Purnananda Guptasarma
Purnananda Guptasarma
Professor of Biological Sciences, Indian Institute of Science Education & Research (IISER) Mohali
Verified email at iisermohali.ac.in - Homepage
Title
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Year
Does replication‐induced transcription regulate synthesis of the myriad low copy number proteins of Escherichia coli?
P Guptasarma
Bioessays 17 (11), 987-997, 1995
1701995
Hydroxyl radical mediated damage to proteins, with special reference to the crystallins
P Guptasarma, D Balasubramanian, S Matsugo, I Saito
Biochemistry 31 (17), 4296-4303, 1992
1471992
Hydroxyl radical mediated damage to proteins, with special reference to the crystallins
P Guptasarma, D Balasubramanian, S Matsugo, I Saito
Biochemistry 31 (17), 4296-4303, 1992
1451992
A novel UV laser-induced visible blue radiation from protein crystals and aggregates: scattering artifacts or fluorescence transitions of peptide electrons delocalized through …
A Shukla, S Mukherjee, S Sharma, V Agrawal, KVR Kishan, ...
Archives of biochemistry and biophysics 428 (2), 144-153, 2004
752004
Use of a hydrophobic dye to indirectly probe the structural organization and conformational plasticity of molecules in amorphous aggregates of carbonic anhydrase
B Kundu, P Guptasarma
Biochemical and biophysical research communications 293 (1), 572-577, 2002
572002
Reversal of peptide backbone direction may result in the mirroring of protein structure
P Guptasarma
FEBS letters 310 (3), 205-210, 1992
571992
Hydrophobic dye inhibits aggregation of molten carbonic anhydrase during thermal unfolding and refolding
B Kundu, P Guptasarma
Proteins: Structure, Function, and Bioinformatics 37 (3), 321-324, 1999
471999
Dityrosine formation in the proteins of the eye lens
P Guptasarma, D Balasubramanian
Current eye research 11 (11), 1121-1125, 1992
311992
Single‐step purification of a protein‐folding catalyst, the SlyD peptidyl prolyl isomerase (PPI), from cytoplasmic extracts of Escherichia coli
S Mukherjee, A Shukla, P Guptasarma
Biotechnology and applied biochemistry 37 (2), 183-186, 2003
262003
Solution-state characteristics of the ultraviolet A-induced visible fluorescence from proteins
P Guptasarma
Archives of biochemistry and biophysics 478 (2), 127-129, 2008
252008
The Achilles’ Heel of “Ultrastable” Hyperthermophile Proteins: Submillimolar Concentrations of SDS Stimulate Rapid Conformational Change, Aggregation, and Amyloid Formation in …
JM Khan, P Sharma, K Arora, N Kishor, P Kaila, P Guptasarma
Biochemistry 55 (28), 3920-3936, 2016
222016
Cooperative relaxation of supercoils and periodic transcriptional initiation within polymerase batteries
P Guptasarma
Bioessays 18 (4), 325-332, 1996
221996
Putative structure and characteristics of a red water-soluble pigment secreted by Penicillium marneffei
S Bhardwaj, A Shukla, S Mukherjee, S Sharma, P Guptasarma, ...
Medical mycology 45 (5), 419-427, 2007
192007
A backbone-reversed form of an all-β α-crystallin domain from a small heat-shock protein (retro-HSP12. 6) folds and assembles into structured multimers
A Shukla, M Raje, P Guptasarma
Journal of Biological Chemistry 278 (29), 26505-26510, 2003
192003
Symmetry transformations at α-carbons
P Guptasarma
Trends in Biotechnology 2 (14), 42-43, 1996
181996
Expression, purification, refolding and characterization of a putative lysophospholipase from Pyrococcus furiosus: Retention of structure and lipase/esterase activity …
SK Chandrayan, N Dhaunta, P Guptasarma
Protein expression and purification 59 (2), 327-333, 2008
152008
The excised heat-shock domain of αB crystallin is a folded, proteolytically susceptible trimer with significant surface hydrophobicity and a tendency to self-aggregate upon heating
B Kundu, A Shukla, R Chaba, P Guptasarma
Protein expression and purification 36 (2), 263-271, 2004
152004
Folding of β/α‐unit scrambled forms of S. cerevisiae triosephosphate isomerase: Evidence for autonomy of substructure formation and plasticity of hydrophobic and hydrogen …
A Shukla, P Guptasarma
PROTEINS: Structure, Function, and Bioinformatics 55 (3), 548-557, 2004
152004
Calcium binding to beta-2-microglobulin at physiological pH drives the occurrence of conformational changes which cause the protein to precipitate into amorphous forms that …
S Kumar, P Sharma, K Arora, M Raje, P Guptasarma
PloS one 9 (4), e95725, 2014
142014
Replacement of the active surface of a thermophile protein by that of a homologous mesophile protein through structure-guided ‘protein surface grafting’
D Kapoor, V Kumar, SK Chandrayan, S Ahmed, S Sharma, M Datt, ...
Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics 1784 (11), 1771-1776, 2008
142008
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