Zobrazeno 1 - 9 of 9 pro vyhledávání: '"B M, McKeever"'
2
New isomeric classes of topically active ocular hypotensive carbonic anhydrase inhibitors: 5-substituted thieno[2,3-b]thiophene-2-sulfonamides and 5-substituted thieno[3,2-b]thiophene-2-sulfonamides
Autor: Harvey Schwam, John M. Sondey, Robert L. Smith, B. M. Mckeever, Michelson, James P. Springer, Pierre Mallorga, Murcko Mark A, George D. Hartman, John D. Prugh
Publikováno v: Journal of Medicinal Chemistry. 34:1805-1818
A series of 5-substituted thieno[2,3-b]- and thieno[3,2-b)- and thieno[3,2-b)thiophene-2-sulfonamides was prepared and evaluated for topical ocular hypotensive activity in glaucoma models. The 5-substituents were varied to maximize both inhibitory po
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5b999cc942df6d9a360ce4ed63b7052
https://doi.org/10.1021/jm00110a008
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3
Positions of His-64 and a bound water in human carbonic anhydrase II upon binding three structurally related inhibitors
Autor: G M, Smith, R S, Alexander, D W, Christianson, B M, McKeever, G S, Ponticello, J P, Springer, W C, Randall, J J, Baldwin, C N, Habecker
Publikováno v: Protein science : a publication of the Protein Society. 3(1)
The 3-dimensional structure of human carbonic anhydrase II (HCAII; EC 4.2.1.1) complexed with 3 structurally related inhibitors, 1a, 1b, and 1c, has been determined by X-ray crystallographic methods. The 3 inhibitors (1a = C8H12N2O4S3) vary only in t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c04f59e61e42db18c27e213a21e2f5bf
https://pubmed.ncbi.nlm.nih.gov/8142888
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4
FK-506-binding protein: three-dimensional structure of the complex with the antagonist L-685,818
Autor: J W, Becker, J, Rotonda, B M, McKeever, H K, Chan, A I, Marcy, G, Wiederrecht, J D, Hermes, J P, Springer
Publikováno v: The Journal of biological chemistry. 268(15)
L-685,818 differs only slightly in structure from the immunosuppressive drug FK-506, and both compounds bind with comparable affinity to the 12-kDa FK-506-binding protein (FKBP12), the major intracellular receptor for the drug. Despite these similari
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::daba5ba4c879fa51f3e4c496d5598c8a
https://pubmed.ncbi.nlm.nih.gov/7684380
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5
Site-directed mutagenesis of glutathione S-transferase YaYa. Important roles of tyrosine 9 and aspartic acid 101 in catalysis
Autor: R W, Wang, D J, Newton, S E, Huskey, B M, McKeever, C B, Pickett, A Y, Lu
Publikováno v: The Journal of biological chemistry. 267(28)
The roles of tyrosine 9 and aspartic acid 101 in the catalytic mechanism of rat glutathione S-transferase YaYa were studied by site-directed mutagenesis. Replacement of tyrosine 9 with phenylalanine (Y9F), threonine (Y9T), histidine (Y9H), or valine
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::729181f6f8b522d46cba47ca5040b296
https://pubmed.ncbi.nlm.nih.gov/1400302
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6
Synthesis and antiviral activity of a series of HIV-1 protease inhibitors with functionality tethered to the P1 or P1' phenyl substituents: X-ray crystal structure assisted design
Autor: W J, Thompson, P M, Fitzgerald, M K, Holloway, E A, Emini, P L, Darke, B M, McKeever, W A, Schleif, J C, Quintero, J A, Zugay, T J, Tucker
Publikováno v: Journal of medicinal chemistry. 35(10)
By tethering of a polar hydrophilic group to the P1 or P1' substituent of a Phe-based hydroxyethylene isostere, the antiviral potency of a series of HIV protease inhibitors was improved. The optimum enhancement of anti-HIV activity was observed with
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::591eaf09a0ced68981b1b99103a93e18
https://pubmed.ncbi.nlm.nih.gov/1588551
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8
Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0-A resolution
Autor: P M, Fitzgerald, B M, McKeever, J F, VanMiddlesworth, J P, Springer, J C, Heimbach, C T, Leu, W K, Herber, R A, Dixon, P L, Darke
Publikováno v: The Journal of biological chemistry. 265(24)
The mode of binding of acetyl-pepstatin to the protease from the human immunodeficiency virus type 1 (HIV-1) has been determined by x-ray diffraction analysis. Crystals of an acetyl-pepstatin-HIV-1 protease complex were obtained in space group P2(1)2
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d42f398200616cdd5f479e0a43fd1891
https://pubmed.ncbi.nlm.nih.gov/2201682
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9
Crystallization of the aspartylprotease from the human immunodeficiency virus, HIV-1
Autor: B M, McKeever, M A, Navia, P M, Fitzgerald, J P, Springer, C T, Leu, J C, Heimbach, W K, Herbert, I S, Sigal, P L, Darke
Publikováno v: The Journal of biological chemistry. 264(4)
The aspartylprotease of the human immunodeficiency virus HIV-1 (NY5) has been crystallized in a form suitable for x-ray diffraction analysis. The crystals are tetragonal bipyramids and produce an x-ray diffraction pattern that exhibits the symmetry a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d906faf9702528694d0d2b6b10c77b29
https://pubmed.ncbi.nlm.nih.gov/2644246
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