Year |
Citation |
Score |
2021 |
Bhatia S, Krishnamoorthy G, Udgaonkar JB. Resolving Site-Specific Heterogeneity of the Unfolded State under Folding Conditions. The Journal of Physical Chemistry Letters. 3295-3302. PMID 33764778 DOI: 10.1021/acs.jpclett.1c00098 |
0.578 |
|
2021 |
Bhatia S, Krishnamoorthy G, Udgaonkar JB. Mapping Distinct Sequences of Structure Formation Differentiating Multiple Folding Pathways of a Small Protein. Journal of the American Chemical Society. PMID 33430589 DOI: 10.1021/jacs.0c11097 |
0.566 |
|
2019 |
Mariam J, Krishnamoorthy G, Anand R. Use of 6-Methylisoxanthopterin, a Fluorescent Guanine Analog, to Probe Fob1-Mediated Dynamics at the Stalling Fork Barrier DNA Sequences. Chemistry, An Asian Journal. PMID 31647188 DOI: 10.1002/Asia.201901061 |
0.32 |
|
2019 |
Bhatia S, Krishnamoorthy G, Dhar D, Udgaonkar JB. Observation of Continuous Contraction and a Metastable Misfolded State during the Collapse and Folding of a Small Protein. Journal of Molecular Biology. PMID 31330152 DOI: 10.1016/j.jmb.2019.07.024 |
0.618 |
|
2019 |
Krishnamoorthy G, Dogra SK. Twisted Intramolecular Charge Transfer Emission of 2-(4'-N,N-dimethylaminophenyl)benzimidazole in Micelles. Journal of Colloid and Interface Science. 213: 53-61. PMID 10191006 DOI: 10.1006/jcis.1999.6091 |
0.306 |
|
2017 |
Biswas A, Mariam J, Kombrabail M, Narayan S, Krishnamoorthy G, Anand R. Site-Specific Fluorescence Dynamics To Probe Polar Arrest by Fob1 in Replication Fork Barrier Sequences. Acs Omega. 2: 7389-7399. PMID 30023550 DOI: 10.1021/acsomega.7b01117 |
0.324 |
|
2017 |
Bhatia S, Krishnamoorthy G, Udgaonkar JB. Site-specific time-resolved FRET reveals local variations in the unfolding mechanism in an apparently two-state protein unfolding transition. Physical Chemistry Chemical Physics : Pccp. PMID 29085950 DOI: 10.1039/c7cp06214a |
0.572 |
|
2013 |
Kishore M, Krishnamoorthy G, Udgaonkar JB. Critical evaluation of the two-state model describing the equilibrium unfolding of the PI3K SH3 domain by time-resolved fluorescence resonance energy transfer. Biochemistry. 52: 9482-96. PMID 24325755 DOI: 10.1021/Bi401337K |
0.651 |
|
2013 |
Sarkar SS, Udgaonkar JB, Krishnamoorthy G. Unfolding of a small protein proceeds via dry and wet globules and a solvated transition state. Biophysical Journal. 105: 2392-402. PMID 24268151 DOI: 10.1016/j.bpj.2013.09.048 |
0.629 |
|
2012 |
Jha A, Narayan S, Udgaonkar JB, Krishnamoorthy G. Solvent-induced tuning of internal structure in a protein amyloid protofibril. Biophysical Journal. 103: 797-806. PMID 22947941 DOI: 10.1016/j.bpj.2012.07.021 |
0.601 |
|
2011 |
Sarkar SS, Udgaonkar JB, Krishnamoorthy G. Reduced fluorescence lifetime heterogeneity of 5-fluorotryptophan in comparison to tryptophan in proteins: implication for resonance energy transfer experiments. The Journal of Physical Chemistry. B. 115: 7479-86. PMID 21574591 DOI: 10.1021/Jp2016984 |
0.623 |
|
2011 |
Dash N, Mishra A, Krishnamoorthy G. Comment on "The interaction of 5-(alkoxy)naphthalen-1-amine with bovine serum albumin and its effect on the conformation of protein". The Journal of Physical Chemistry. B. 115: 6806-7; discussion 6. PMID 21539322 DOI: 10.1021/Jp111012W |
0.317 |
|
2011 |
Jha A, Ishii K, Udgaonkar JB, Tahara T, Krishnamoorthy G. Exploration of the correlation between solvation dynamics and internal dynamics of a protein. Biochemistry. 50: 397-408. PMID 21141874 DOI: 10.1021/Bi101440C |
0.571 |
|
2010 |
Haldar S, Kombrabail M, Krishnamoorthy G, Chattopadhyay A. Monitoring membrane protein conformational heterogeneity by fluorescence lifetime distribution analysis using the maximum entropy method. Journal of Fluorescence. 20: 407-13. PMID 19816758 DOI: 10.1007/S10895-009-0554-Z |
0.304 |
|
2010 |
Noothi SK, Kombrabail M, Rao BJ, Krishnamoorthy G. Fluorescence characterization of the structural heterogeneity of polytene chromosomes Journal of Fluorescence. 20: 37-41. PMID 19629653 DOI: 10.1007/s10895-009-0519-2 |
0.351 |
|
2009 |
Jha A, Udgaonkar JB, Krishnamoorthy G. Characterization of the heterogeneity and specificity of interpolypeptide interactions in amyloid protofibrils by measurement of site-specific fluorescence anisotropy decay kinetics. Journal of Molecular Biology. 393: 735-52. PMID 19716830 DOI: 10.1016/j.jmb.2009.08.053 |
0.627 |
|
2009 |
Jha SK, Dhar D, Krishnamoorthy G, Udgaonkar JB. Continuous dissolution of structure during the unfolding of a small protein. Proceedings of the National Academy of Sciences of the United States of America. 106: 11113-8. PMID 19553216 DOI: 10.1073/pnas.0812564106 |
0.635 |
|
2008 |
Kumar S, Singh AK, Krishnamoorthy G, Swaminathan R. Thioflavin T displays enhanced fluorescence selectively inside anionic micelles and mammalian cells. Journal of Fluorescence. 18: 1199-205. PMID 18506603 DOI: 10.1007/S10895-008-0378-2 |
0.7 |
|
2007 |
Bandyopadhyay AK, Krishnamoorthy G, Padhy LC, Sonawat HM. Kinetics of salt-dependent unfolding of [2Fe-2S] ferredoxin of Halobacterium salinarum. Extremophiles : Life Under Extreme Conditions. 11: 615-25. PMID 17406782 DOI: 10.1007/s00792-007-0075-0 |
0.339 |
|
2006 |
Saxena AM, Udgaonkar JB, Krishnamoorthy G. Characterization of intra-molecular distances and site-specific dynamics in chemically unfolded barstar: evidence for denaturant-dependent non-random structure. Journal of Molecular Biology. 359: 174-89. PMID 16603185 DOI: 10.1016/j.jmb.2006.03.013 |
0.639 |
|
2006 |
Mukhopadhyay S, Nayak PK, Udgaonkar JB, Krishnamoorthy G. Characterization of the formation of amyloid protofibrils from barstar by mapping residue-specific fluorescence dynamics. Journal of Molecular Biology. 358: 935-42. PMID 16546212 DOI: 10.1016/J.Jmb.2006.02.006 |
0.711 |
|
2005 |
Saxena AM, Udgaonkar JB, Krishnamoorthy G. Protein dynamics control proton transfer from bulk solvent to protein interior: a case study with a green fluorescent protein. Protein Science : a Publication of the Protein Society. 14: 1787-99. PMID 15937281 DOI: 10.1110/ps.051391205 |
0.591 |
|
2004 |
Mukhopadhyay S, Maitra U, Ira I, Krishnamoorthy G, Schmidt J, Talmon Y. Structure and dynamics of a molecular hydrogel derived from a tripodal cholamide. Journal of the American Chemical Society. 126: 15905-14. PMID 15571416 DOI: 10.1021/Ja046788T |
0.645 |
|
2004 |
Sridevi K, Lakshmikanth GS, Krishnamoorthy G, Udgaonkar JB. Increasing stability reduces conformational heterogeneity in a protein folding intermediate ensemble. Journal of Molecular Biology. 337: 699-711. PMID 15019788 DOI: 10.1016/j.jmb.2003.12.083 |
0.551 |
|
2003 |
Krishnamoorthy G. Fluorescence spectroscopy in molecular description of biological processes Indian Journal of Biochemistry and Biophysics. 40: 147-159. PMID 22900304 |
0.327 |
|
2003 |
Rami BR, Krishnamoorthy G, Udgaonkar JB. Dynamics of the core tryptophan during the formation of a productive molten globule intermediate of barstar. Biochemistry. 42: 7986-8000. PMID 12834351 DOI: 10.1021/Bi030006B |
0.583 |
|
2001 |
Lakshmikanth GS, Sridevi K, Krishnamoorthy G, Udgaonkar JB. Structure is lost incrementally during the unfolding of barstar. Nature Structural Biology. 8: 799-804. PMID 11524685 DOI: 10.1038/nsb0901-799 |
0.666 |
|
2001 |
Bandyopadhyay AK, Krishnamoorthy G, Sonawat HM. Structural stabilization of [2Fe-2S] ferredoxin from Halobacterium salinarum Biochemistry. 40: 1284-1292. PMID 11170454 DOI: 10.1021/bi001614j |
0.309 |
|
2000 |
Sridevi K, Juneja J, Bhuyan AK, Krishnamoorthy G, Udgaonkar JB. The slow folding reaction of barstar: the core tryptophan region attains tight packing before substantial secondary and tertiary structure formation and final compaction of the polypeptide chain. Journal of Molecular Biology. 302: 479-95. PMID 10970747 DOI: 10.1006/jmbi.2000.4060 |
0.626 |
|
1999 |
Lakshmikanth GS, Krishnamoorthy G. Solvent-exposed trytophans probe the dynamics at protein surfaces Biophysical Journal. 77: 1100-1106. PMID 10423454 |
0.301 |
|
1997 |
Srivastava A, Krishnamoorthy G. Time-resolved fluorescence microscopy could correct for probe binding while estimating intracellular pH Analytical Biochemistry. 249: 140-146. PMID 9212865 DOI: 10.1006/abio.1997.2164 |
0.323 |
|
1996 |
Swaminathan R, Nath U, Udgaonkar JB, Periasamy N, Krishnamoorthy G. Motional dynamics of a buried tryptophan reveals the presence of partially structured forms during denaturation of barstar. Biochemistry. 35: 9150-7. PMID 8703920 DOI: 10.1021/Bi9603478 |
0.741 |
|
1994 |
Swaminathan R, Krishnamoorthy G, Periasamy N. Similarity of fluorescence lifetime distributions for single tryptophan proteins in the random coil state Biophysical Journal. 67: 2013-2023. PMID 7858139 DOI: 10.1016/S0006-3495(94)80685-X |
0.686 |
|
1992 |
Ahmed I, Krishnamoorthy G. The non-equivalence of binding sites of coenzyme quinone and rotenone in mitochondrial NADH-CoQ reductase Febs Letters. 300: 275-278. PMID 1313376 DOI: 10.1016/0014-5793(92)80862-B |
0.317 |
|
1987 |
Krishnamoorthy G, Periasamy N, Venkataraman B. On the origin of heterogeneity of fluorescence decay kinetics of reduced nicotinamide adenine dinucleotide Biochemical and Biophysical Research Communications. 144: 387-392. PMID 3579915 DOI: 10.1016/S0006-291X(87)80522-3 |
0.31 |
|
1982 |
Krishnamoorthy G, Prabhananda BS. Phenolsulfophthalein dyes as probes in the study of lysozyme activity towards cell wall substrates Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 709: 234-246. PMID 7150607 DOI: 10.1016/0167-4838(82)90466-6 |
0.717 |
|
1982 |
Krishnamoorthy G, Prabhananda BS. Binding site of the dye in bromophenol blue-lysozyme complex proton magnetic resonance study in aqueous solutions Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 709: 53-57. PMID 7150603 DOI: 10.1016/0167-4838(82)90420-4 |
0.72 |
|
1979 |
Krishnamoorthy G, Prabhananda BS, Gurnani S. Bromophenol red as a probe of lysozyme-active site environment: a temperature-jump study Biopolymers - Peptide Science Section. 18: 1937-1963. PMID 497350 |
0.7 |
|
Show low-probability matches. |