Year |
Citation |
Score |
2023 |
Panda AK, Biswas A. Editorial: Influence of mutations, stresses and post-translational modifications on the structure and function of heat shock proteins and their relationship with various diseases. Frontiers in Molecular Biosciences. 10: 1310272. PMID 37928643 DOI: 10.3389/fmolb.2023.1310272 |
0.615 |
|
2023 |
Chakraborty A, Mohapatra SS, Barik S, Roy I, Gupta B, Biswas A. Impact of nanoparticles on amyloid beta-induced Alzheimer's disease, tuberculosis, leprosy and cancer: A systematic review. Bioscience Reports. PMID 36630532 DOI: 10.1042/BSR20220324 |
0.64 |
|
2022 |
Panda AK, Biswas A. Editorial: The Role of Mutations, Stresses and Post-Translational Modifications in the Structure and Function of Small Heat Shock Proteins and Their Relationship with Different Human Diseases. Frontiers in Molecular Biosciences. 9: 922959. PMID 35755803 DOI: 10.3389/fmolb.2022.922959 |
0.618 |
|
2022 |
Nandi SK, Panda AK, Chakraborty A, Rathee S, Roy I, Barik S, Mohapatra SS, Biswas A. Role of ATP-Small Heat Shock Protein Interaction in Human Diseases. Frontiers in Molecular Biosciences. 9: 844826. PMID 35252358 DOI: 10.3389/fmolb.2022.844826 |
0.783 |
|
2021 |
Chakraborty A, Ghosh R, Biswas A. Interaction of constituents of MDT regimen for leprosy with Mycobacterium leprae HSP18: Impact on its structure and function. The Febs Journal. PMID 34555271 DOI: 10.1111/febs.16212 |
0.676 |
|
2020 |
Ghosh R, Chakraborty A, Biswas A, Chowdhuri S. Depicting the inhibitory potential of polyphenols from root against the main protease of SARS CoV-2 using computational approaches. Journal of Biomolecular Structure & Dynamics. 1-12. PMID 33292085 DOI: 10.1080/07391102.2020.1858164 |
0.582 |
|
2020 |
Ghosh R, Chakraborty A, Biswas A, Chowdhuri S. Computer aided identification of potential SARS CoV-2 main protease inhibitors from diterpenoids and biflavonoids of leaves. Journal of Biomolecular Structure & Dynamics. 1-16. PMID 33140695 DOI: 10.1080/07391102.2020.1841680 |
0.576 |
|
2020 |
Ghosh R, Chakraborty A, Biswas A, Chowdhuri S. Identification of alkaloids from as potent SARS CoV-2 main protease inhibitors: An perspective. Journal of Molecular Structure. 129489. PMID 33100380 DOI: 10.1016/j.molstruc.2020.129489 |
0.566 |
|
2020 |
Ghosh R, Chakraborty A, Biswas A, Chowdhuri S. Potential therapeutic use of corticosteroids as SARS CoV-2 main protease inhibitors: a computational study. Journal of Biomolecular Structure & Dynamics. 1-14. PMID 33094701 DOI: 10.1080/07391102.2020.1835728 |
0.558 |
|
2020 |
Ghosh R, Chakraborty A, Biswas A, Chowdhuri S. Identification of polyphenols from as SARS CoV-2 main protease inhibitors using docking and molecular dynamics simulation approaches. Journal of Biomolecular Structure & Dynamics. 1-14. PMID 32762411 DOI: 10.1080/07391102.2020.1802347 |
0.61 |
|
2020 |
Dash SP, Panda AK, Pasayat S, Majumder S, Biswas A, Kaminsky W, Mukhopadhyay S, Bhutia SK, Dinda R. Corrigendum to "Evaluation of the cell cytotoxicity and DNA/BSA binding and cleavage activity of some dioxidovanadium(V) complexes containing aroylhydrazones" [J. Inorg. Biochem. 144 (2015) 1-12]. Journal of Inorganic Biochemistry. 210: 111135. PMID 32569883 DOI: 10.1016/J.Jinorgbio.2020.111135 |
0.585 |
|
2020 |
Ghosh R, Chakraborty A, Biswas A, Chowdhuri S. Evaluation of green tea polyphenols as novel corona virus (SARS CoV-2) main protease (Mpro) inhibitors - an docking and molecular dynamics simulation study. Journal of Biomolecular Structure & Dynamics. 1-13. PMID 32568613 DOI: 10.1080/07391102.2020.1779818 |
0.613 |
|
2020 |
Chakraborty A, Biswas A. Structure, stability and chaperone function of Mycobacterium leprae Heat Shock Protein 18 are differentially affected upon interaction with gold and silver nanoparticles. International Journal of Biological Macromolecules. PMID 32084461 DOI: 10.1016/J.Ijbiomac.2020.02.182 |
0.668 |
|
2019 |
Nandi SK, Chakraborty A, Panda AK, Biswas A. M. leprae HSP18 suppresses copper (II) mediated ROS generation: Effect of redox stress on its structure and function. International Journal of Biological Macromolecules. PMID 31883890 DOI: 10.1016/J.Ijbiomac.2019.12.215 |
0.779 |
|
2019 |
Panda AK, Chakraborty A, Nandi SK, Biswas A. The impact of different mutations at arginine141 on the structure, subunit exchange dynamics and chaperone activity of Hsp16.3. Proteins. PMID 31860142 DOI: 10.1002/Prot.25864 |
0.78 |
|
2019 |
Chakraborty A, Panda AK, Ghosh R, Biswas A. DNA minor groove binding of a well known anti-mycobacterial drug dapsone: A spectroscopic, viscometric and molecular docking study. Archives of Biochemistry and Biophysics. 665: 107-113. PMID 30851241 DOI: 10.1016/J.Abb.2019.03.001 |
0.716 |
|
2019 |
Chakraborty A, Panda AK, Ghosh R, Roy I, Biswas A. Depicting the DNA binding and photo-nuclease ability of anti-mycobacterial drug rifampicin: A biophysical and molecular docking perspective. International Journal of Biological Macromolecules. PMID 30633932 DOI: 10.1016/J.Ijbiomac.2019.01.034 |
0.755 |
|
2018 |
Nandi SK, Chakraborty A, Panda AK, Kar RK, Bhunia A, Biswas A. Evidences for zinc (II) and copper (II) ion interactions with Mycobacterium leprae HSP18: Effect on its structure and chaperone function. Journal of Inorganic Biochemistry. 188: 62-75. PMID 30121399 DOI: 10.1016/J.Jinorgbio.2018.08.010 |
0.774 |
|
2018 |
Chakraborty A, Nandi SK, Panda AK, Mahapatra PP, Giri S, Biswas A. Probing the structure-function relationship of Mycobacterium leprae HSP18 under different UV radiations. International Journal of Biological Macromolecules. PMID 30055280 DOI: 10.1016/J.Ijbiomac.2018.07.151 |
0.765 |
|
2017 |
Majumder S, Pasayat S, Panda AK, Dash SP, Roy S, Biswas A, Varma ME, Joshi BN, Garribba E, Kausar C, Patra SK, Kaminsky W, Crochet A, Dinda R. Monomeric and Dimeric Oxidomolybdenum(V and VI) Complexes, Cytotoxicity, and DNA Interaction Studies: Molybdenum Assisted C═N Bond Cleavage of Salophen Ligands. Inorganic Chemistry. PMID 28858483 DOI: 10.1021/Acs.Inorgchem.7B01578 |
0.592 |
|
2017 |
Mukhi P, Mohapatra SS, Bhattacharjee M, Ray KK, Muraleedharan TS, Arun A, Sathyavathi R, Juluri RR, Satyam PV, Panda AK, Biswas A, Nayak S, Bojja S, Pratihar S, Roy S. Mercury based drug in ancient India: The red sulfide of mercury (rasasindur) in nanoscale. Journal of Ayurveda and Integrative Medicine. PMID 28600164 DOI: 10.1016/J.Jaim.2017.01.009 |
0.588 |
|
2016 |
Panda AK, Chakraborty A, Nandi SK, Kaushik A, Biswas A. The C-terminal Extension of Mycobacterium tuberculosis Hsp16.3 Regulates its Oligomerization, Subunit Exchange Dynamics and Chaperone Function. The Febs Journal. PMID 27885799 DOI: 10.1111/Febs.13975 |
0.796 |
|
2016 |
Dash SP, Panda AK, Dhaka S, Pasayat S, Biswas A, Maurya MR, Majhi PK, Crochet A, Dinda R. A study of DNA/BSA interaction and catalytic potential of oxidovanadium(v) complexes with ONO donor ligands. Dalton Transactions (Cambridge, England : 2003). PMID 27805190 DOI: 10.1039/C6Dt03228A |
0.605 |
|
2016 |
Nandi SK, Chakraborty A, Panda AK, Biswas A. Conformational perturbation, hydrophobic interactions and oligomeric association are responsible for the enhanced chaperone function of Mycobacterium leprae HSP18 under pre-thermal condition Rsc Advances. 6: 62146-62156. DOI: 10.1039/C6Ra00167J |
0.79 |
|
2015 |
Nandi SK, Panda AK, Chakraborty A, Ray SS, Biswas A. Role of Subunit Exchange and Electrostatic Interactions on the Chaperone Activity of Mycobacterium leprae HSP18. Plos One. 10: e0129734. PMID 26098662 DOI: 10.1371/Journal.Pone.0129734 |
0.796 |
|
2015 |
Panda AK, Nandi SK, Chakraborty A, Nagaraj RH, Biswas A. Differential role of arginine mutations on the structure and functions of α-crystallin. Biochimica Et Biophysica Acta. PMID 26080000 DOI: 10.1016/J.Bbagen.2015.06.004 |
0.781 |
|
2015 |
Biswas A, Karmakar S, Chowdhury A, Das KP. Interaction of α-crystallin with some small molecules and its effect on its structure and function. Biochimica Et Biophysica Acta. PMID 26073614 DOI: 10.1016/J.Bbagen.2015.06.002 |
0.392 |
|
2015 |
Nandi SK, Chakraborty A, Panda AK, Ray SS, Kar RK, Bhunia A, Biswas A. Interaction of ATP with a small heat shock protein from Mycobacterium leprae: effect on its structure and function. Plos Neglected Tropical Diseases. 9: e0003661. PMID 25811190 DOI: 10.1371/Journal.Pntd.0003661 |
0.803 |
|
2015 |
Saswati, Chakraborty A, Dash SP, Panda AK, Acharyya R, Biswas A, Mukhopadhyay S, Bhutia SK, Crochet A, Patil YP, Nethaji M, Dinda R. Synthesis, X-ray structure and in vitro cytotoxicity studies of Cu(I/II) complexes of thiosemicarbazone: special emphasis on their interactions with DNA. Dalton Transactions (Cambridge, England : 2003). 44: 6140-57. PMID 25736331 DOI: 10.1039/C4Dt03764B |
0.699 |
|
2015 |
Dash SP, Panda AK, Pasayat S, Majumder S, Biswas A, Kaminsky W, Mukhopadhyay S, Bhutia SK, Dinda R. Evaluation of the cell cytotoxicity and DNA/BSA binding and cleavage activity of some dioxidovanadium(V) complexes containing aroylhydrazones. Journal of Inorganic Biochemistry. 144: 1-12. PMID 25575303 DOI: 10.1016/J.Jinorgbio.2014.12.018 |
0.608 |
|
2015 |
Karmakar S, Biswas A, Das KP. Structural Stabilization and Functional Enhancement of Miceller Protein α-Crystallin by ATP and Zn2+ Journal of Surface Science and Technology. 31: 13-20. DOI: 10.17834/Ijsstissst.V31I1-2.79920 |
0.392 |
|
2015 |
Hossain SM, Lakma A, Pradhan RN, Chakraborty A, Biswas A, Singh AK. Synthesis and characterization of a novel, ditopic, reversible and highly selective, “Turn-On” fluorescent chemosensor for Al3+ ion Rsc Advances. 5: 63338-63344. DOI: 10.1039/C5Ra12040C |
0.537 |
|
2015 |
Dash SP, Panda AK, Pasayat S, Dinda R, Biswas A, Tiekink ERT, Mukhopadhyay S, Bhutia SK, Kaminsky W, Sinn E. Oxidovanadium(v) complexes of aroylhydrazones incorporating heterocycles: synthesis, characterization and study of DNA binding, photo-induced DNA cleavage and cytotoxic activities Rsc Advances. 5: 51852-51867. DOI: 10.1039/C4Ra14369H |
0.583 |
|
2014 |
DiMauro MA, Nandi SK, Raghavan CT, Kar RK, Wang B, Bhunia A, Nagaraj RH, Biswas A. Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin. Biochemistry. 53: 7269-82. PMID 25393041 DOI: 10.1021/Bi501004Y |
0.728 |
|
2014 |
Dash SP, Panda AK, Pasayat S, Dinda R, Biswas A, Tiekink ER, Patil YP, Nethaji M, Kaminsky W, Mukhopadhyay S, Bhutia SK. Syntheses and structural investigation of some alkali metal ion-mediated LV(V)O2(-) (L(2-) = tridentate ONO ligands) species: DNA binding, photo-induced DNA cleavage and cytotoxic activities. Dalton Transactions (Cambridge, England : 2003). 43: 10139-56. PMID 24874519 DOI: 10.1039/C4Dt00883A |
0.61 |
|
2013 |
Nahomi RB, Huang R, Nandi SK, Wang B, Padmanabha S, Santhoshkumar P, Filipek S, Biswas A, Nagaraj RH. Acetylation of lysine 92 improves the chaperone and anti-apoptotic activities of human αB-crystallin. Biochemistry. 52: 8126-38. PMID 24128140 DOI: 10.1021/Bi400638S |
0.753 |
|
2013 |
Nandi SK, Rehna EA, Panda AK, Shiburaj S, Dharmalingam K, Biswas A. A S52P mutation in the 'α-crystallin domain' of Mycobacterium leprae HSP18 reduces its oligomeric size and chaperone function. The Febs Journal. 280: 5994-6009. PMID 24024660 DOI: 10.1111/Febs.12519 |
0.813 |
|
2013 |
Nagaraj RH, Panda AK, Shanthakumar S, Santhoshkumar P, Pasupuleti N, Wang B, Biswas A. MGO reacts with proteins to form AGEs, like, hydroimidazolone, argpyrimidine and MOLD in tissue proteins. Plos One. DOI: 10.1371/Journal.Pone.0030257.G001 |
0.595 |
|
2012 |
Nagaraj RH, Panda AK, Shanthakumar S, Santhoshkumar P, Pasupuleti N, Wang B, Biswas A. Hydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimics. Plos One. 7: e30257. PMID 22272318 DOI: 10.1371/Journal.Pone.0030257 |
0.683 |
|
2012 |
Wang ZQ, Tejero J, Wei CC, Haque MM, Santolini J, Fadlalla M, Biswas A, Stuehr DJ. Arg375 tunes tetrahydrobiopterin functions and modulates catalysis by inducible nitric oxide synthase. Journal of Inorganic Biochemistry. 108: 203-15. PMID 22173094 DOI: 10.1016/J.Jinorgbio.2011.11.015 |
0.527 |
|
2012 |
Nagaraj RH, Nahomi RB, Shanthakumar S, Linetsky M, Padmanabha S, Pasupuleti N, Wang B, Santhoshkumar P, Panda AK, Biswas A. Acetylation of αA-crystallin in the human lens: effects on structure and chaperone function. Biochimica Et Biophysica Acta. 1822: 120-9. PMID 22120592 DOI: 10.1016/J.Bbadis.2011.11.011 |
0.653 |
|
2011 |
Tejero J, Biswas A, Haque MM, Wang ZQ, Hemann C, Varnado CL, Novince Z, Hille R, Goodwin DC, Stuehr DJ. Mesohaem substitution reveals how haem electronic properties can influence the kinetic and catalytic parameters of neuronal NO synthase. The Biochemical Journal. 433: 163-74. PMID 20950274 DOI: 10.1042/Bj20101353 |
0.496 |
|
2010 |
Waheed SM, Ghosh A, Chakravarti R, Biswas A, Haque MM, Panda K, Stuehr DJ. Nitric oxide blocks cellular heme insertion into a broad range of heme proteins. Free Radical Biology & Medicine. 48: 1548-58. PMID 20211245 DOI: 10.1016/J.Freeradbiomed.2010.02.038 |
0.556 |
|
2010 |
Bhattacharya M, Biswas A, Das AK. Interaction analysis of TcrX/Y two component system from Mycobacterium tuberculosis. Biochimie. 92: 263-72. PMID 19962420 DOI: 10.1016/J.Biochi.2009.11.009 |
0.318 |
|
2008 |
Tejero J, Biswas A, Wang ZQ, Page RC, Haque MM, Hemann C, Zweier JL, Misra S, Stuehr DJ. Stabilization and characterization of a heme-oxy reaction intermediate in inducible nitric-oxide synthase. The Journal of Biological Chemistry. 283: 33498-507. PMID 18815130 DOI: 10.1074/Jbc.M806122200 |
0.514 |
|
2008 |
Nagaraj RH, Biswas A, Miller A, Oya-Ito T, Bhat M. The other side of the Maillard reaction. Annals of the New York Academy of Sciences. 1126: 107-12. PMID 18448802 DOI: 10.1196/Annals.1433.045 |
0.364 |
|
2008 |
Biswas A, Lewis S, Wang B, Miyagi M, Santoshkumar P, Gangadhariah MH, Nagaraj RH. Chemical modulation of the chaperone function of human alphaA-crystallin. Journal of Biochemistry. 144: 21-32. PMID 18344542 DOI: 10.1093/Jb/Mvn037 |
0.391 |
|
2008 |
Biswas A, Das KP. Zn2+ enhances the molecular chaperone function and stability of alpha-crystallin. Biochemistry. 47: 804-16. PMID 18095658 DOI: 10.1021/Bi7011965 |
0.594 |
|
2008 |
Biswas A, Wang B, Miyagi M, Nagaraj RH. Effect of methylglyoxal modification on stress-induced aggregation of client proteins and their chaperoning by human alphaA-crystallin. The Biochemical Journal. 409: 771-7. PMID 17941823 DOI: 10.1042/Bj20071006 |
0.391 |
|
2007 |
Puttaiah S, Biswas A, Staniszewska M, Nagaraj RH. Methylglyoxal inhibits glycation-mediated loss in chaperone function and synthesis of pentosidine in alpha-crystallin. Experimental Eye Research. 84: 914-21. PMID 17368444 DOI: 10.1016/J.Exer.2007.01.013 |
0.341 |
|
2007 |
Biswas A, Goshe J, Miller A, Santhoshkumar P, Luckey C, Bhat MB, Nagaraj RH. Paradoxical effects of substitution and deletion mutation of Arg56 on the structure and chaperone function of human alphaB-crystallin. Biochemistry. 46: 1117-27. PMID 17260942 DOI: 10.1021/Bi061323W |
0.39 |
|
2007 |
Biswas A, Das KP. Alpha-crystallin assisted refolding of enzyme substrates: optimization of external parameters. The Protein Journal. 26: 247-55. PMID 17211683 DOI: 10.1007/S10930-006-9066-8 |
0.571 |
|
2007 |
Biswas A, Das KP. Differential recognition of natural and nonnatural substrate by molecular chaperone alpha-crystallin-A subunit exchange study. Biopolymers. 85: 189-97. PMID 17103422 DOI: 10.1002/Bip.20630 |
0.581 |
|
2005 |
Bhattacharjee C, Saha S, Biswas A, Kundu M, Ghosh L, Das KP. Structural changes of beta-lactoglobulin during thermal unfolding and refolding--an FT-IR and circular dichroism study. The Protein Journal. 24: 27-35. PMID 15756815 DOI: 10.1007/S10930-004-0603-Z |
0.577 |
|
2004 |
Biswas A, Das KP. SDS induced structural changes in alpha-crystallin and it's effect on refolding. The Protein Journal. 23: 529-38. PMID 15648975 DOI: 10.1007/S10930-004-7880-4 |
0.623 |
|
2004 |
Biswas A, Das KP. Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function. The Journal of Biological Chemistry. 279: 42648-57. PMID 15292216 DOI: 10.1074/Jbc.M404444200 |
0.648 |
|
2002 |
Biswas A, Saha S, Das KP. Structural Features of Molecular Chaperones: A Possible Micellar Connection Journal of Surface Science and Technology. 18: 1-24. DOI: 10.18311/Jsst/2002/2029 |
0.641 |
|
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