Zobrazeno 1 - 10 of 189 pro vyhledávání: '"Ed, Getzoff"'
1
Structural basis for hemophilia A caused by mutations in the C domains of blood coagulation factor VIII
Autor: Aj, Gale, Jean-Luc Pellequer, Ed, Getzoff, Jh, Griffin
Publikováno v: Europe PubMed Central
Three dimensional homology models for the C1 and C2 domains of factor VIII (FVIII) were generated. Each C domain formed a beta-sandwich, and C1 was covalently connected to C2 in a head-to-head orientation. Of the250 missense mutations that cause FVII
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::0407f853d08be4f6cd3925501a0e63ac
https://pubmed.ncbi.nlm.nih.gov/10669159
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2
Electrostatic orientation of the electron-transfer complex between plastocyanin and cytochrome c
Autor: Va, Roberts, Hc, Freeman, Aj, Olson, John Tainer, Ed, Getzoff
Publikováno v: Europe PubMed Central
To understand the specificity and efficiency of protein-protein interactions promoting electron transfer, we evaluated the role of electrostatic forces in precollision orientation by the development of two new methods, computer graphics alignment of
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::9c51dc11538941cc35385e80afc96e6a
https://pubmed.ncbi.nlm.nih.gov/1649191
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3
Genetically engineered polymers of human CuZn superoxide dismutase. Biochemistry and serum half-lives
Autor: Ra, Hallewell, Laria I, Tabrizi A, Carlin G, Ed, Getzoff, John Tainer, Ls, Cousens, Gt, Mullenbach
Publikováno v: Europe PubMed Central
CuZn superoxide dismutase is a highly stable dimer of identical subunits with a combined molecular mass of 32,000 daltons. Two human superoxide dismutase genes have been joined in the same translational reading frame, using spacers of different lengt
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::8836095f1464b3e4cab5279b4b03e6d1
https://pubmed.ncbi.nlm.nih.gov/2647749
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4
Crystallographic characterization of recombinant human CuZn superoxide dismutase
Autor: He, Parge, Ed, Getzoff, Cs, Scandella, Ra, Hallewell, John Tainer
Publikováno v: Europe PubMed Central
Recombinant human CuZn superoxide dismutase as expressed in yeast has been crystallized in three different crystal forms. Hexagonal plates grow from 2.4 M ammonium sulfate, pH 7.5, and belong to the space group P6(3)22, with cell dimensions a = b = 1
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::15bee32e4f533b87f8c9850a821da75b
http://europepmc.org/abstract/med/3782115
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5
Changes in crystallographic structure and thermostability of a Cu,Zn superoxide dismutase mutant resulting from the removal of a buried cysteine
Autor: McRee DE, Sm, Redford, Ed, Getzoff, Jr, Lepock, Ra, Hallewell, John Tainer
Publikováno v: Europe PubMed Central
In principle, protein thermostability depends on efficient interior packing of apolar residues and on avoidance of irreversible denaturation in the unfolded state. To study these effects, the single free cysteine in the highly stable enzyme bovine Cu
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::b6574812c5fab7ea7b049727276a9839
http://europepmc.org/abstract/med/2387847
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6
Biochemical purification and crystallographic characterization of the fiber-forming protein pilin from Neisseria gonorrhoeae
Autor: He, Parge, Sl, Bernstein, Cd, Deal, McRee DE, Christensen D, Ma, Capozza, Bw, Kays, Tm, Fieser, Draper D, So M, Ed, Getzoff, John Tainer
Publikováno v: Europe PubMed Central
Pilus fibers are long protein filaments on many pathogenic bacteria that participate in attachment to host cells. Although the self-assembling protein pilin is the major structural component of the Neisseria gonorrhoeae pilus fiber, several other pro
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::862b1b8a2ff0da11e6c7bf69370fc562
http://europepmc.org/abstract/med/1967608
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7
Three-dimensional model of coagulation factor Va bound to activated protein C
Autor: Jean-Luc Pellequer, Aj, Gale, Ed, Getzoff, Jh, Griffin
Publikováno v: Europe PubMed Central
A complete molecular model of blood coagulation factor Va (FVa) bound to anticoagulant activated protein C (APC) and to a phospholipid membrane was constructed. The three homologous A domains and the two homologous C domains of FVA were modeled based
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::885f09ad4c9bca1cd0897db6aba988d7
http://europepmc.org/abstract/med/11127867
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10
Akademický článek
Structural Changes during the Photorepair and Binding Processes of Xenopus (6-4) Photolyase with (6-4) Photoproducts in Single- and Double-Stranded DNA.
Autor: Yamada D; Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.; Graduate School of Science, University of Hyogo, Hyogo 678-1297, Japan., Yamamoto J; Graduate School of Engineering Science, Osaka University, Toyonaka, Osaka 560-8531, Japan., Getzoff ED; Department of Integrative Structural and Computational Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, United States.; Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, United States., Iwata T; Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.; Faculty of Pharmaceutical Sciences, Toho University, Funabashi, Chiba 274-8510, Japan., Kandori H; Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.
Publikováno v: Biochemistry [Biochemistry] 2021 Nov 02; Vol. 60 (43), pp. 3253-3261. Date of Electronic Publication: 2021 Oct 17.
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