Výsledky vyhledávání - "John R. Vasquez"

Identification of Cryptosporidium parvum Dihydrofolate Reductase Inhibitors by Complementation in Saccharomyces cerevisiae

Autor: Victoria H. Brophy, Carol Hopkins Sibley, John R. Forney, John R. Vasquez, Richard G. Nelson, Andre Rosowsky

Publikováno v: Antimicrobial Agents and Chemotherapy. 44:1019-1028

There is a pressing need for drugs effective against the opportunistic protozoan pathogen Cryptosporidium parvum . Folate metabolic enzymes and enzymes of the thymidylate cycle, particularly dihydrofolate reductase (DHFR), have been widely exploited

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3a5599500e272c1e9335cd757fd3a5d
https://doi.org/10.1128/aac.44.4.1019-1028.2000

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Rabbit Muscle Creatine Kinase: Consequences of the Mutagenesis of Conserved Histidine Residues

Autor: Lorenzo H. Chen, George L. Kenyon, Charles L. Borders, John R. Vasquez

Publikováno v: Biochemistry. 35:7895-7902

Creatine kinase (CK; EC 2.7.3.2) catalyzes the reversible conversion of creatine and MgATP to phosphocreatine and MgADP. In the absence of an X-ray crystal structure, we have used the sequence homology of creatine kinases and other guanidino kinases

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45ec8198b3f25b9ac885ffaf162c183a
https://doi.org/10.1021/bi952798i

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Perturbing the polar environment of Asp102 in trypsin: consequences of replacing conserved Ser214

Autor: John R. Vasquez, An-Suei Yang, Robert J. Fletterick, Charles S. Craik, Barry Honig, Mary E. McGrath

Publikováno v: Biochemistry. 31:3059-3064

Much of the catalytic power of trypsin is derived from the unusual buried, charged side chain of Aspl02. A polar cave provides the stabilization for maintaining the buried charge, and it features the conserved amino acid Ser214 adjacent to Aspl02. Se

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c78cfb020ebc6e81ab2a10aa3d239c5a
https://doi.org/10.1021/bi00127a005

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Substrate specificity of trypsin investigated by using a genetic selection

Autor: John R. Vasquez, Charles S. Craik, Luke B. Evnin

Publikováno v: Proceedings of the National Academy of Sciences. 87:6659-6663

The structural determinants of the primary substrate specificity of rat anionic trypsin were examined by using oligonucleotide-directed mutagenesis coupled to a genetic selection. A library was created that encoded trypsins substituted at amino acid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc0a5b41979fa672fc96d23867f696a0
https://doi.org/10.1073/pnas.87.17.6659

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An alternate geometry for the catalytic triad of serine proteases

Autor: Charles S. Craik, John R. Vasquez, Mary E. McGrath, Robert J. Fletterick, David R. Corey

Publikováno v: Journal of the American Chemical Society. 114:4905-4907

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4cef9308f897ee9b28900ed5bfc21015
https://doi.org/10.1021/ja00038a067

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An expression system for trypsin

Autor: John R. Vasquez, Jeffrey N. Higaki, Charles S. Craik, Luke B. Evnin

Publikováno v: Journal of Cellular Biochemistry. 39:265-276

The eukaryotic serine protease, rat anionic trypsin, and various mutants created by site-directed mutagenesis have been heterologously expressed in Escherichia coli. The bacterial alkaline phosphatase (phoA) promoter was used to control the expressio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a63200c86214a008bb3ea7aec6fd5dd9
https://doi.org/10.1002/jcb.240390306

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