Zobrazeno 1 - 10 of 13 pro vyhledávání: '"W. C. Stallings"'
1
In vitro Sequential Selection and Characterization of Human Immunodeficiency Virus Type 1 Variants with Reduced Sensitivity to Hydroxyethylurea Protease Inhibitors
Autor: Simon P. Tucker, W. C. Stallings, T. R. Stiebel, Karen E. Potts, Joseph J. McDonald, Mary Smidt, Martin L. Bryant
Publikováno v: Antiviral Chemistry and Chemotherapy. 8:447-456
In vitro resistance to the human immunodeficiency virus (HIV) protease inhibitors SC-52151 and SC-55389A was evaluated in an in vitro sequential selection scheme. HIVRF variants were selected for reduced sensitivity to SC-52151 and subsequently passa
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6f8c4d0804677bf0994220417f83322a
https://doi.org/10.1177/095632029700800508
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2
A mutation in human immunodeficiency virus type 1 protease at position 88, located outside the active site, confers resistance to the hydroxyethylurea inhibitor SC-55389A
Autor: L Blystone, D Pillay, Karen E. Potts, Martin L. Bryant, Simon P. Tucker, W. C. Stallings, Mary Smidt, T. R. Stiebel, D D Richman, Joseph J. McDonald
Publikováno v: Antimicrobial Agents and Chemotherapy. 41:515-522
The hydroxyethylurea human immunodeficiency virus type 1 (HIV-1) protease inhibitors SC-55389A and SC-52151 were used to select drug-resistant variants in vitro. One clinical HIV-1 strain (89-959) and one laboratory HIV-1 strain (LAI) were passaged i
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16db6aa83e299a33a5a2349b4c436df3
https://doi.org/10.1128/aac.41.3.515
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3
Manganese superoxide dismutase from Thermus thermophilus. A structural model refined at 1.8 A resolution
Autor: M L, Ludwig, A L, Metzger, K A, Pattridge, W C, Stallings
Publikováno v: Journal of molecular biology. 219(2)
The structure of Mn(III) superoxide dismutase (Mn(III)SOD) from Thermus thermophilus, a tetramer of chains 203 residues in length, has been refined by restrained least-squares methods. The R-factor [formula: see text] for the 54,056 unique reflection
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b8d79142b88474537cca669b5a82e8eb
https://pubmed.ncbi.nlm.nih.gov/2038060
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5
Ethylenediamine citrate
Autor: N. Gavrushenko, H. L. Carrell, W. C. Stallings, J. P. Glusker
Publikováno v: Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 33:3936-3939
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8488802ea6c291de9262d6fd33ea9f6e
https://doi.org/10.1107/s0567740877012515
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9
Crystallographic studies of Escherichia coli citrate synthase
Autor: B H, Rubin, W C, Stallings, J P, Glusker, M E, Bayer, J, Janin, P A, Srere
Publikováno v: The Journal of biological chemistry. 258(2)
The citrate synthase from Escherichia coli B has been crystallized in a cubic space group with a unit cell spacing of 220 A. X-ray diffraction, electron microscopy, symmetry considerations, and low resolution projection Patterson syntheses are consis
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9dc3586ba40b7442ac1bba3265cb0b85
https://pubmed.ncbi.nlm.nih.gov/6337135
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10
Characterization of crystals of tetrameric manganese superoxide dismutase from Thermus thermophilus HB8
Autor: W C, Stallings, K A, Pattridge, T B, Powers, J A, Fee, M L, Ludwig
Publikováno v: The Journal of biological chemistry. 256(11)
The tetrameric manganese superoxide dismutase from the extreme thermophile Thermus thermophilus HB8 crystallizes in space group P41212 (or its enantiomorph) with a = b = 147.5 A, c = 55.9 A. The diffraction patterns extent to 1.4 A, and the crystals
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c09de953ab64f86950afb319b6182de2
https://pubmed.ncbi.nlm.nih.gov/7240177
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