreras Martos S, Kosol S, Tompa P. Intrinsic structural disorder in cytoskeletal proteins. Cytoskeleton (Hoboken, N.J.). 70: 550-71. PMID 23761374 DOI: 10.1002/cm.21118  0.368
2013 Bhowmick P, Pancsa R, Guharoy M, Tompa P. Functional diversity and structural disorder in the human ubiquitination pathway. Plos One. 8: e65443. PMID 23734257 DOI: 10.1371/journal.pone.0065443  0.825
2013 Bánóczi Z, Tantos Á, Farkas A, Majer Z, Dókus LE, Tompa P, Hudecz F. New m-calpain substrate-based azapeptide inhibitors. Journal of Peptide Science : An Official Publication of the European Peptide Society. 19: 370-6. PMID 23613308 DOI: 10.1002/psc.2511  0.776
2013 Schad E, Kalmar L, Tompa P. Exon-phase symmetry and intrinsic structural disorder promote modular evolution in the human genome. Nucleic Acids Research. 41: 4409-22. PMID 23460204 DOI: 10.1093/nar/gkt110  0.847
2013 Schad E, Kalmar L, Tompa P. Exon-phase symmetry and intrinsic structural disorder promote modular evolution in the human genome. Nucleic Acids Research. 41: 4409-22. PMID 23460204 DOI: 10.1093/nar/gkt110  0.429
2013 Kovacs D, Szabo B, Pancsa R, Tompa P. Intrinsically disordered proteins undergo and assist folding transitions in the proteome. Archives of Biochemistry and Biophysics. 531: 80-9. PMID 23142500 DOI: 10.1016/j.abb.2012.09.010  0.463
2013 Tantos A, Szrnka K, Szabo B, Bokor M, Kamasa P, Matus P, Bekesi A, Tompa K, Han KH, Tompa P. Structural disorder and local order of hNopp140. Biochimica Et Biophysica Acta. 1834: 342-50. PMID 22906532 DOI: 10.1016/j.bbapap.2012.08.005  0.86
2013 Tantos A, Szrnka K, Szabo B, Bokor M, Kamasa P, Matus P, Bekesi A, Tompa K, Han KH, Tompa P. Structural disorder and local order of hNopp140. Biochimica Et Biophysica Acta. 1834: 342-50. PMID 22906532 DOI: 10.1016/j.bbapap.2012.08.005  0.465
2012 Tompa P. Intrinsically disordered proteins: a 10-year recap. Trends in Biochemical Sciences. 37: 509-16. PMID 22989858 DOI: 10.1016/j.tibs.2012.08.004  0.414
2012 Tompa P. Intrinsically disordered proteins: a 10-year recap. Trends in Biochemical Sciences. 37: 509-16. PMID 22989858 DOI: 10.1016/j.tibs.2012.08.004  0.414
2012 Kovacs D, Tompa P. Diverse functional manifestations of intrinsic structural disorder in molecular chaperones. Biochemical Society Transactions. 40: 963-8. PMID 22988848 DOI: 10.1042/BST20120108  0.472
2012 Kalmar L, Acs V, Silhavy D, Tompa P. Long-range interactions in nonsense-mediated mRNA decay are mediated by intrinsically disordered protein regions. Journal of Molecular Biology. 424: 125-31. PMID 22971338 DOI: 10.1016/j.jmb.2012.09.002  0.713
2012 Kalmar L, Acs V, Silhavy D, Tompa P. Long-range interactions in nonsense-mediated mRNA decay are mediated by intrinsically disordered protein regions. Journal of Molecular Biology. 424: 125-31. PMID 22971338 DOI: 10.1016/j.jmb.2012.09.002  0.713
2012 Tantos A, Tompa P. Proteomic methods for the identification of intrinsically disordered proteins. Methods in Molecular Biology (Clifton, N.J.). 896: 429-37. PMID 22821542 DOI: 10.1007/978-1-4614-3704-8_29  0.865
2012 Tantos A, Tompa P. Proteomic methods for the identification of intrinsically disordered proteins. Methods in Molecular Biology (Clifton, N.J.). 896: 429-37. PMID 22821542 DOI: 10.1007/978-1-4614-3704-8_29  0.488
2012 Tantos A, Tompa P. Identification of intrinsically disordered proteins by a special 2D electrophoresis. Methods in Molecular Biology (Clifton, N.J.). 896: 215-22. PMID 22821526 DOI: 10.1007/978-1-4614-3704-8_13  0.849
2012 Tantos A, Tompa P. Identification of intrinsically disordered proteins by a special 2D electrophoresis. Methods in Molecular Biology (Clifton, N.J.). 896: 215-22. PMID 22821526 DOI: 10.1007/978-1-4614-3704-8_13  0.423
2012 Tompa P. On the supertertiary structure of proteins. Nature Chemical Biology. 8: 597-600. PMID 22710296 DOI: 10.1038/nchembio.1009  0.354
2012 Tompa P. On the supertertiary structure of proteins. Nature Chemical Biology. 8: 597-600. PMID 22710296 DOI: 10.1038/nchembio.1009  0.354
2012 Kalmar L, Homola D, Varga G, Tompa P. Structural disorder in proteins brings order to crystal growth in biomineralization. Bone. 51: 528-34. PMID 22634174 DOI: 10.1016/J.Bone.2012.05.009  0.8
2012 Kalmar L, Homola D, Varga G, Tompa P. Structural disorder in proteins brings order to crystal growth in biomineralization. Bone. 51: 528-34. PMID 22634174 DOI: 10.1016/J.Bone.2012.05.009  0.8
2012 Pancsa R, Tompa P. Structural disorder in eukaryotes. Plos One. 7: e34687. PMID 22496841 DOI: 10.1371/journal.pone.0034687  0.431
2012 Fuxreiter M, Tompa P. Fuzzy complexes: a more stochastic view of protein function. Advances in Experimental Medicine and Biology. 725: 1-14. PMID 22399315 DOI: 10.1007/978-1-4614-0659-4_1  0.43
2012 Hegyi H, Tompa P. Increased structural disorder of proteins encoded on human sex chromosomes. Molecular Biosystems. 8: 229-36. PMID 22105808 DOI: 10.1039/c1mb05285c  0.367
2012 Tantos A, Han KH, Tompa P. Intrinsic disorder in cell signaling and gene transcription. Molecular and Cellular Endocrinology. 348: 457-65. PMID 21782886 DOI: 10.1016/j.mce.2011.07.015  0.861
2012 Tantos A, Han KH, Tompa P. Intrinsic disorder in cell signaling and gene transcription. Molecular and Cellular Endocrinology. 348: 457-65. PMID 21782886 DOI: 10.1016/j.mce.2011.07.015  0.469
2012 Tompa P, Han K. Intrinsically disordered proteins Physics Today. 65: 64-65. DOI: 10.1063/PT.3.1689  0.49
2011 Schad E, Tompa P, Hegyi H. The relationship between proteome size, structural disorder and organism complexity. Genome Biology. 12: R120. PMID 22182830 DOI: 10.1186/gb-2011-12-12-r120  0.849
2011 Szasz CS, Alexa A, Toth K, Rakacs M, Langowski J, Tompa P. Protein disorder prevails under crowded conditions. Biochemistry. 50: 5834-44. PMID 21634433 DOI: 10.1021/bi200365j  0.422
2011 Tompa P. Unstructural biology coming of age. Current Opinion in Structural Biology. 21: 419-25. PMID 21514142 DOI: 10.1016/j.sbi.2011.03.012  0.419
2011 Tompa P. Unstructural biology coming of age. Current Opinion in Structural Biology. 21: 419-25. PMID 21514142 DOI: 10.1016/j.sbi.2011.03.012  0.419
2011 Szalainé Ágoston B, Kovács D, Tompa P, Perczel A. Full backbone assignment and dynamics of the intrinsically disordered dehydrin ERD14. Biomolecular Nmr Assignments. 5: 189-93. PMID 21336827 DOI: 10.1007/s12104-011-9297-2  0.396
2011 Hegyi H, Kalmar L, Horvath T, Tompa P. Verification of alternative splicing variants based on domain integrity, truncation length and intrinsic protein disorder. Nucleic Acids Research. 39: 1208-19. PMID 20972208 DOI: 10.1093/nar/gkq843  0.758
2011 Hegyi H, Kalmar L, Horvath T, Tompa P. Verification of alternative splicing variants based on domain integrity, truncation length and intrinsic protein disorder. Nucleic Acids Research. 39: 1208-19. PMID 20972208 DOI: 10.1093/nar/gkq843  0.758
2010 Buday L, Tompa P. Accessory proteins in signal transduction: scaffold proteins and beyond. The Febs Journal. 277: 4347. PMID 21069901 DOI: 10.1111/J.1742-4658.2010.07863.X  0.321
2010 Buday L, Tompa P. Functional classification of scaffold proteins and related molecules. The Febs Journal. 277: 4348-55. PMID 20883491 DOI: 10.1111/J.1742-4658.2010.07864.X  0.403
2010 Tompa P, Kalmar L. Power law distribution defines structural disorder as a structural element directly linked with function. Journal of Molecular Biology. 403: 346-50. PMID 20816987 DOI: 10.1016/j.jmb.2010.07.044  0.383
2010 Tompa P, Kalmar L. Power law distribution defines structural disorder as a structural element directly linked with function. Journal of Molecular Biology. 403: 346-50. PMID 20816987 DOI: 10.1016/j.jmb.2010.07.044  0.742
2010 Burra PV, Kalmar L, Tompa P. Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes. Plos One. 5: e12069. PMID 20711457 DOI: 10.1371/journal.pone.0012069  0.772
2010 Burra PV, Kalmar L, Tompa P. Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes. Plos One. 5: e12069. PMID 20711457 DOI: 10.1371/journal.pone.0012069  0.456
2010 Tompa P, Kovacs D. Intrinsically disordered chaperones in plants and animals. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 88: 167-74. PMID 20453919 DOI: 10.1139/o09-163  0.475
2010 Kovacs E, Tompa P, Liliom K, Kalmar L. Dual coding in alternative reading frames correlates with intrinsic protein disorder. Proceedings of the National Academy of Sciences of the United States of America. 107: 5429-34. PMID 20212158 DOI: 10.1073/pnas.0907841107  0.763
2010 Kovacs E, Tompa P, Liliom K, Kalmar L. Dual coding in alternative reading frames correlates with intrinsic protein disorder. Proceedings of the National Academy of Sciences of the United States of America. 107: 5429-34. PMID 20212158 DOI: 10.1073/pnas.0907841107  0.434
2010 Uversky VN, Cortese MS, Tompa P, Csizmok V, Dunker AK. Large-Scale Identification of Intrinsically Disordered Proteins Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation. 671-693. DOI: 10.1002/9780470602614.ch23  0.403
2009 Hegyi H, Buday L, Tompa P. Intrinsic structural disorder confers cellular viability on oncogenic fusion proteins. Plos Computational Biology. 5: e1000552. PMID 19888473 DOI: 10.1371/Journal.Pcbi.1000552  0.443
2009 Tompa P. Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins. The Febs Journal. 276: 5406-15. PMID 19712107 DOI: 10.1111/j.1742-4658.2009.07250.x  0.362
2009 Balázs A, Csizmok V, Buday L, Rakács M, Kiss R, Bokor M, Udupa R, Tompa K, Tompa P. High levels of structural disorder in scaffold proteins as exemplified by a novel neuronal protein, CASK-interactive protein1. The Febs Journal. 276: 3744-56. PMID 19523119 DOI: 10.1111/J.1742-4658.2009.07090.X  0.51
2009 Hazy E, Tompa P. Limitations of induced folding in molecular recognition by intrinsically disordered proteins. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 10: 1415-9. PMID 19462392 DOI: 10.1002/cphc.200900205  0.448
2009 Hazy E, Tompa P. Limitations of induced folding in molecular recognition by intrinsically disordered proteins. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 10: 1415-9. PMID 19462392 DOI: 10.1002/cphc.200900205  0.448
2009 Bermel W, Bertini I, Csizmok V, Felli IC, Pierattelli R, Tompa P. H-start for exclusively heteronuclear NMR spectroscopy: the case of intrinsically disordered proteins. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 198: 275-81. PMID 19307141 DOI: 10.1016/J.Jmr.2009.02.012  0.332
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  0.469
2009 Tantos A, Friedrich P, Tompa P. Cold stability of intrinsically disordered proteins. Febs Letters. 583: 465-9. PMID 19121309 DOI: 10.1016/J.Febslet.2008.12.054  0.857
2009 Kovacs D, Rakacs M, Agoston B, Lenkey K, Semrad K, Schroeder R, Tompa P. Janus chaperones: assistance of both RNA- and protein-folding by ribosomal proteins. Febs Letters. 583: 88-92. PMID 19071121 DOI: 10.1016/j.febslet.2008.11.049  0.391
2008 Kovacs D, Agoston B, Tompa P. Disordered plant LEA proteins as molecular chaperones. Plant Signaling & Behavior. 3: 710-3. PMID 19704836  0.407
2008 Csizmok V, Felli IC, Tompa P, Banci L, Bertini I. Structural and dynamic characterization of intrinsically disordered human securin by NMR spectroscopy Journal of the American Chemical Society. 130: 16873-16879. PMID 19053469 DOI: 10.1021/Ja805510B  0.319
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  0.337
2008 Albà MM, Tompa P, Veitia RA. Amino acid repeats and the structure and evolution of proteins. Genome Dynamics. 3: 119-130. PMID 18753788 DOI: 10.1159/000107607  0.358
2008 Dosztányi Z, Tompa P. Prediction of protein disorder. Methods in Molecular Biology (Clifton, N.J.). 426: 103-15. PMID 18542859 DOI: 10.1007/978-1-60327-058-8_6  0.485
2008 Dosztányi Z, Tompa P. Prediction of protein disorder. Methods in Molecular Biology (Clifton, N.J.). 426: 103-15. PMID 18542859 DOI: 10.1007/978-1-60327-058-8_6  0.485
2008 Kiss R, Bozoky Z, Kovács D, Róna G, Friedrich P, Dvortsák P, Weisemann R, Weisemann R, Tompa P, Perczel A. Calcium-induced tripartite binding of intrinsically disordered calpastatin to its cognate enzyme, calpain. Febs Letters. 582: 2149-54. PMID 18519038 DOI: 10.1016/J.Febslet.2008.05.032  0.65
2008 Szollosi E, Bokor M, Bodor A, Perczel A, Klement E, Medzihradszky KF, Tompa K, Tompa P. Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities. Journal of Proteome Research. 7: 2291-9. PMID 18484763 DOI: 10.1021/pr700720c  0.495
2008 Szollosi E, Bokor M, Bodor A, Perczel A, Klement E, Medzihradszky KF, Tompa K, Tompa P. Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities. Journal of Proteome Research. 7: 2291-9. PMID 18484763 DOI: 10.1021/pr700720c  0.495
2008 Tusnády GE, Kalmár L, Hegyi H, Tompa P, Simon I. TOPDOM: database of domains and motifs with conservative location in transmembrane proteins. Bioinformatics (Oxford, England). 24: 1469-70. PMID 18434342 DOI: 10.1093/bioinformatics/btn202  0.69
2008 Hegyi H, Tompa P. Intrinsically disordered proteins display no preference for chaperone binding in vivo. Plos Computational Biology. 4: e1000017. PMID 18369417 DOI: 10.1371/journal.pcbi.1000017  0.489
2008 Kovacs D, Kalmar E, Torok Z, Tompa P. Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. Plant Physiology. 147: 381-90. PMID 18359842 DOI: 10.1104/pp.108.118208  0.407
2008 Tompa P, Fuxreiter M. Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends in Biochemical Sciences. 33: 2-8. PMID 18054235 DOI: 10.1016/j.tibs.2007.10.003  0.499
2008 Tompa P, Fuxreiter M. Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends in Biochemical Sciences. 33: 2-8. PMID 18054235 DOI: 10.1016/j.tibs.2007.10.003  0.499
2008 Tompa P, Prilusky J, Silman I, Sussman JL. Structural disorder serves as a weak signal for intracellular protein degradation Proteins: Structure, Function and Genetics. 71: 903-909. PMID 18004785 DOI: 10.1002/Prot.21773  0.518
2008 Kiss R, Bozoky Z, Kovács D, Róna G, Friedrich P, Dvortsák P, Weisemann R, Tompa P, Perczel A. Corrigendum to “Calcium‐induced tripartite binding of intrinsically disordered calpastatin to its cognate enzyme, calpain” [FEBS Lett. 582 (2008) 2149–2154] Febs Letters. 582: 2816-2816. DOI: 10.1016/J.Febslet.2008.06.032  0.664
2007 Hegyi H, Schad E, Tompa P. Structural disorder promotes assembly of protein complexes. Bmc Structural Biology. 7: 65. PMID 17922903 DOI: 10.1186/1472-6807-7-65  0.852
2007 Mészáros B, Tompa P, Simon I, Dosztányi Z. Molecular principles of the interactions of disordered proteins. Journal of Molecular Biology. 372: 549-61. PMID 17681540 DOI: 10.1016/j.jmb.2007.07.004  0.446
2007 Mészáros B, Tompa P, Simon I, Dosztányi Z. Molecular principles of the interactions of disordered proteins. Journal of Molecular Biology. 372: 549-61. PMID 17681540 DOI: 10.1016/j.jmb.2007.07.004  0.446
2007 Csizmók V, Dosztányi Z, Simon I, Tompa P. Towards proteomic approaches for the identification of structural disorder. Current Protein & Peptide Science. 8: 173-9. PMID 17430198 DOI: 10.2174/138920307780363479  0.447
2007 Csizmók V, Dosztányi Z, Simon I, Tompa P. Towards proteomic approaches for the identification of structural disorder. Current Protein & Peptide Science. 8: 173-9. PMID 17430198 DOI: 10.2174/138920307780363479  0.447
2007 Dosztányi Z, Sándor M, Tompa P, Simon I. Prediction of protein disorder at the domain level. Current Protein & Peptide Science. 8: 161-71. PMID 17430197 DOI: 10.2174/138920307780363406  0.484
2007 Dosztányi Z, Sándor M, Tompa P, Simon I. Prediction of protein disorder at the domain level. Current Protein & Peptide Science. 8: 161-71. PMID 17430197 DOI: 10.2174/138920307780363406  0.484
2007 Fuxreiter M, Tompa P, Simon I. Local structural disorder imparts plasticity on linear motifs. Bioinformatics (Oxford, England). 23: 950-6. PMID 17387114 DOI: 10.1093/bioinformatics/btm035  0.431
2007 Fuxreiter M, Tompa P, Simon I. Local structural disorder imparts plasticity on linear motifs. Bioinformatics (Oxford, England). 23: 950-6. PMID 17387114 DOI: 10.1093/bioinformatics/btm035  0.431
2007 Banóczi Z, Tantos A, Farkas A, Tompa P, Friedrich P, Hudecz F. Synthesis of cell-penetrating conjugates of calpain activator peptides. Bioconjugate Chemistry. 18: 130-7. PMID 17226965 DOI: 10.1021/Bc0601976  0.771
2007 Sickmeier M, Hamilton JA, LeGall T, Vacic V, Cortese MS, Tantos A, Szabo B, Tompa P, Chen J, Uversky VN, Obradovic Z, Dunker AK. DisProt: the Database of Disordered Proteins. Nucleic Acids Research. 35: D786-93. PMID 17145717 DOI: 10.1093/Nar/Gkl893  0.88
2006 Dosztányi Z, Chen J, Dunker AK, Simon I, Tompa P. Disorder and sequence repeats in hub proteins and their implications for network evolution. Journal of Proteome Research. 5: 2985-95. PMID 17081050 DOI: 10.1021/Pr060171O  0.406
2006 Tompa P, Dosztanyi Z, Simon I. Prevalent structural disorder in E. coli and S. cerevisiae proteomes. Journal of Proteome Research. 5: 1996-2000. PMID 16889422 DOI: 10.1021/pr0600881  0.467
2006 Tompa P, Dosztanyi Z, Simon I. Prevalent structural disorder in E. coli and S. cerevisiae proteomes. Journal of Proteome Research. 5: 1996-2000. PMID 16889422 DOI: 10.1021/pr0600881  0.467
2006 Tompa P, Bánki P, Bokor M, Kamasa P, Kovács D, Lasanda G, Tompa K. Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects. Biophysical Journal. 91: 2243-9. PMID 16798808 DOI: 10.1529/biophysj.106.084723  0.316
2006 Kókai E, Tantos A, Vissi E, Szöor B, Tompa P, Gausz J, Alphey L, Friedrich P, Dombrádi V. CG15031/PPYR1 is an intrinsically unstructured protein that interacts with protein phosphatase Y. Archives of Biochemistry and Biophysics. 451: 59-67. PMID 16631104 DOI: 10.1016/J.Abb.2006.03.020  0.839
2006 Csizmók V, Szollosi E, Friedrich P, Tompa P. A novel two-dimensional electrophoresis technique for the identification of intrinsically unstructured proteins. Molecular & Cellular Proteomics : McP. 5: 265-73. PMID 16223749 DOI: 10.1074/Mcp.M500181-Mcp200  0.698
2006 Csizmók V, Szollosi E, Friedrich P, Tompa P. A novel two-dimensional electrophoresis technique for the identification of intrinsically unstructured proteins. Molecular & Cellular Proteomics : McP. 5: 265-73. PMID 16223749 DOI: 10.1074/Mcp.M500181-Mcp200  0.698
2005 Tompa P, Szász C, Buday L. Structural disorder throws new light on moonlighting. Trends in Biochemical Sciences. 30: 484-9. PMID 16054818 DOI: 10.1016/J.Tibs.2005.07.008  0.427
2005 Dosztányi Z, Csizmok V, Tompa P, Simon I. IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics (Oxford, England). 21: 3433-4. PMID 15955779 DOI: 10.1093/bioinformatics/bti541  0.338
2005 Dosztányi Z, Csizmok V, Tompa P, Simon I. IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics (Oxford, England). 21: 3433-4. PMID 15955779 DOI: 10.1093/bioinformatics/bti541  0.338
2005 Tompa P. The interplay between structure and function in intrinsically unstructured proteins. Febs Letters. 579: 3346-54. PMID 15943980 DOI: 10.1016/j.febslet.2005.03.072  0.436
2005 Dosztányi Z, Csizmók V, Tompa P, Simon I. The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. Journal of Molecular Biology. 347: 827-39. PMID 15769473 DOI: 10.1016/J.JMB.2005.01.071  0.428
2005 Csizmók V, Bokor M, Bánki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P. Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2. Biochemistry. 44: 3955-64. PMID 15751971 DOI: 10.1021/Bi047817F  0.7
2005 Csizmók V, Bokor M, Bánki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P. Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2. Biochemistry. 44: 3955-64. PMID 15751971 DOI: 10.1021/Bi047817F  0.7
2005 Bokor M, Csizmók V, Kovács D, Bánki P, Friedrich P, Tompa P, Tompa K. NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins. Biophysical Journal. 88: 2030-7. PMID 15613629 DOI: 10.1529/Biophysj.104.051912  0.708
2005 Bokor M, Csizmók V, Kovács D, Bánki P, Friedrich P, Tompa P, Tompa K. NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins. Biophysical Journal. 88: 2030-7. PMID 15613629 DOI: 10.1529/Biophysj.104.051912  0.708
2005 Bozóky Z, Alexa A, Tompa P, Friedrich P. Multiple interactions of the 'transducer' govern its function in calpain activation by Ca2+. The Biochemical Journal. 388: 741-4. PMID 15569003 DOI: 10.1042/Bj20041935  0.603
2005 Bozóky Z, Alexa A, Tompa P, Friedrich P. Multiple interactions of the 'transducer' govern its function in calpain activation by Ca2+. The Biochemical Journal. 388: 741-4. PMID 15569003 DOI: 10.1042/Bj20041935  0.603
2004 Friedrich P, Tompa P, Farkas A. The calpain-system of Drosophila melanogaster: coming of age. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 26: 1088-96. PMID 15382138 DOI: 10.1002/Bies.20106  0.622
2004 Friedrich P, Tompa P, Farkas A. The calpain-system of Drosophila melanogaster: coming of age. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 26: 1088-96. PMID 15382138 DOI: 10.1002/Bies.20106  0.622
2004 Tompa P, Csermely P. The role of structural disorder in the function of RNA and protein chaperones. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 18: 1169-75. PMID 15284216 DOI: 10.1096/Fj.04-1584Rev  0.485
2004 Farkas A, Nardai G, Csermely P, Tompa P, Friedrich P. DUK114, the Drosophila orthologue of bovine brain calpain activator protein, is a molecular chaperone. The Biochemical Journal. 383: 165-70. PMID 15250825 DOI: 10.1042/Bj20040668  0.624
2004 Farkas A, Nardai G, Csermely P, Tompa P, Friedrich P. DUK114, the Drosophila orthologue of bovine brain calpain activator protein, is a molecular chaperone. The Biochemical Journal. 383: 165-70. PMID 15250825 DOI: 10.1042/Bj20040668  0.624
2004 Fuxreiter M, Simon I, Friedrich P, Tompa P. Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. Journal of Molecular Biology. 338: 1015-26. PMID 15111064 DOI: 10.1016/J.Jmb.2004.03.017  0.664
2004 Fuxreiter M, Simon I, Friedrich P, Tompa P. Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. Journal of Molecular Biology. 338: 1015-26. PMID 15111064 DOI: 10.1016/J.Jmb.2004.03.017  0.664
2004 Friedrich P, Papp H, Halasy K, Farkas A, Farkas B, Tompa P, Kása P. Differential distribution of calpain small subunit 1 and 2 in rat brain. The European Journal of Neuroscience. 19: 1819-25. PMID 15078555 DOI: 10.1111/J.1460-9568.2004.03313.X  0.566
2004 Friedrich P, Papp H, Halasy K, Farkas A, Farkas B, Tompa P, Kása P. Differential distribution of calpain small subunit 1 and 2 in rat brain. The European Journal of Neuroscience. 19: 1819-25. PMID 15078555 DOI: 10.1111/J.1460-9568.2004.03313.X  0.566
2004 Jánossy J, Ubezio P, Apáti A, Magócsi M, Tompa P, Friedrich P. Calpain as a multi-site regulator of cell cycle. Biochemical Pharmacology. 67: 1513-21. PMID 15041468 DOI: 10.1016/J.Bcp.2003.12.021  0.571
2004 Jánossy J, Ubezio P, Apáti A, Magócsi M, Tompa P, Friedrich P. Calpain as a multi-site regulator of cell cycle. Biochemical Pharmacology. 67: 1513-21. PMID 15041468 DOI: 10.1016/J.Bcp.2003.12.021  0.571
2004 Tompa P, Buzder-Lantos P, Tantos A, Farkas A, Szilágyi A, Bánóczi Z, Hudecz F, Friedrich P. On the sequential determinants of calpain cleavage. The Journal of Biological Chemistry. 279: 20775-85. PMID 14988399 DOI: 10.1074/Jbc.M313873200  0.8
2004 Tompa P, Buzder-Lantos P, Tantos A, Farkas A, Szilágyi A, Bánóczi Z, Hudecz F, Friedrich P. On the sequential determinants of calpain cleavage. The Journal of Biological Chemistry. 279: 20775-85. PMID 14988399 DOI: 10.1074/Jbc.M313873200  0.8
2004 Alexa A, Bozóky Z, Farkas A, Tompa P, Friedrich P. Contribution of distinct structural elements to activation of calpain by Ca2+ ions. The Journal of Biological Chemistry. 279: 20118-26. PMID 14976200 DOI: 10.1074/Jbc.M311969200  0.586
2004 Alexa A, Bozóky Z, Farkas A, Tompa P, Friedrich P. Contribution of distinct structural elements to activation of calpain by Ca2+ ions. The Journal of Biological Chemistry. 279: 20118-26. PMID 14976200 DOI: 10.1074/Jbc.M311969200  0.586
2004 Farkas A, Tompa P, Schád E, Sinka R, Jékely G, Friedrich P. Autolytic activation and localization in Schneider cells (S2) of calpain B from Drosophila. The Biochemical Journal. 378: 299-305. PMID 14614768 DOI: 10.1042/Bj20031310  0.768
2004 Farkas A, Tompa P, Schád E, Sinka R, Jékely G, Friedrich P. Autolytic activation and localization in Schneider cells (S2) of calpain B from Drosophila. The Biochemical Journal. 378: 299-305. PMID 14614768 DOI: 10.1042/Bj20031310  0.768
2003 Mucsi Z, Hudecz F, Hollósi M, Tompa P, Friedrich P. Binding-induced folding transitions in calpastatin subdomains A and C. Protein Science : a Publication of the Protein Society. 12: 2327-36. PMID 14500891 DOI: 10.1110/Ps.03138803  0.642
2003 Mucsi Z, Hudecz F, Hollósi M, Tompa P, Friedrich P. Binding-induced folding transitions in calpastatin subdomains A and C. Protein Science : a Publication of the Protein Society. 12: 2327-36. PMID 14500891 DOI: 10.1110/Ps.03138803  0.642
2003 Tompa P. Intrinsically unstructured proteins evolve by repeat expansion. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 25: 847-55. PMID 12938174 DOI: 10.1002/BIES.10324  0.392
2003 Farkas A, Tompa P, Friedrich P. Revisiting ubiquity and tissue specificity of human calpains. Biological Chemistry. 384: 945-9. PMID 12887062 DOI: 10.1515/Bc.2003.106  0.564
2003 Farkas A, Tompa P, Friedrich P. Revisiting ubiquity and tissue specificity of human calpains. Biological Chemistry. 384: 945-9. PMID 12887062 DOI: 10.1515/Bc.2003.106  0.564
2003 Spadoni C, Farkas A, Sinka R, Tompa P, Friedrich P. Molecular cloning and RNA expression of a novel Drosophila calpain, Calpain C. Biochemical and Biophysical Research Communications. 303: 343-9. PMID 12646209 DOI: 10.1016/S0006-291X(03)00350-4  0.629
2003 Spadoni C, Farkas A, Sinka R, Tompa P, Friedrich P. Molecular cloning and RNA expression of a novel Drosophila calpain, Calpain C. Biochemical and Biophysical Research Communications. 303: 343-9. PMID 12646209 DOI: 10.1016/S0006-291X(03)00350-4  0.629
2002 Alexa A, Schmidt G, Tompa P, Ogueta S, Vázquez J, Kulcsár P, Kovács J, Dombrádi V, Friedrich P. The phosphorylation state of threonine-220, a uniquely phosphatase-sensitive protein kinase A site in microtubule-associated protein MAP2c, regulates microtubule binding and stability. Biochemistry. 41: 12427-35. PMID 12369833 DOI: 10.1021/Bi025916S  0.627
2002 Tompa P. Intrinsically unstructured proteins. Trends in Biochemical Sciences. 27: 527-33. PMID 12368089 DOI: 10.1016/S0968-0004(02)02169-2  0.379
2002 Tompa P, Tusnády GE, Friedrich P, Simon I. The role of dimerization in prion replication. Biophysical Journal. 82: 1711-8. PMID 11916832 DOI: 10.1016/S0006-3495(02)75523-9  0.603
2002 Tompa P, Tusnády GE, Friedrich P, Simon I. The role of dimerization in prion replication. Biophysical Journal. 82: 1711-8. PMID 11916832 DOI: 10.1016/S0006-3495(02)75523-9  0.603
2002 Schád E, Farkas A, Jékely G, Tompa P, Friedrich P. A novel human small subunit of calpains. The Biochemical Journal. 362: 383-8. PMID 11853546 DOI: 10.1042/0264-6021:3620383  0.81
2002 Schád E, Farkas A, Jékely G, Tompa P, Friedrich P. A novel human small subunit of calpains. The Biochemical Journal. 362: 383-8. PMID 11853546 DOI: 10.1042/0264-6021:3620383  0.81
2002 Tompa P, Mucsi Z, Orosz G, Friedrich P. Calpastatin subdomains A and C are activators of calpain. The Journal of Biological Chemistry. 277: 9022-6. PMID 11809743 DOI: 10.1074/Jbc.C100700200  0.578
2002 Tompa P, Mucsi Z, Orosz G, Friedrich P. Calpastatin subdomains A and C are activators of calpain. The Journal of Biological Chemistry. 277: 9022-6. PMID 11809743 DOI: 10.1074/Jbc.C100700200  0.578
2001 Tompa P, Tusnády GE, Cserzo M, Simon I. Prion protein: evolution caught en route. Proceedings of the National Academy of Sciences of the United States of America. 98: 4431-6. PMID 11287647 DOI: 10.1073/pnas.071308398  0.385
2001 Tompa P, Töth-Boconádi R, Friedrich P. Frequency decoding of fast calcium oscillations by calpain. Cell Calcium. 29: 161-70. PMID 11162853 DOI: 10.1054/ceca.2000.0179  0.557
2001 Tompa P, Emori Y, Sorimachi H, Suzuki K, Friedrich P. Domain III of calpain is a ca2+-regulated phospholipid-binding domain. Biochemical and Biophysical Research Communications. 280: 1333-9. PMID 11162675 DOI: 10.1006/Bbrc.2001.4279  0.589
2000 Wronski R, Tompa P, Hutter-Paier B, Crailsheim K, Friedrich P, Windisch M. Inhibitory effect of a brain derived peptide preparation on the Ca++-dependent protease, calpain. Journal of Neural Transmission (Vienna, Austria : 1996). 107: 145-57. PMID 10847556 DOI: 10.1007/s007020050013  0.642
2000 Tompa P, Schád E, Friedrich P. A sensitive and continuous fluorometric activity assay using a natural substrate. Microtubule-associated protein 2. Methods in Molecular Biology (Clifton, N.J.). 144: 137-41. PMID 10818758 DOI: 10.1385/1-59259-050-0:137  0.637
2000 Tompa P, Friedrich P. Kinetic analysis of human mu-calpain autolysis. Methods in Molecular Biology (Clifton, N.J.). 144: 129-36. PMID 10818757 DOI: 10.1385/1-59259-050-0:129  0.538
2000 Tusnády GE, Tompa P, Cserzö M, Simon I. Prion protein: evolution caught en route? Biochemical Society Transactions. 28: A413-A413. DOI: 10.1042/bst028a413a  0.32
1998 Tompa P, Friedrich P. Prion proteins as memory molecules: an hypothesis. Neuroscience. 86: 1037-43. PMID 9697111 DOI: 10.1016/S0306-4522(98)00148-1  0.683
1998 Tompa P, Friedrich P. Synaptic metaplasticity and the local charge effect in postsynaptic densities. Trends in Neurosciences. 21: 97-102. PMID 9530914 DOI: 10.1016/S0166-2236(97)01176-4  0.554
1996 Tompa P, Baki A, Schád E, Friedrich P. The calpain cascade. Mu-calpain activates m-calpain. The Journal of Biological Chemistry. 271: 33161-4. PMID 8969168 DOI: 10.1074/Jbc.271.52.33161  0.55
1996 Sánchez C, Tompa P, Szücs K, Friedrich P, Avila J. Phosphorylation and dephosphorylation in the proline-rich C-terminal domain of microtubule-associated protein 2. European Journal of Biochemistry / Febs. 241: 765-71. PMID 8944764 DOI: 10.1111/J.1432-1033.1996.00765.X  0.6
1996 Baki A, Tompa P, Alexa A, Molnár O, Friedrich P. Autolysis parallels activation of mu-calpain. The Biochemical Journal. 318: 897-901. PMID 8836135 DOI: 10.1042/Bj3180897  0.57
1996 Alexa A, Tompa P, Baki A, Vereb G, Friedrich P. Mutual protection of microtubule-associated protein 2 (MAP2) and cyclic AMP-dependent protein kinase II against mu-calpain. Journal of Neuroscience Research. 44: 438-45. PMID 8776665 DOI: 10.1002/(Sici)1097-4547(19960601)44:5<438::Aid-Jnr4>3.0.Co;2-G  0.601
1995 Tompa P, Schád E, Baki A, Alexa A, Batke J, Friedrich P. An ultrasensitive, continuous fluorometric assay for calpain activity. Analytical Biochemistry. 228: 287-93. PMID 8572308 DOI: 10.1006/Abio.1995.1352  0.601
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