Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Mahesh S. Chandak"'
Autor:
Toshio Takenaka, Takashi Nakamura, Saeko Yanaka, Maho Yagi-Utsumi, Mahesh S Chandak, Kazunobu Takahashi, Subhankar Paul, Koki Makabe, Munehito Arai, Koichi Kato, Kunihiro Kuwajima
Publikováno v:
PLoS ONE, Vol 12, Iss 10, p e0187022 (2017)
We studied the interaction between GroES and a single-ring mutant (SR1) of GroEL by the NMR titration of 15N-labeled GroES with SR1 at three different temperatures (20, 25 and 30°C) in the presence of 3 mM ADP in 100 mM KCl and 10 mM MgCl2 at pH 7.5
Externí odkaz:
https://doaj.org/article/6700e73727f14ac1b29a2c34e8fcd593
DNA ligase I (LIG1) completes base excision repair (BER) pathway at the last nick sealing step following DNA polymerase (pol) β gap filling DNA synthesis. We previously reported that pol β 8-oxo-2’-deoxyribonucleoside 5’-triphosphate (8-oxodGTP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9510ebb2a6c1ed5555b45c9b5a65c0e9
https://doi.org/10.1101/2020.10.30.362251
https://doi.org/10.1101/2020.10.30.362251
Publikováno v:
The Journal of Biological Chemistry
DNA ligase I (LIG1) completes the base excision repair (BER) pathway at the last nick-sealing step after DNA polymerase (pol) β gap-filling DNA synthesis. However, the mechanism by which LIG1 fidelity mediates the faithful substrate–product channe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7239570e5faacca364983b765bf82fde
https://pubmed.ncbi.nlm.nih.gov/33600799
https://pubmed.ncbi.nlm.nih.gov/33600799
Autor:
Mahesh S. Chandak, Saeko Yanaka, Maho Yagi-Utsumi, Koichi Kato, Methanee Hiranyakorn, Kunihiro Kuwajima, Takashi Nakamura
Publikováno v:
Biophys J
The characterization of residual structures persistent in unfolded proteins in concentrated denaturant solution is currently an important issue in studies of protein folding because the residual structure present, if any, in the unfolded state may fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25c9b1adc2aafe08b6deec5a909aedae
https://europepmc.org/articles/PMC7732725/
https://europepmc.org/articles/PMC7732725/
Autor:
Veronica Nash, Andrew G. McKee, Hope Woods, Jens Meiler, Mahesh S. Chandak, Douglas B. Rusch, Charles P. Kuntz, Chris Hemmerich, Wesley D. Penn, Timothy C. Gruenhagen, Francis J. Roushar, Jonathan P. Schlebach
Publikováno v:
Science Advances
Sequence constraints associated with topological energetics restrict the evolution and mutational tolerance of membrane proteins.
Membrane proteins must balance the sequence constraints associated with folding and function against the hydrophobi
Membrane proteins must balance the sequence constraints associated with folding and function against the hydrophobi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7181e33c7c3b9c034c2bc6d56f3bf56e
http://europepmc.org/articles/PMC7056298
http://europepmc.org/articles/PMC7056298
Autor:
Mahesh S. Chandak, Sandeep Rai, Yashoda R Kattimani, Chander P Puri, Shibban K Kaul, Madhur Rai
Publikováno v:
MGM Journal of Medical Sciences. 3:126-130
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9620505d172834842b7dbf978ff2f9f2
https://doi.org/10.5005/jp-journals-10036-1107
https://doi.org/10.5005/jp-journals-10036-1107
Autor:
Takashi Nakamura, Takumi Yamaguchi, Koichi Kato, Mahesh S. Chandak, Kunihiro Kuwajima, Maho Yagi-Utsumi
The characterization of residual structures persistent in unfolded proteins in concentrated denaturant solution is currently an important issue in studies of protein folding, because the residual structure present, if any, in the unfolded state may f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32f6b12c741b73b16b6acd296565d457
Autor:
Subhankar Paul, Koki Makabe, Kunihiro Kuwajima, Mahesh S. Chandak, Koichi Kato, Toshio Takenaka, Munehito Arai, Maho Yagi-Utsumi, Takashi Nakamura, Saeko Yanaka, Kazunobu Takahashi
Publikováno v:
PLoS ONE, Vol 12, Iss 10, p e0187022 (2017)
PLoS ONE
PLoS ONE
We studied the interaction between GroES and a single-ring mutant (SR1) of GroEL by the NMR titration of 15N-labeled GroES with SR1 at three different temperatures (20, 25 and 30°C) in the presence of 3 mM ADP in 100 mM KCl and 10 mM MgCl2 at pH 7.5
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::943ba223e224ab5c48a61481e5e896af
http://europepmc.org/articles/PMC5653362?pdf=render
http://europepmc.org/articles/PMC5653362?pdf=render
Publikováno v:
Biophysical Journal. 116:15a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::511e1b6c0b3b962954e07ada28902285
https://doi.org/10.1016/j.bpj.2018.11.125
https://doi.org/10.1016/j.bpj.2018.11.125
Publikováno v:
Biophysical Journal. 116:63a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ab68f5b86f06d4ac13f78f8cbd392e13
https://doi.org/10.1016/j.bpj.2018.11.385
https://doi.org/10.1016/j.bpj.2018.11.385