| Year |
Citation |
Score |
| 2023 |
Mahato J, Mukherjee R, Bose A, Mehra S, Gadhe L, Maji SK, Chowdhury A. Sensitized Emission Imaging Allows Nanoscale Surface Polarity Mapping of α-Synuclein Amyloid Fibrils. Acs Chemical Neuroscience. PMID 38099928 DOI: 10.1021/acschemneuro.3c00467 |
0.356 |
|
| 2022 |
Poudyal M, Sakunthala A, Mukherjee S, Gadhe L, Maji SK. Phase separation and other forms of α-Synuclein self-assemblies. Essays in Biochemistry. PMID 36373662 DOI: 10.1042/EBC20220055 |
0.412 |
|
| 2022 |
Mahato J, Ray S, Maji SK, Chowdhury A. Spectrally Resolved FRET Microscopy of α-Synuclein Phase-Separated Liquid Droplets. Methods in Molecular Biology (Clifton, N.J.). 2551: 425-447. PMID 36310218 DOI: 10.1007/978-1-0716-2597-2_27 |
0.778 |
|
| 2022 |
Mehra S, Ahlawat S, Kumar H, Datta D, Navalkar A, Singh N, Patel K, Gadhe L, Kadu P, Kumar R, Jha NN, Sakunthala A, Sawner AS, Padinhateeri R, Udgaonkar JB, ... ... Maji SK, et al. α-Synuclein aggregation intermediates form fibril polymorphs with distinct prion-like properties. Journal of Molecular Biology. 167761. PMID 35907572 DOI: 10.1016/j.jmb.2022.167761 |
0.406 |
|
| 2022 |
Sakunthala A, Datta D, Navalkar A, Gadhe L, Kadu P, Patel K, Mehra S, Kumar R, Chatterjee D, Devi J, Sengupta K, Padinhateeri R, Maji SK. Direct Demonstration of Seed Size-Dependent α-Synuclein Amyloid Amplification. The Journal of Physical Chemistry Letters. 6427-6438. PMID 35816132 DOI: 10.1021/acs.jpclett.2c01650 |
0.37 |
|
| 2022 |
Mukherjee S, Sakunthala A, Gadhe L, Poudyal M, Sawner AS, Kadu P, Maji SK. Liquid-liquid Phase Separation of α-Synuclein: A New Mechanistic Insight for α-Synuclein Aggregation Associated with Parkinson's Disease Pathogenesis. Journal of Molecular Biology. 167713. PMID 35787838 DOI: 10.1016/j.jmb.2022.167713 |
0.389 |
|
| 2022 |
Chatterjee D, Jacob RS, Ray S, Navalkar A, Singh N, Sengupta S, Gadhe L, Kadu P, Datta D, Paul A, Arunima S, Mehra S, Pindi C, Kumar S, Singru P, ... ... Maji SK, et al. Co-aggregation and secondary nucleation in the life cycle of human prolactin/galanin functional amyloids. Elife. 11. PMID 35257659 DOI: 10.7554/eLife.73835 |
0.384 |
|
| 2021 |
Gadhe L, Sakunthala A, Mukherjee S, Gahlot N, Bera R, Sawner AS, Kadu P, Maji SK. Intermediates of α-synuclein aggregation: Implications in Parkinson's disease pathogenesis. Biophysical Chemistry. 281: 106736. PMID 34923391 DOI: 10.1016/j.bpc.2021.106736 |
0.31 |
|
| 2021 |
Mahato J, Ray KK, Das S, Kadu P, Maji SK, Chowdhury A. Investigation of Structural Heterogeneity in Individual Amyloid Fibrils Using Polarization-Resolved Microscopy. The Journal of Physical Chemistry. B. PMID 34861110 DOI: 10.1021/acs.jpcb.1c08604 |
0.783 |
|
| 2021 |
Tikader B, Maji SK, Kar S. A generic approach to decipher the mechanistic pathway of heterogeneous protein aggregation kinetics. Chemical Science. 12: 13530-13545. PMID 34777773 DOI: 10.1039/d1sc03190b |
0.39 |
|
| 2021 |
Mehra S, Gadhe L, Bera R, Sawner AS, Maji SK. Structural and Functional Insights into α-Synuclein Fibril Polymorphism. Biomolecules. 11. PMID 34680054 DOI: 10.3390/biom11101419 |
0.36 |
|
| 2021 |
Sawner AS, Ray S, Yadav P, Mukherjee S, Panigrahi R, Poudyal M, Patel K, Ghosh D, Kummerant E, Kumar A, Riek R, Maji SK. Modulating α-Synuclein Liquid-Liquid Phase Separation. Biochemistry. PMID 34431665 DOI: 10.1021/acs.biochem.1c00434 |
0.598 |
|
| 2020 |
Joseph J, Maji SK, Padinhateeri R. Computational Model for Studying Breakage-Dependent Amyloid Growth. Acs Chemical Neuroscience. PMID 33050701 DOI: 10.1021/acschemneuro.0c00481 |
0.325 |
|
| 2020 |
Seuring C, Verasdonck J, Gath J, Ghosh D, Nespovitaya N, Wälti MA, Maji SK, Cadalbert R, Güntert P, Meier BH, Riek R. The three-dimensional structure of human β-endorphin amyloid fibrils. Nature Structural & Molecular Biology. PMID 33046908 DOI: 10.1038/s41594-020-00515-z |
0.586 |
|
| 2020 |
Sharma K, Mehra S, Sawner AS, Markam PS, Panigrahi R, Navalkar A, Chatterjee D, Kumar R, Kadu P, Patel K, Ray S, Kumar A, Maji SK. Effect of disease-associated P123H and V70M mutations on β-synuclein fibrillation. Acs Chemical Neuroscience. PMID 32833434 DOI: 10.1021/Acschemneuro.0C00405 |
0.736 |
|
| 2020 |
Ray S, Maji SK. Predictable phase-separated proteins. Nature Chemistry. PMID 32807882 DOI: 10.1038/S41557-020-0532-2 |
0.3 |
|
| 2020 |
Pravin N, Kumar R, Tripathi S, Kumar P, Mohite GM, Navalkar A, Panigrahi R, Singh N, Gadhe LG, Manchanda S, Shimozawa M, Nilsson P, Johansson J, Kumar A, Maji SK, et al. Benzimidazole based fluorophores for the detection of amyloid fibrils with higher sensitivity than Thioflavin-T. Journal of Neurochemistry. PMID 32750740 DOI: 10.1111/Jnc.15138 |
0.5 |
|
| 2020 |
Ray S, Singh N, Kumar R, Patel K, Pandey S, Datta D, Mahato J, Panigrahi R, Navalkar A, Mehra S, Gadhe L, Chatterjee D, Sawner AS, Maiti S, Bhatia S, ... ... Maji SK, et al. α-Synuclein aggregation nucleates through liquid-liquid phase separation. Nature Chemistry. PMID 32514159 DOI: 10.1038/S41557-020-0465-9 |
0.776 |
|
| 2019 |
Kirti S, Patel K, Das S, Shrimali P, Samanta S, Kumar R, Chatterjee D, Ghosh D, Kumar A, Tayalia P, Maji SK. Amyloid Fibrils with Positive Charge Enhance Retroviral Transduction in Mammalian Cells. Acs Biomaterials Science & Engineering. 5: 126-138. PMID 33405876 DOI: 10.1021/acsbiomaterials.8b00248 |
0.391 |
|
| 2019 |
Lima I, Navalkar A, Maji S, Silva JL, Oliveira G, Cino E. Biophysical characterization of p53 core domain aggregates. The Biochemical Journal. PMID 31841126 DOI: 10.1042/Bcj20190778 |
0.49 |
|
| 2019 |
Jacob RS, Anoop A, Maji SK. Protein Nanofibrils as Storage Forms of Peptide Drugs and Hormones. Advances in Experimental Medicine and Biology. 1174: 265-290. PMID 31713202 DOI: 10.1007/978-981-13-9791-2_8 |
0.49 |
|
| 2019 |
Navalkar A, Ghosh S, Pandey S, Paul A, Datta D, Maji SK. Prion-like p53 amyloids in cancer. Biochemistry. PMID 31603660 DOI: 10.1021/Acs.Biochem.9B00796 |
0.358 |
|
| 2019 |
Mukhopadhyay A, Mehra S, Kumar R, Maji SK, Krishnamoorthy G, Sharma K. α-Synuclein Spontaneously Adopts Stable and Reversible α-Helical Structure in Water-less Environment. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 31515915 DOI: 10.1002/Cphc.201900868 |
0.396 |
|
| 2019 |
Bhattacharyya D, Mohite GM, Krishnamoorthy J, Gayen N, Mehera S, Navalkar A, Kotler SA, Ratha BN, Ghosh A, Kumar R, Garai K, Mandal AK, Maji SK, Bhunia A. Lipopolysaccharide from Gut Microbiota Modulates α-Synuclein Aggregation and Alters its Biological Function. Acs Chemical Neuroscience. PMID 30855940 DOI: 10.1021/Acschemneuro.8B00733 |
0.447 |
|
| 2019 |
Mehra S, Sahay S, Maji SK. α-Synuclein misfolding and aggregation: Implications in Parkinson's disease pathogenesis. Biochimica Et Biophysica Acta. Proteins and Proteomics. PMID 30853581 DOI: 10.1016/J.Bbapap.2019.03.001 |
0.488 |
|
| 2019 |
Jayarajan R, Kumar R, Gupta J, Dev G, Kadu P, Chatterjee D, Bahadur D, Maiti D, Maji SK. Fabrication of an amyloid fibril-palladium nanocomposite: a sustainable catalyst for C–H activation and the electrooxidation of ethanol Journal of Materials Chemistry A. 7: 4486-4493. DOI: 10.1039/C8Ta11134K |
0.359 |
|
| 2018 |
Jacob RS, Das S, Singh N, Patel K, Datta D, Sen S, Maji SK. Amyloids Are Novel Cell-Adhesive Matrices. Advances in Experimental Medicine and Biology. 1112: 79-97. PMID 30637692 DOI: 10.1007/978-981-13-3065-0_7 |
0.451 |
|
| 2018 |
Mohite GM, Navalkar A, Kumar R, Mehra S, Das S, Gadhe LG, Ghosh D, Alias B, Chandrawanshi V, Ramakrishnan A, Mehra S, Maji SK. Familial α-synuclein A53E mutation enhances cell death in response to environmental toxins due to more population of oligomers. Biochemistry. PMID 30025458 DOI: 10.1021/Acs.Biochem.8B00321 |
0.381 |
|
| 2018 |
Mehra S, Ghosh D, Kumar R, Mondal M, Gadhe LG, Das S, Anoop A, Jha NN, Jacob RS, Chatterjee D, Ray S, Singh N, Kumar A, Maji SK. Glycosaminoglycans have variable effects on α-synuclein aggregation and differentially affect the activities of the resulting amyloid fibrils. The Journal of Biological Chemistry. PMID 29959225 DOI: 10.1074/Jbc.Ra118.004267 |
0.53 |
|
| 2018 |
Mohite GM, Dwivedi S, Das S, Kumar R, Paluri S, Mehra S, Ruhela N, S A, Jha NN, Maji SK. Parkinson's disease associated α-synuclein familial mutants promote dopaminergic neuronal death in Drosophila melanogaster. Acs Chemical Neuroscience. PMID 29906099 DOI: 10.1021/Acschemneuro.8B00107 |
0.415 |
|
| 2018 |
Mohite GM, Kumar R, Panigrahi R, Navalkar A, Singh N, Datta D, Mehra S, Ray S, Gadhe LG, Das S, Singh N, Chatterjee D, Kumar A, Maji SK. Comparison of kinetics, toxicity, oligomers formation and membrane binding capacity of α-synuclein familial mutations at A53 site including newly discovered A53V mutation. Biochemistry. PMID 29771508 DOI: 10.1021/Acs.Biochem.8B00314 |
0.441 |
|
| 2018 |
Das S, Jacob RS, Patel K, Singh N, Maji SK. Amyloid fibrils: Versatile biomaterials for cell adhesion and tissue engineering applications. Biomacromolecules. PMID 29701992 DOI: 10.1021/Acs.Biomac.8B00279 |
0.31 |
|
| 2018 |
Bhattacharyya D, Kumar R, Mehra S, Ghosh A, Maji SK, Bhunia A. Multitude NMR studies of α-synuclein familial mutants: probing their differential aggregation propensities. Chemical Communications (Cambridge, England). PMID 29568828 DOI: 10.1039/C7Cc09597J |
0.48 |
|
| 2018 |
Kumar R, Das S, Mohite GM, Rout SK, Halder S, Jha NN, Ray S, Mehra S, Agarwal V, Maji SK. Cytotoxic oligomers and fibrils trapped in a gel-like state of α-synuclein assemblies. Angewandte Chemie (International Ed. in English). PMID 29524323 DOI: 10.1002/Anie.201711854 |
0.481 |
|
| 2018 |
Kirti S, Patel K, Das S, Shrimali P, Samanta S, Kumar R, Chatterjee D, Ghosh D, Kumar A, Tayalia P, Maji SK. Amyloid Fibrils with Positive Charge Enhance Retroviral Transduction in Mammalian Cells Acs Biomaterials Science & Engineering. 5: 126-138. DOI: 10.1021/Acsbiomaterials.8B00248 |
0.496 |
|
| 2018 |
Khatri A, Punjabi N, Ghosh D, Maji SK, Mukherji S. Detection and differentiation of α-Synuclein monomer and fibril by chitosan film coated nanogold array on optical sensor platform Sensors and Actuators B: Chemical. 255: 692-700. DOI: 10.1016/J.Snb.2017.08.051 |
0.396 |
|
| 2017 |
Jha NN, Ranganathan S, Kumar R, Mehra S, Panigrahi R, Navalkar A, Ghosh D, Kumar A, Padinhateeri R, Maji SK. Complexation of NAC derived peptide ligands with C-terminus of α-synuclein accelerates its aggregation. Biochemistry. PMID 29286644 DOI: 10.1021/Acs.Biochem.7B01090 |
0.51 |
|
| 2017 |
Jha NN, Kumar R, Panigrahi R, Navalkar A, Ghosh D, Sahay S, Mondal M, Kumar A, Maji SK. Comparison of α-synuclein fibril inhibition by four different amyloid inhibitors. Acs Chemical Neuroscience. PMID 28872299 DOI: 10.1021/Acschemneuro.7B00261 |
0.5 |
|
| 2017 |
Das S, Kumar R, Jha NN, Maji SK. Controlled Exposure of Bioactive Growth Factor in 3D Amyloid Hydrogel for Stem Cells Differentiation. Advanced Healthcare Materials. PMID 28736995 DOI: 10.1002/Adhm.201700368 |
0.321 |
|
| 2017 |
Ghosh S, Salot S, Sengupta S, Navalkar A, Ghosh D, Jacob R, Das S, Kumar R, Jha NN, Sahay S, Mehra S, Mohite GM, Ghosh SK, Kombrabail M, Krishnamoorthy G, ... ... Maji SK, et al. p53 amyloid formation leading to its loss of function: implications in cancer pathogenesis. Cell Death and Differentiation. PMID 28644435 DOI: 10.1038/Cdd.2017.105 |
0.355 |
|
| 2017 |
Sengupta S, Maji SK, Ghosh SK. Evidence of a prion-like transmission of p53 amyloid in Saccharomyces cerevisiae. Molecular and Cellular Biology. PMID 28630281 DOI: 10.1128/Mcb.00118-17 |
0.368 |
|
| 2016 |
Sahay S, Krishnamoorthy G, Maji SK. Site-specific structural dynamics of α-Synuclein revealed by time-resolved fluorescence spectroscopy: a review. Methods and Applications in Fluorescence. 4: 042002. PMID 28192290 DOI: 10.1088/2050-6120/4/4/042002 |
0.481 |
|
| 2016 |
Ranjan P, Ghosh D, Yarramala DS, Das S, Maji SK, Kumar A. Differential copper binding to Alpha-synuclein and its disease-associated mutants affect the aggregation and amyloid formation. Biochimica Et Biophysica Acta. PMID 27916677 DOI: 10.1016/J.Bbagen.2016.11.043 |
0.388 |
|
| 2016 |
Ghosh D, Mehra S, Sahay S, Singh PK, Maji SK. α-synuclein aggregation and its modulation. International Journal of Biological Macromolecules. PMID 27737778 DOI: 10.1016/J.Ijbiomac.2016.10.021 |
0.438 |
|
| 2016 |
Ranganathan S, Maji SK, Padinhateeri R. Defining a physical basis for diversity in protein self-assemblies using a minimal model. Journal of the American Chemical Society. PMID 27690405 DOI: 10.1021/Jacs.6B06433 |
0.407 |
|
| 2016 |
Jha NN, Ghosh D, Das S, Anoop A, Jacob RS, Singh PK, Ayyagari N, Namboothiri IN, Maji SK. Effect of curcumin analogs onα-synuclein aggregation and cytotoxicity. Scientific Reports. 6: 28511. PMID 27338805 DOI: 10.1038/Srep28511 |
0.49 |
|
| 2016 |
Jacob RS, Das S, Ghosh S, Anoop A, Jha NN, Khan T, Singru P, Kumar A, Maji SK. Amyloid formation of growth hormone in presence of zinc: Relevance to its storage in secretory granules. Scientific Reports. 6: 23370. PMID 27004850 DOI: 10.1038/Srep23370 |
0.433 |
|
| 2016 |
Sahay S, Ghosh D, Singh PK, Maji SK. Alteration of Structure and Aggregation of a-Synuclein by Familial Parkinson's Disease Associated Mutations. Current Protein & Peptide Science. PMID 26972727 DOI: 10.2174/1389203717666160314151706 |
0.383 |
|
| 2016 |
Ranganathan S, Ghosh D, Maji SK, Padinhateeri R. A minimal conformational switching-dependent model for amyloid self-assembly. Scientific Reports. 6: 21103. PMID 26883720 DOI: 10.1038/Srep21103 |
0.475 |
|
| 2016 |
Jacob RS, George E, Singh PK, Salot S, Anoop A, Jha NN, Sen S, Maji SK. Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif. The Journal of Biological Chemistry. PMID 26742841 DOI: 10.1074/Jbc.M115.678177 |
0.495 |
|
| 2016 |
Das S, Zhou K, Ghosh D, Jha NN, Singh PK, Jacob RS, Bernard CC, Finkelstein DI, Forsythe JS, Maji SK. Implantable amyloid hydrogels for promoting stem cell differentiation to neurons Npg Asia Materials. 8: e304-e304. DOI: 10.1038/Am.2016.116 |
0.323 |
|
| 2016 |
Ranganathan S, Maji SK, Padinhateeri R. A Minimalistic Kinetic Model for Amyloid Self-Assembly Biophysical Journal. 110: 220a. DOI: 10.1016/J.Bpj.2015.11.1218 |
0.483 |
|
| 2016 |
Jacob RS, Sen S, Maji SK. Adhesion of Human Mesenchymal Stem Cells and Differentiation of SH-SY5Y Cells on Amyloid Fibrils Macromolecular Symposia. 369: 35-42. DOI: 10.1002/Masy.201600071 |
0.455 |
|
| 2015 |
Jacob RS, Das S, Ghosh D, Maji SK. Influence of retinoic acid on mesenchymal stem cell differentiation in amyloid hydrogels. Data in Brief. 5: 954-8. PMID 26740966 DOI: 10.1016/J.Dib.2015.11.015 |
0.314 |
|
| 2015 |
Jacob RS, Ghosh D, Singh PK, Basu SK, Jha NN, Das S, Sukul PK, Patil S, Sathaye S, Kumar A, Chowdhury A, Malik S, Sen S, Maji SK. Self healing hydrogels composed of amyloid nano fibrils for cell culture and stem cell differentiation. Biomaterials. 54: 97-105. PMID 25907043 DOI: 10.1016/J.Biomaterials.2015.03.002 |
0.501 |
|
| 2015 |
Singh PK, Ghosh D, Tewari D, Mohite GM, Carvalho E, Jha NN, Jacob RS, Sahay S, Banerjee R, Bera AK, Maji SK. Cytotoxic helix-rich oligomer formation by melittin and pancreatic polypeptide. Plos One. 10: e0120346. PMID 25803428 DOI: 10.1371/Journal.Pone.0120346 |
0.484 |
|
| 2015 |
Ghosh D, Singh PK, Sahay S, Jha NN, Jacob RS, Sen S, Kumar A, Riek R, Maji SK. Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation. Scientific Reports. 5: 9228. PMID 25784353 DOI: 10.1038/Srep09228 |
0.675 |
|
| 2015 |
Sahay S, Ghosh D, Dwivedi S, Anoop A, Mohite GM, Kombrabail M, Krishnamoorthy G, Maji SK. Familial Parkinson disease-associated mutations alter the site-specific microenvironment and dynamics of α-synuclein. The Journal of Biological Chemistry. 290: 7804-22. PMID 25635052 DOI: 10.1074/Jbc.M114.598607 |
0.441 |
|
| 2015 |
Ghosh D, Maji SK. Preparation of aggregate-free α -synuclein for in vitro aggregation study Protocol Exchange. DOI: 10.1038/Protex.2015.037 |
0.483 |
|
| 2014 |
Ghosh D, Sahay S, Ranjan P, Salot S, Mohite GM, Singh PK, Dwivedi S, Carvalho E, Banerjee R, Kumar A, Maji SK. The newly discovered Parkinson's disease associated Finnish mutation (A53E) attenuates α-synuclein aggregation and membrane binding. Biochemistry. 53: 6419-21. PMID 25268550 DOI: 10.1021/Bi5010365 |
0.426 |
|
| 2014 |
Ghosh S, Ghosh D, Ranganathan S, Anoop A, P SK, Jha NN, Padinhateeri R, Maji SK. Investigating the intrinsic aggregation potential of evolutionarily conserved segments in p53. Biochemistry. 53: 5995-6010. PMID 25181279 DOI: 10.1021/Bi500825D |
0.43 |
|
| 2014 |
Anoop A, Ranganathan S, Das Dhaked B, Jha NN, Pratihar S, Ghosh S, Sahay S, Kumar S, Das S, Kombrabail M, Agarwal K, Jacob RS, Singru P, Bhaumik P, Padinhateeri R, ... ... Maji SK, et al. Elucidating the role of disulfide bond on amyloid formation and fibril reversibility of somatostatin-14: relevance to its storage and secretion. The Journal of Biological Chemistry. 289: 16884-903. PMID 24782311 DOI: 10.1074/Jbc.M114.548354 |
0.487 |
|
| 2014 |
Ghosh D, Dutta P, Chakraborty C, Singh PK, Anoop A, Jha NN, Jacob RS, Mondal M, Mankar S, Das S, Malik S, Maji SK. Complexation of amyloid fibrils with charged conjugated polymers. Langmuir : the Acs Journal of Surfaces and Colloids. 30: 3775-86. PMID 24678792 DOI: 10.1021/La404739F |
0.403 |
|
| 2014 |
Sahay S, Anoop A, Krishnamoorthy G, Maji SK. Site-specific fluorescence dynamics of α-synuclein fibrils using time-resolved fluorescence studies: effect of familial Parkinson's disease-associated mutations. Biochemistry. 53: 807-9. PMID 24450731 DOI: 10.1021/Bi401543Z |
0.457 |
|
| 2013 |
Sukul PK, Singh PK, Maji SK, Malik S. Aggregation induced chirality in a self assembled perylene based hydrogel: application of the intracellular pH measurement. Journal of Materials Chemistry. B. 1: 153-156. PMID 32260687 DOI: 10.1039/C2Tb00007E |
0.334 |
|
| 2013 |
Jha NN, Anoop A, Ranganathan S, Mohite GM, Padinhateeri R, Maji SK. Characterization of amyloid formation by glucagon-like peptides: role of basic residues in heparin-mediated aggregation. Biochemistry. 52: 8800-10. PMID 24236650 DOI: 10.1021/Bi401398K |
0.483 |
|
| 2013 |
Ghosh D, Mondal M, Mohite GM, Singh PK, Ranjan P, Anoop A, Ghosh S, Jha NN, Kumar A, Maji SK. The Parkinson's disease-associated H50Q mutation accelerates α-Synuclein aggregation in vitro. Biochemistry. 52: 6925-7. PMID 24047453 DOI: 10.1021/Bi400999D |
0.468 |
|
| 2013 |
Singh PK, Kotia V, Ghosh D, Mohite GM, Kumar A, Maji SK. Curcumin modulates α-synuclein aggregation and toxicity. Acs Chemical Neuroscience. 4: 393-407. PMID 23509976 DOI: 10.1021/Cn3001203 |
0.478 |
|
| 2013 |
Jacob RS, Mondal M, Kumar A, Maji SK. Amyloid Formation by Human Growth Hormone Biophysical Journal. 104: 72a-73a. DOI: 10.1016/J.Bpj.2012.11.438 |
0.434 |
|
| 2012 |
Sahu BS, Obbineni JM, Sahu G, Allu PK, Subramanian L, Sonawane PJ, Singh PK, Sasi BK, Senapati S, Maji SK, Bera AK, Gomathi BS, Mullasari AS, Mahapatra NR. Functional genetic variants of the catecholamine-release-inhibitory peptide catestatin in an Indian population: allele-specific effects on metabolic traits. The Journal of Biological Chemistry. 287: 43840-52. PMID 23105094 DOI: 10.1074/Jbc.M112.407916 |
0.306 |
|
| 2012 |
Singh PK, Maji SK. Amyloid-like fibril formation by tachykinin neuropeptides and its relevance to amyloid β-protein aggregation and toxicity. Cell Biochemistry and Biophysics. 64: 29-44. PMID 22628076 DOI: 10.1007/S12013-012-9364-Z |
0.531 |
|
| 2012 |
Ranganathan S, Singh PK, Singh U, Singru PS, Padinhateeri R, Maji SK. Molecular interpretation of ACTH-β-endorphin coaggregation: relevance to secretory granule biogenesis. Plos One. 7: e31924. PMID 22403619 DOI: 10.1371/Journal.Pone.0031924 |
0.447 |
|
| 2012 |
Sahu BS, Mohan J, Obbineni JM, Sahu G, Singh PK, Sonawane PJ, Sasi BK, Allu PK, Maji SK, Bera AK, Senapati S, Mahapatra NR. Molecular interactions of the physiological anti-hypertensive peptide catestatin with the neuronal nicotinic acetylcholine receptor. Journal of Cell Science. 125: 2323-37. PMID 22357947 DOI: 10.1242/Jcs.103176 |
0.316 |
|
| 2011 |
Mankar S, Anoop A, Sen S, Maji SK. Nanomaterials: amyloids reflect their brighter side. Nano Reviews. 2. PMID 22110868 DOI: 10.3402/Nano.V2I0.6032 |
0.473 |
|
| 2011 |
Winner B, Jappelli R, Maji SK, Desplats PA, Boyer L, Aigner S, Hetzer C, Loher T, Vilar M, Campioni S, Tzitzilonis C, Soragni A, Jessberger S, Mira H, Consiglio A, et al. In vivo demonstration that alpha-synuclein oligomers are toxic. Proceedings of the National Academy of Sciences of the United States of America. 108: 4194-9. PMID 21325059 DOI: 10.1073/Pnas.1100976108 |
0.639 |
|
| 2011 |
Maji SK. Amyloid: A natural nanomaterial International Journal of Nanoscience. 10: 909-917. DOI: 10.1142/S0219581X11009362 |
0.53 |
|
| 2010 |
Anoop A, Singh PK, Jacob RS, Maji SK. CSF Biomarkers for Alzheimer's Disease Diagnosis. International Journal of Alzheimer's Disease. 2010. PMID 20721349 DOI: 10.4061/2010/606802 |
0.351 |
|
| 2009 |
Maji SK, Wang L, Greenwald J, Riek R. Structure-activity relationship of amyloid fibrils. Febs Letters. 583: 2610-7. PMID 19596006 DOI: 10.1016/J.Febslet.2009.07.003 |
0.66 |
|
| 2009 |
Maji SK, Ogorzalek Loo RR, Inayathullah M, Spring SM, Vollers SS, Condron MM, Bitan G, Loo JA, Teplow DB. Amino acid position-specific contributions to amyloid beta-protein oligomerization. The Journal of Biological Chemistry. 284: 23580-91. PMID 19567875 DOI: 10.1074/Jbc.M109.038133 |
0.783 |
|
| 2009 |
Maji SK, Perrin MH, Sawaya MR, Jessberger S, Vadodaria K, Rissman RA, Singru PS, Nilsson KP, Simon R, Schubert D, Eisenberg D, Rivier J, Sawchenko P, Vale W, Riek R. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science (New York, N.Y.). 325: 328-32. PMID 19541956 DOI: 10.1126/Science.1173155 |
0.632 |
|
| 2009 |
Dvir H, Lundberg ME, Maji SK, Riek R, Choe S. Mistic: cellular localization, solution behavior, polymerization, and fibril formation. Protein Science : a Publication of the Protein Society. 18: 1564-70. PMID 19475664 DOI: 10.1002/Pro.148 |
0.522 |
|
| 2008 |
Wang L, Maji SK, Sawaya MR, Eisenberg D, Riek R. Bacterial inclusion bodies contain amyloid-like structure. Plos Biology. 6: e195. PMID 18684013 DOI: 10.1371/Journal.Pbio.0060195 |
0.659 |
|
| 2008 |
Vilar M, Chou HT, Lührs T, Maji SK, Riek-Loher D, Verel R, Manning G, Stahlberg H, Riek R. The fold of alpha-synuclein fibrils. Proceedings of the National Academy of Sciences of the United States of America. 105: 8637-42. PMID 18550842 DOI: 10.1073/Pnas.0712179105 |
0.585 |
|
| 2008 |
Maji SK, Schubert D, Rivier C, Lee S, Rivier JE, Riek R. Amyloid as a depot for the formulation of long-acting drugs. Plos Biology. 6: e17. PMID 18254658 DOI: 10.1371/Journal.Pbio.0060017 |
0.619 |
|
| 2008 |
Lazo ND, Maji SK, Fradinger EA, Bitan G, Teplow DB. The Amyloid β Protein Amyloid Proteins: the Beta Sheet Conformation and Disease. 2: 384-491. DOI: 10.1002/9783527619344.ch17 |
0.698 |
|
| 2007 |
Perrin MH, Grace CR, Digruccio MR, Fischer WH, Maji SK, Cantle JP, Smith S, Manning G, Vale WW, Riek R. Distinct structural and functional roles of conserved residues in the first extracellular domain of receptors for corticotropin-releasing factor and related G-protein-coupled receptors. The Journal of Biological Chemistry. 282: 37529-36. PMID 17940290 DOI: 10.1074/Jbc.M703748200 |
0.513 |
|
| 2005 |
Maji SK, Amsden JJ, Rothschild KJ, Condron MM, Teplow DB. Conformational dynamics of amyloid beta-protein assembly probed using intrinsic fluorescence. Biochemistry. 44: 13365-76. PMID 16201761 DOI: 10.1021/Bi0508284 |
0.644 |
|
| 2004 |
Maji S, Bitan G, Vollers SS, Spring S, Condron MM, Teplow DB. P1-236 Site-specific analysis of Abeta oligomerization using photochemical cross-linking Neurobiology of Aging. 25: S163. DOI: 10.1016/S0197-4580(04)80549-9 |
0.656 |
|
| 2004 |
Maji S, Condron MM, Teplow DB. P1-154 Assembly-dependent Abeta conformational transitions revealed using intrinsic fluorescence Neurobiology of Aging. 25: S139. DOI: 10.1016/S0197-4580(04)80467-6 |
0.566 |
|
| 2004 |
Banerjee A, Maji SK, Drew MG, Haldar D, Das AK, Banerjee A. Hydrogen-bonded dimer can mediate supramolecular β-sheet formation and subsequent amyloid-like fibril formation: a model study Tetrahedron. 60: 5935-5944. DOI: 10.1016/J.Tet.2004.05.041 |
0.508 |
|
| 2004 |
Maji SK, Haldar D, Drew MG, Banerjee A, Das AK, Banerjee A. Self-assembly of β-turn forming synthetic tripeptides into supramolecular β-sheets and amyloid-like fibrils in the solid state Tetrahedron. 60: 3251-3259. DOI: 10.1016/J.Tet.2004.02.019 |
0.491 |
|
| 2003 |
Maji SK, Haldar D, Banerjee A, Mukhopadhyay C, Banerjee A. Conformational Heterogeneity of a Tripeptide in the Solid State and in Solution: Characterization of a g-Turn Containing Incipient Hairpin in Solution Journal of Structural Chemistry. 44: 790-795. DOI: 10.1023/B:Jory.0000029816.31278.7B |
0.403 |
|
| 2003 |
Banerjee A, Maji SK, Drew MG, Haldar D, Banerjee A. An amyloid-like fibril forming antiparallel supramolecular β-sheet from a synthetic tripeptide: a crystallographic signature Tetrahedron Letters. 44: 6741-6744. DOI: 10.1016/S0040-4039(03)01642-3 |
0.431 |
|
| 2003 |
Maji SK, Malik S, Drew MG, Nandi AK, Banerjee A. A synthetic tripeptide as a novel organo-gelator: a structural investigation Tetrahedron Letters. 44: 4103-4107. DOI: 10.1016/S0040-4039(03)00839-6 |
0.411 |
|
| 2003 |
Banerjee A, Maji SK, Drew MG, Haldar D, Banerjee A. Supramolecular peptide helix from a novel double turn forming peptide containing a β-amino acid Tetrahedron Letters. 44: 699-702. DOI: 10.1016/S0040-4039(02)02675-8 |
0.445 |
|
| 2003 |
Banerjee A, Maji SK, Drew MG, Haldar D, Banerjee A. Amyloid-like fibril-forming supramolecular β-sheets from a β-turn forming tripeptide containing non-coded amino acids: the crystallographic signature Tetrahedron Letters. 44: 335-339. DOI: 10.1016/S0040-4039(02)02570-4 |
0.455 |
|
| 2003 |
Maji SK, Haldar D, Bhattacharyya D, Banerjee A. Conformational heterogeneity of a turn mimetic pseudo-peptide: comparison of crystal state, solution and theoretically derived structures Journal of Molecular Structure. 646: 111-123. DOI: 10.1016/S0022-2860(02)00619-1 |
0.34 |
|
| 2002 |
Maji SK, Banerjee R, Velmurugan D, Razak A, Fun HK, Banerjee A. Peptide design using omega-amino acids: unusual turn structures nucleated by an N-terminal single gamma-aminobutyric acid residue in short model peptides. The Journal of Organic Chemistry. 67: 633-9. PMID 11856000 DOI: 10.1021/Jo010314K |
0.347 |
|
| 2002 |
Malik S, Maji SK, Banerjee A, Nandi AK. A synthetic tripeptide as organogelator: elucidation of gelation mechanism Journal of the Chemical Society-Perkin Transactions 1. 1177-1186. DOI: 10.1039/B111598G |
0.327 |
|
| 2002 |
Maji SK, Banerjee A, Drew MG, Haldar D, Banerjee A. Self-assembly of a tetrapeptide in which a unique supramolecular helical structure is formed via intermolecular hydrogen bonding in the solid state Tetrahedron Letters. 43: 6759-6762. DOI: 10.1016/S0040-4039(02)01521-6 |
0.373 |
|
| 2002 |
Haldar D, Maji SK, Drew MG, Banerjee A, Banerjee A. Self-assembly of a short peptide monomer into a continuous hydrogen bonded supramolecular helix: the crystallographic signature Tetrahedron Letters. 43: 5465-5468. DOI: 10.1016/S0040-4039(02)01050-X |
0.386 |
|
| 2002 |
Haldar D, Maji SK, Sheldrick WS, Banerjee A. First crystallographic signature of the highly ordered supramolecular helical assemblage from a tripeptide containing a non-coded amino acid Tetrahedron Letters. 43: 2653-2656. DOI: 10.1016/S0040-4039(02)00283-6 |
0.414 |
|
| 2002 |
Maji SK, Haldar D, Banerjee A, Banerjee A. Fibril-forming model synthetic peptides containing 3-aminophenylacetic acid Tetrahedron. 58: 8695-8702. DOI: 10.1016/S0040-4020(02)01093-1 |
0.457 |
|
| 2001 |
Maji SK, Drew MG, Banerjee A. First crystallographic signature of amyloid-like fibril forming beta-sheet assemblage from a tripeptide with non-coded amino acids. Chemical Communications (Cambridge, England). 1946-7. PMID 12240232 DOI: 10.1039/B105418J |
0.363 |
|
| 2001 |
Maji SK, Halder D, Velmurugan D, Rajakannan V, Banerjee A. A unique example of a pseudo-peptide containing noncoded amino acids self-assembling into a supramolecular β-sheet-like structure in crystals Letters in Peptide Science. 8: 61-67. DOI: 10.1023/A:1015015723006 |
0.397 |
|
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