| Year |
Citation |
Score |
| 2025 |
Devi S, Garg DK, Bhat R. Green tea polyphenol EGCG acts differentially on end-stage amyloid polymorphs of α-synuclein formed in different polyol osmolytes. Biochimica Et Biophysica Acta. Proteins and Proteomics. 1873: 141073. PMID 40189174 DOI: 10.1016/j.bbapap.2025.141073 |
0.738 |
|
| 2024 |
Bhat R. Flavones Suppress Aggregation and Amyloid Fibril Formation of Human Lysozyme under Macromolecular Crowding Conditions. Biochemistry. PMID 39385522 DOI: 10.1021/acs.biochem.4c00362 |
0.324 |
|
| 2024 |
Singh SL, Bhat R. Cyclic-NDGA Effectively Inhibits Human γ-Synuclein Fibrillation, Forms Nontoxic Off-Pathway Species, and Disintegrates Preformed Mature Fibrils. Acs Chemical Neuroscience. PMID 38637513 DOI: 10.1021/acschemneuro.3c00793 |
0.315 |
|
| 2023 |
Jain MK, Bhat R. Modulation of the conformation, fibrillation, and fibril morphologies of human brain α-, β-, and γ-synuclein proteins by the disaccharide chemical chaperone trehalose. Biochimica Et Biophysica Acta. Proteins and Proteomics. 1871: 140932. PMID 37433401 DOI: 10.1016/j.bbapap.2023.140932 |
0.318 |
|
| 2023 |
Devi S, Garg DK, Bhat R. Kinetic control in amyloid polymorphism: Different agitation and solution conditions promote distinct amyloid polymorphs of alpha-synuclein. Biochimica Et Biophysica Acta. Proteins and Proteomics. 1871: 140917. PMID 37061153 DOI: 10.1016/j.bbapap.2023.140917 |
0.731 |
|
| 2022 |
Garg DK, Bhat R. Modulation of assembly of TDP-43 low-complexity domain by heparin: From droplets to amyloid fibrils. Biophysical Journal. PMID 35644946 DOI: 10.1016/j.bpj.2022.05.042 |
0.731 |
|
| 2021 |
Aune K, Lee J, Prakash V, Bhat R, Andreu J, Monasterio O, Perez-Ramirez B, Shearwin K, Arakawa T, Carpenter J, Crowe J, Crowe L, Somero G, Gagnon P, Charles MT. A tribute to Dr. Serge N. Timasheff, our mentor. Biophysical Reviews. 13: 459-484. PMID 34471434 DOI: 10.1007/s12551-021-00814-9 |
0.663 |
|
| 2020 |
Verma G, Singh P, Bhat R. Disorder under stress: Role of polyol osmolytes in modulating fibrillation and aggregation of intrinsically disordered proteins. Biophysical Chemistry. 264: 106422. PMID 32707418 DOI: 10.1016/J.Bpc.2020.106422 |
0.421 |
|
| 2019 |
Singh P, Bhat R. Binding of Noradrenaline to native and intermediate states during fibrillation of α-Synuclein leads to the formation of stable and structured cytotoxic species. Acs Chemical Neuroscience. PMID 30917654 DOI: 10.1021/Acschemneuro.8B00650 |
0.38 |
|
| 2018 |
Roy S, Bhat R. Suppression, Disaggregation, and Modulation of γ-Synuclein Fibrillation Pathway by Green Tea Polyphenol EGCG. Protein Science : a Publication of the Protein Society. PMID 30394624 DOI: 10.1002/Pro.3549 |
0.624 |
|
| 2018 |
Roy S, Bhat R. Effect of polyols on the structure and aggregation of recombinant human γ-Synuclein, an intrinsically disordered protein. Biochimica Et Biophysica Acta. PMID 30003969 DOI: 10.1016/J.Bbapap.2018.07.003 |
0.667 |
|
| 2018 |
Jain MK, Singh P, Roy S, Bhat R. Comparative analysis of the conformation, aggregation, interaction and fibril morphologies of human α, β and γ synuclein proteins. Biochemistry. PMID 29851342 DOI: 10.1021/Acs.Biochem.8B00343 |
0.632 |
|
| 2017 |
Zaidi FK, Bhat R. Resveratrol Interferes with an Early step in the Fibrillation pathway of Human lysozyme and Modulates it towards less-toxic, Off-pathway Aggregates. Chembiochem : a European Journal of Chemical Biology. PMID 29105927 DOI: 10.1002/Cbic.201700207 |
0.388 |
|
| 2016 |
Vashist A, Prithvi Raj D, Gupta UD, Bhat R, Tyagi JS. The α10 helix of DevR, the Mycobacterium tuberculosis dormancy response regulator, regulates its DNA binding and activity. The Febs Journal. PMID 26799615 DOI: 10.1111/Febs.13664 |
0.36 |
|
| 2015 |
Uppal S, Salhotra S, Mukhi N, Zaidi FK, Seal M, Dey SG, Bhat R, Kundu S. Significantly enhanced heme retention ability of myoglobin engineered to mimic the third covalent linkage by nonaxial histidine to heme (vinyl) in synechocystis hemoglobin. The Journal of Biological Chemistry. 290: 1979-93. PMID 25451928 DOI: 10.1074/Jbc.M114.603225 |
0.342 |
|
| 2015 |
Rabbani G, Ahmad E, Khan MV, Ashraf MT, Bhat R, Khan RH. Impact of structural stability of cold adapted Candida antarctica lipase B (CaLB): In relation to pH, chemical and thermal denaturation Rsc Advances. 5: 20115-20131. DOI: 10.1039/C4Ra17093H |
0.327 |
|
| 2012 |
Devaraneni PK, Mishra N, Bhat R. Polyol osmolytes stabilize native-like cooperative intermediate state of yeast hexokinase A at low pH. Biochimie. 94: 947-52. PMID 22203099 DOI: 10.1016/J.Biochi.2011.12.012 |
0.582 |
|
| 2009 |
Akhtar K, Gupta V, Koul A, Alam N, Bhat R, Bamezai RN. Differential behavior of missense mutations in the intersubunit contact domain of the human pyruvate kinase M2 isozyme. The Journal of Biological Chemistry. 284: 11971-81. PMID 19265196 DOI: 10.1074/Jbc.M808761200 |
0.319 |
|
| 2007 |
Das U, Hariprasad G, Ethayathulla AS, Manral P, Das TK, Pasha S, Mann A, Ganguli M, Verma AK, Bhat R, Chandrayan SK, Ahmed S, Sharma S, Kaur P, Singh TP, et al. Inhibition of protein aggregation: supramolecular assemblies of arginine hold the key. Plos One. 2: e1176. PMID 18000547 DOI: 10.1371/Journal.Pone.0001176 |
0.41 |
|
| 2007 |
Mishra R, Bhat R, Seckler R. Chemical chaperone-mediated protein folding: stabilization of P22 tailspike folding intermediates by glycerol. Biological Chemistry. 388: 797-804. PMID 17655498 DOI: 10.1515/Bc.2007.096 |
0.376 |
|
| 2006 |
Tiwari A, Bhat R. Stabilization of yeast hexokinase A by polyol osmolytes: correlation with the physicochemical properties of aqueous solutions. Biophysical Chemistry. 124: 90-9. PMID 16828962 DOI: 10.1016/J.Bpc.2006.06.003 |
0.595 |
|
| 2005 |
Mishra R, Seckler R, Bhat R. Efficient refolding of aggregation-prone citrate synthase by polyol osmolytes: how well are protein folding and stability aspects coupled? The Journal of Biological Chemistry. 280: 15553-60. PMID 15695514 DOI: 10.1074/Jbc.M410947200 |
0.408 |
|
| 2004 |
Welker E, Maki K, Shastry MC, Juminaga D, Bhat R, Scheraga HA, Roder H. Ultrarapid mixing experiments shed new light on the characteristics of the initial conformational ensemble during the folding of ribonuclease A. Proceedings of the National Academy of Sciences of the United States of America. 101: 17681-6. PMID 15574490 DOI: 10.1073/Pnas.0407999101 |
0.416 |
|
| 2004 |
Singh S, Singh A, Aziz MA, Waheed SM, Bhat R, Bhatnagar R. Thermal inactivation of protective antigen of Bacillus anthracis and its prevention by polyol osmolytes. Biochemical and Biophysical Research Communications. 322: 1029-37. PMID 15336568 DOI: 10.1016/J.Bbrc.2004.08.020 |
0.312 |
|
| 2004 |
Kumar DP, Tiwari A, Bhat R. Effect of pH on the stability and structure of yeast hexokinase A. Acidic amino acid residues in the cleft region are critical for the opening and the closing of the structure. The Journal of Biological Chemistry. 279: 32093-9. PMID 15145950 DOI: 10.1074/Jbc.M313449200 |
0.569 |
|
| 2003 |
Bhat R, Wedemeyer WJ, Scheraga HA. Proline isomerization in bovine pancreatic ribonuclease A. 2. Folding conditions. Biochemistry. 42: 5722-8. PMID 12741829 DOI: 10.1021/bi030024t |
0.343 |
|
| 2003 |
Kaushik JK, Bhat R. Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose. The Journal of Biological Chemistry. 278: 26458-65. PMID 12702728 DOI: 10.1074/Jbc.M300815200 |
0.41 |
|
| 2001 |
Gupta P, Singh S, Tiwari A, Bhat R, Bhatnagar R. Effect of pH on stability of anthrax lethal factor: Correlation between denaturation and activity Biochemical and Biophysical Research Communications. 284: 568-573. PMID 11396937 DOI: 10.1006/Bbrc.2001.5018 |
0.314 |
|
| 1999 |
Kaushik JK, Bhat R. A mechanistic analysis of the increase in the thermal stability of proteins in aqueous carboxylic acid salt solutions Protein Science. 8: 222-233. PMID 10210200 DOI: 10.1110/Ps.8.1.222 |
0.403 |
|
| 1998 |
Kaushik JK, Bhat R. Thermal stability of proteins in aqueous polyol solutions: Role of the surface tension of water in the stabilizing effect of polyols Journal of Physical Chemistry B. 102: 7058-7066. DOI: 10.1021/Jp981119L |
0.343 |
|
| 1998 |
Devi YS, Nair UB, Bhat R. Effect of a mixed stabilizer-denaturant system on the stability of enzyme activity at high temperatures : lysozyme as a model Progress in Biotechnology. 15: 263-268. DOI: 10.1016/S0921-0423(98)80041-5 |
0.3 |
|
| 1992 |
Bhat R, Timasheff SN. Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols. Protein Science : a Publication of the Protein Society. 1: 1133-43. PMID 1304392 DOI: 10.1002/Pro.5560010907 |
0.56 |
|
| 1990 |
Arakawa T, Bhat R, Timasheff SN. Why preferential hydration does not always stabilize the native structure of globular proteins. Biochemistry. 29: 1924-31. PMID 2331472 DOI: 10.1021/Bi00459A037 |
0.6 |
|
| 1990 |
Arakawa T, Bhat R, Timasheff SN. Preferential interactions determine protein solubility in three-component solutions: the MgCl2 system. Biochemistry. 29: 1914-23. PMID 2331471 DOI: 10.1021/Bi00459A036 |
0.596 |
|
| 1990 |
Sharma VK, Bhat R. Thermodynamic studies on the interaction of some ureas and salts with micellar triton-X-100 in aqueous solutions Thermochimica Acta. 160: 315-322. DOI: 10.1016/0040-6031(90)80271-Y |
0.347 |
|
| 1989 |
Kishore N, Bhat R, Ahluwalia JC. Thermodynamics of some nucleic acid bases and nucleosides in water, and their transfer to aqueous glucose and sucrose solutions at 298.15 K. Biophysical Chemistry. 33: 227-36. PMID 2804241 DOI: 10.1016/0301-4622(89)80024-9 |
0.701 |
|
| 1989 |
Sharma VK, Bhat R. Calorimetric studies on the interaction of sugars and polyols with the non-ionic surfactant TRITON-X-100 in aqueous solutions Thermochimica Acta. 138: 359-366. DOI: 10.1016/0040-6031(89)87272-7 |
0.358 |
|
| 1988 |
Bhat R, Kishore N, Ahluwalia JC. Thermodynamic studies of transfer of some amino acids and peptides from water to aqueous glucose and sucrose solutions at 298.15 K Journal of the Chemical Society, Faraday Transactions 1: Physical Chemistry in Condensed Phases. 84: 2651-2665. DOI: 10.1039/F19888402651 |
0.707 |
|
| 1987 |
Bhat R, Ahluwalia JC. Effect of calcium chloride on the conformation of proteins. Thermodynamic studies of some model compounds. International Journal of Peptide and Protein Research. 30: 145-52. PMID 3679668 DOI: 10.1111/J.1399-3011.1987.Tb03323.X |
0.638 |
|
| 1985 |
Bhat R, Ahluwalia JC. Partial molar heat capacities and volumes of transfer of some amino acids and peptides from water to aqueous sodium chloride solutions at 298.15 K The Journal of Physical Chemistry. 89: 1099-1105. DOI: 10.1021/J100253A011 |
0.601 |
|
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