about
Hydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimicsInteraction of ATP with a small heat shock protein from Mycobacterium leprae: effect on its structure and functionRole of Subunit Exchange and Electrostatic Interactions on the Chaperone Activity of Mycobacterium leprae HSP18Differential role of arginine mutations on the structure and functions of α-crystallin.Synthesis, X-ray structure and in vitro cytotoxicity studies of Cu(I/II) complexes of thiosemicarbazone: special emphasis on their interactions with DNA.Evaluation of the cell cytotoxicity and DNA/BSA binding and cleavage activity of some dioxidovanadium(V) complexes containing aroylhydrazones.Acetylation of αA-crystallin in the human lens: effects on structure and chaperone function.The C-terminal extension of Mycobacterium tuberculosis Hsp16.3 regulates its oligomerization, subunit exchange dynamics and chaperone function.Mercury based drug in ancient India: The red sulfide of mercury in nanoscale.A S52P mutation in the 'α-crystallin domain' of Mycobacterium leprae HSP18 reduces its oligomeric size and chaperone function.Monomeric and Dimeric Oxidomolybdenum(V and VI) Complexes, Cytotoxicity, and DNA Interaction Studies: Molybdenum Assisted C═N Bond Cleavage of Salophen Ligands.A study of DNA/BSA interaction and catalytic potential of oxidovanadium(v) complexes with ONO donor ligands.Probing the structure-function relationship of Mycobacterium leprae HSP18 under different UV radiationsDepicting the DNA binding and photo-nuclease ability of anti-mycobacterial drug rifampicin: A biophysical and molecular docking perspectiveEvidences for zinc (II) and copper (II) ion interactions with Mycobacterium leprae HSP18: Effect on its structure and chaperone functionThe impact of different mutations at arginine141 on the structure, subunit exchange dynamics and chaperone activity of Hsp16.3.DNA minor groove binding of a well known anti-mycobacterial drug dapsone: A spectroscopic, viscometric and molecular docking study
P50
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P50
description
researcher ORCID ID = 0000-0002-4452-993X
@en
wetenschapper
@nl
name
Alok Kumar Panda
@ast
Alok Kumar Panda
@en
Alok Kumar Panda
@es
Alok Kumar Panda
@nl
type
label
Alok Kumar Panda
@ast
Alok Kumar Panda
@en
Alok Kumar Panda
@es
Alok Kumar Panda
@nl
prefLabel
Alok Kumar Panda
@ast
Alok Kumar Panda
@en
Alok Kumar Panda
@es
Alok Kumar Panda
@nl
P106
P1153
54581436700
P31
P496
0000-0002-4452-993X