Year |
Citation |
Score |
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 |
0.764 |
|
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 |
0.764 |
|
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 |
0.767 |
|
2019 |
Nahomi RB, Nandi SK, Rakete S, Michel C, Fritz KS, Nagaraj RH. Lysine malonylation and propionylation are prevalent in human lens proteins. Experimental Eye Research. 107864. PMID 31678036 DOI: 10.1016/J.Exer.2019.107864 |
0.357 |
|
2019 |
Nahomi RB, Nandi SK, Nagaraj RH. A monoclonal antibody targeted to the functional peptide of αB-crystallin inhibits the chaperone and anti-apoptotic activities. Journal of Immunological Methods. PMID 30738041 DOI: 10.1016/J.Jim.2019.02.004 |
0.373 |
|
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 |
0.746 |
|
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 |
0.741 |
|
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 |
0.787 |
|
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 |
0.782 |
|
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 |
0.787 |
|
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 |
0.759 |
|
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 |
0.795 |
|
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 |
0.63 |
|
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 |
0.664 |
|
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 |
0.791 |
|
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