Zobrazeno 1 - 10
of 141
pro vyhledávání: '"Kandala V R Chary"'
Publikováno v:
PLoS Pathogens, Vol 13, Iss 5, p e1006332 (2017)
Cell cycle of Entamoeba histolytica, the etiological agent of amoebiasis, follows a novel pathway, which includes nuclear division without the nuclear membrane disassembly. We report a nuclear localized Ca2+-binding protein from E. histolytica (abbre
Externí odkaz:
https://doaj.org/article/9deafd4fbb1e47389864ee55f159e571
Publikováno v:
PLoS ONE, Vol 9, Iss 9, p e106457 (2014)
Cellular metabolite analyses by (13)C-NMR showed that C. reinhardtii cells assimilate acetate at a faster rate in heterotrophy than in mixotrophy. While heterotrophic cells produced bicarbonate and CO2aq, mixotrophy cells produced bicarbonate alone a
Externí odkaz:
https://doaj.org/article/37f2cbf79d754f1982a46f365315a1ac
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e42948 (2012)
Numerous experimental techniques and computational studies, proposed in recent times, have revolutionized the understanding of protein-folding paradigm. The complete understanding of protein folding and intermediates are of medical relevance, as the
Externí odkaz:
https://doaj.org/article/33d2564146e9439c838323dba6f458ba
Autor:
Manish Shukla, Renu Minda, Himanshu Singh, Srikanth Tirumani, Kandala V R Chary, Basuthkar J Rao
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e51913 (2012)
UVI31+ is an evolutionarily conserved BolA family protein. In this study we examine the presence, localization and possible functions of this protein in the context of a unicellular alga, Chlamydomonas reinhardtii. UVI31+ in C. reinhardtii exhibits D
Externí odkaz:
https://doaj.org/article/21b93453ca5b4bf6af949af02ddc14c9
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 38:5287-5292
Communicated by Ramaswamy H. Sarma.
Autor:
Kandala V. R. Chary
Publikováno v:
Biophys Rev
It gives me great pleasure to introduce myself to the readers of Biophysical Reviews. I share a brief account of my career and experiences in biophysical research spanning four decades. For the most of this period, I have worked at the Tata Institute
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8126c620541b6d8c9f024db9d99ba647
https://europepmc.org/articles/PMC8724384/
https://europepmc.org/articles/PMC8724384/
Publikováno v:
The Journal of Physical Chemistry B. 123:10384-10393
Despite the increasing health risk from infantile cataracts, identifying the mechanism of this disease remains a challenge due to a lack of structural investigations using experimental and computational approaches. Mutations in human γS-crystallin a
Publikováno v:
Biochemical and Biophysical Research Communications. 514:901-906
Our two recent reports on the high resolution NMR structure and conformational dynamics of G57W variant of human γS-crystallin (abbreviated as γS-G57W) causing severe infantile cataracts, revealed slackening of its N-terminal domain with enhanced l
Publikováno v:
Biochemical and Biophysical Research Communications. 514:946-952
Transient excited states in proteins can be accurately probed from temperature dependence of amide proton (1HN) chemical shifts displaying significant curvatures. Characterizing these near-native alternative states is of high therapeutic relevance in
Autor:
Rakesh Joshi, Glenn F. King, Janeka Gartia, Raveendra Anangi, Ashok P. Giri, Ravi Pratap Barnwal, Kandala V. R. Chary
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 38:1388-1397
Although several plant protease inhibitors have been structurally characterized using X-ray crystallography, very few have been studied using NMR techniques. Here, we report an NMR study of the sol...