Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Maria Tordova"'
Autor:
Andrew Howard, Gary L. Gilliland, Edward Eisenstein, Galina Obmolova, Narmada Thanki, Maria Tordova, Alexey Teplyakov, Nicklas Bonander
Publikováno v:
Proteins: Structure, Function, and Genetics. 48:220-226
A hypothetical protein encoded by the gene YjeE of Haemophilus influenzae was selected as part of a structural genomics project for X-ray analysis to assist with the functional assignment. The protein is considered essential to bacteria because the g
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6a16ff4d0ce56c668a2f6c32f8feaaf
https://doi.org/10.1002/prot.10114
https://doi.org/10.1002/prot.10114
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 56:996-1001
Quality data collection for macromolecular cryocrystallography requires suppressing the formation of crystalline or microcrystalline ice that may result from flash-freezing crystals. Described here is the use of lithium formate, lithium chloride and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::913e80268553c901cd76354043344730
https://doi.org/10.1107/s0907444900007587
https://doi.org/10.1107/s0907444900007587
Autor:
Jane E. Ladner, Andrew Howard, Gary L. Gilliland, Andrew M. Davis, Maria Tordova, Prasad T. Reddy
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 56:673-683
The crystal structure of the Bacillus subtilis chorismate mutase, an enzyme of the aromatic amino acids biosynthetic pathway, was determined to 1.30 A resolution. The structure of the homotrimer was determined by molecular replacement using orthorhom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7402cbc3604e63cd4ce37aa6dc1b1c95
https://doi.org/10.1107/s0907444900004625
https://doi.org/10.1107/s0907444900004625
The three-dimensional structures of two isoforms of nucleoside diphosphate kinase from bovine retina
Autor:
Najmoutin G. Abdulaev, Kevin D. Ridge, Maria Tordova, Gary L. Gilliland, Dmitri L. Kakuev, Jane E. Ladner
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 55:1127-1135
The crystal structures of two isoforms of nucleoside diphosphate kinase from bovine retina overexpressed in Escherischia coli have been determined to 2.4 Å resolution. Both the isoforms, NBR-A and NBR-B, are hexameric and the fold of the monomer is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::445e7dd9a9beae07734151e7dbc8278f
https://doi.org/10.1107/s0907444999002528
https://doi.org/10.1107/s0907444999002528
Autor:
Jaya Jagadeesh, Gary L. Gilliland, Alexander C. Drohat, Gaoyi Xiao, James T. Stivers, Maria Tordova
Publikováno v:
Proteins: Structure, Function, and Genetics. 35:13-24
The DNA repair enzyme uracil DNA glycosylase (UDG) catalyzes the hydrolysis of premu- tagenic uracil residues from single-stranded or du- plex DNA, producing free uracil and abasic DNA. Here we report the high-resolution crystal struc- tures of free
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0e9f6be65fe11d3fa469d286c0315fc7
https://doi.org/10.1002/(sici)1097-0134(19990401)35:1<13::aid-prot2>3.0.co
https://doi.org/10.1002/(sici)1097-0134(19990401)35:1<13::aid-prot2>3.0.co
Publikováno v:
Journal of Molecular Biology. 278:641-653
The crystal structure of unliganded mutant R111M of human cellular retinoic acid-binding protein type II (apo-CRABPII (R111M)) has been determined at 2.3 A and refined to a crystallographic R-factor of 0. 18. Although the mutant protein has lower aff
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abcbd340b702306b69cdc57b48904c97
https://doi.org/10.1006/jmbi.1998.1734
https://doi.org/10.1006/jmbi.1998.1734
Publikováno v:
Journal of Biological Chemistry. 273:11770-11775
The murine monoclonal IgG1 antibody 7A9 binds specifically to the endothelial leukocyte adhesion molecule-1 (E-selectin), inhibiting the attachment of neutrophils to endothelial cells. The primary and three-dimensional structures of the Fab fragment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81522e62a39d90ea4dfa431b75dc7dde
https://doi.org/10.1074/jbc.273.19.11770
https://doi.org/10.1074/jbc.273.19.11770
Autor:
Maria Tordova, Gary L. Gilliland, Travis Gallagher, Joel Hoskins, Orna Almog, Philip N. Bryan
Publikováno v:
Proteins: Structure, Function, and Genetics. 31:21-32
The three-dimensional struc- ture of a subtilisin BPN8 construct that was produced and folded without its prodomain shows the tertiary structure is nearly identical to the wild-type enzyme and not a folding interme- diate. The subtilisin BPN8 variant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::509b68a8dab169a9936a5c9a34367874
https://doi.org/10.1002/(sici)1097-0134(19980401)31:1<21::aid-prot3>3.0.co
https://doi.org/10.1002/(sici)1097-0134(19980401)31:1<21::aid-prot3>3.0.co
Autor:
Eugene Melamud, Edward Eisenstein, Osnat Herzberg, Aleksandra Tempczyk, Narmada Thanki, Galina Obmolova, Maria Tordova, Nicklas Bonander, Deok Cheon Yeh, John Moult, James F. Parsons, Wojciech W. Krajewski, Hong Zhang, Kap Lim, Jane E. Ladner, Gary L. Gilliland, John Orban, J. Toedt, Andrew Howard, Prasad T. Reddy, Alexey Teplyakov, C. V. Rao, Kui Huang, Lisa Parsons, Zhong Li, Kathryn E. Fisher
Publikováno v:
Europe PubMed Central
The three-dimensional structures of Haemophilus influenzae proteins whose biological functions are unknown are being determined as part of a structural genomics project to ask whether structural information can assist in assigning the functions of pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3991374baec2d3c8df5d6cd95550a7b
https://pubmed.ncbi.nlm.nih.gov/12570740
https://pubmed.ncbi.nlm.nih.gov/12570740
Autor:
Maria Tordova, Gary L. Gilliland, Frederick P. Schwarz, Inna Gorshkova, Ying Shi, Shenglun Wang, Seung Y. Chu
Publikováno v:
The Journal of biological chemistry. 276(14)
The x-ray crystal structure of the cAMP-ligated T127L/S128A double mutant of cAMP receptor protein (CRP) was determined to a resolution of 2.2 A. Although this structure is close to that of the x-ray crystal structure of cAMP-ligated CRP with one sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::006db37a2fa706e7ac88a1f1c12e3469
https://pubmed.ncbi.nlm.nih.gov/11124966
https://pubmed.ncbi.nlm.nih.gov/11124966