Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Sarata C Sahu"'
Autor:
Arash Bahrami, Marco Tonelli, Sarata C Sahu, Kiran K Singarapu, Hamid R Eghbalnia, John L Markley
Publikováno v:
PLoS ONE, Vol 7, Iss 3, p e33173 (2012)
ADAPT-NMR (Assignment-directed Data collection Algorithm utilizing a Probabilistic Toolkit in NMR) represents a groundbreaking prototype for automated protein structure determination by nuclear magnetic resonance (NMR) spectroscopy. With a [(13)C,(15
Externí odkaz:
https://doaj.org/article/f78bc75a01c141c8bb5f36ccfbf9c1a5
Letter to the Editor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::683dc5c387cdc2b69591875b82bcb340
Autor:
Claudia C. Cornilescu, Zsolt Zolnai, Brian F. Volkman, George N. Phillips, Karl W. Nichols, Sarata C. Sahu, Craig A. Bingman, Ronnie O. Frederick, Frank C. Vojtik, John L. Markley, Russell L. Wrobel, Shin-ichi Makino, Paul G. Blommel, Grzegorz Sabat, Soyoon Sarah Hwang, David J. Aceti, John G. Primm, Lai F. Bergeman, Katarzyna A. Gromek, Kory D. Seder, Brian G. Fox
Publikováno v:
Journal of Structural and Functional Genomics. 16:67-80
Vectors designed for protein production in Escherichia coli and by wheat germ cell-free translation were tested using 21 well-characterized eukaryotic proteins chosen to serve as controls within the context of a structural genomics pipeline. The cont
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b85d66f08ff2aee4ed62ae13779d3b6e
https://doi.org/10.1007/s10969-015-9198-1
https://doi.org/10.1007/s10969-015-9198-1
Autor:
David Live, Christian Gruta, Sarata C. Sahu, Laura C. Morris, James H. Prestegard, Wendy K. Nkari
Publikováno v:
Journal of Biomolecular NMR. 55:201-209
While chemical shift prediction has played an important role in aspects of protein NMR that include identification of secondary structure, generation of torsion angle constraints for structure determination, and assignment of resonances in spectra of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::459d7f7acc5c94bb0df2d93979a4813d
https://doi.org/10.1007/s10858-012-9702-x
https://doi.org/10.1007/s10858-012-9702-x
Autor:
Sandra Z. Haslam, Elaine T. Alarid, John L. Markley, Anastasia Kariagina, Sarata C. Sahu, Kelley J. Kadunc, Natalia M. Solodin, Prashant Rajbhandari, Kun Ping Lu, Greg Finn, Stephanie J. Ellison-Zelski, Kiran Kumar Singarapu
Publikováno v:
Molecular and Cellular Biology. 32:445-457
Estrogen receptor alpha (ERα), a key driver of growth in the majority of breast cancers, contains an unstructured transactivation domain (AF1) in its N terminus that is a convergence point for growth factor and hormonal activation. This domain is co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21e29a685cc6f62486758eaa95a3c988
https://doi.org/10.1128/mcb.06073-11
https://doi.org/10.1128/mcb.06073-11
Autor:
Brian F. Volkman, Karl W. Nichols, Brian G. Fox, David J. Aceti, Frank C. Vojtik, Russell L. Wrobel, John L. Markley, George N. Phillips, Craig A. Bingman, John G. Primm, Zsolt Zolnai, Sarata C. Sahu, Ronnie O. Frederick, Shin-ichi Makino
Publikováno v:
Journal of Structural and Functional Genomics
The Center for Eukaryotic Structural Genomics (CESG) is a “specialized” or “technology development” center supported by the Protein Structure Initiative (PSI). CESG’s mission is to develop improved methods for the high-throughput solution o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95795edd9c558e66753bde4af2b8aa68
http://europepmc.org/articles/PMC2705709
http://europepmc.org/articles/PMC2705709
Autor:
Elisa Domingues, Sarata C. Sahu, Tsuey Chyi Tam, Michael C. Marden, Véronique Baudin-Creuza, Chien Ho, Corinne Vasseur-Godbillon, Janel L. Giovannelli, Nancy T. Ho, Christophe Fablet
Publikováno v:
FEBS Journal. 273:230-241
We have engineered a stable octameric hemoglobin (Hb) of molecular mass 129 kDa, a dimer of recombinant hemoglobin (rHb βG83C-F41Y) tetramers joined by disulfide bonds at the β83 position. One of the major problems with oxygen carriers based on ace
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6a5d2f96a5689fe8491eab6a279c3c82
https://doi.org/10.1111/j.1742-4658.2005.05063.x
https://doi.org/10.1111/j.1742-4658.2005.05063.x
Publikováno v:
Biochemistry. 40:14392-14403
We present the three-dimensional (3D) solution structure of a calcium-binding protein from Entamoeba histolytica (EhCaBP), an etiologic agent of amoebiasis affecting millions worldwide. EhCaBP is a 14.7 kDa (134 residues) monomeric protein thought to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea8738006e8d470eefa190bff3288c9c
https://doi.org/10.1021/bi0114978
https://doi.org/10.1021/bi0114978
Publikováno v:
Journal of Biomolecular NMR. 18:107-118
Backbone dynamics of uniformly 15N-labeled free barnase and its complex with unlabelled barstar have been studied at 40 °C, pH 6.6, using 15N relaxation data obtained from proton-detected 2D {1H}-15N NMR spectroscopy. 15N spin-lattice relaxation rat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bc4591f08545a615bcabdd47a2dcf431
https://doi.org/10.1023/a:1008310402933
https://doi.org/10.1023/a:1008310402933
Publikováno v:
Proteins: Structure, Function, and Genetics. 41:460-474
Backbone dynamics of uniformly (15)N-labeled barstar have been studied at 32 degrees C, pH 6.7, by using (15)N relaxation data obtained from proton-detected 2D (1)H-(15)N NMR spectroscopy. (15)N spin-lattice relaxation rate constants (R(1)), spin-spi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36b7262f9ca6b33a3b70ad8c5eb1dd96
https://doi.org/10.1002/1097-0134(20001201)41:4<460::aid-prot40>3.0.co
https://doi.org/10.1002/1097-0134(20001201)41:4<460::aid-prot40>3.0.co