Výsledky vyhledávání - "F. A. Quiocho"

Preliminary time-of-flight neutron diffraction studies ofEscherichia coliABC transport receptor phosphate-binding protein at the Protein Crystallography Station

Autor: Katherine H. Sippel, John-Paul Bacik, S. Z. Fisher, F. A. Quiocho

Publikováno v: Acta Crystallographica Section F Structural Biology Communications. 70:819-822

Inorganic phosphate is an essential molecule for all known life. Organisms have developed many mechanisms to ensure an adequate supply, even in low-phosphate conditions. In prokaryotes phosphate transport is instigated by the phosphate-binding protei

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cdd431220c054a18892110841f58f2b
https://doi.org/10.1107/s2053230x14009704

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Akademický článek

Inhibitors of sterol synthesis. Chemical synthesis, structure, and biological activities of (25R)-3 beta,26-dihydroxy-5 alpha-cholest-8(14)-en-15-one, a metabolite of 3 beta-hydroxy-5 alpha-cholest-8(14)-en-15-one.

Autor: H S Kim, W K Wilson, D H Needleman, F D Pinkerton, D K Wilson, F A Quiocho, G J Schroepfer, Jr

Publikováno v: Journal of Lipid Research, Vol 30, Iss 2, Pp 247-261 (1989)

3 beta-Hydroxy-5 alpha-cholest-8(14)-en-15-one (I) is a potent inhibitor of sterol synthesis with significant hypocholesterolemic activity. (25R)-3 beta,26-Dihydroxy-5 alpha-cholest-8(14)-en-15-one (II) has been shown to be a major metabolite of I af

Externí odkaz: https://doaj.org/article/8f8985ab75134d23853f8a93bc6f2786

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Protein–ligand interactions

Autor: F. A. Quiocho, A. E. Hodel

Publikováno v: International Tables for Crystallography ISBN: 9780470660782
International Tables for Crystallography
International Tables for Crystallography ISBN: 9780792368571

Protein–ligand interactions are described and several of the unique interactions observed between proteins and other molecules are illustrated. The chapter covers protein–carbohydrate interactions, metal ions associated with proteins, protein–n

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1075dbd17e8a7936478ead407f2242dd
https://doi.org/10.1107/97809553602060000892

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Aldose reductase catalysis and crystallography. Insights from recent advances in enzyme structure and function

Autor: J. M. Petrash, I. Tarle, D. K. Wilson, F. A. Quiocho

Publikováno v: Diabetes. 43:955-959

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::bc996e3702a0acb1eba6828fb2b14e59
https://doi.org/10.2337/diabetes.43.8.955

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The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis

Autor: J C Spurlino, G Y Lu, F A Quiocho

Publikováno v: Journal of Biological Chemistry. 266:5202-5219

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::871eb9f36eb225925c3b881531b2c7bc
https://doi.org/10.1016/s0021-9258(19)67774-4

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Structural features of the aldose reductase and aldehyde reductase inhibitor-binding sites

Autor: O, El-Kabbani, D K, Wilson, M, Petrash, F A, Quiocho

Publikováno v: Molecular vision. 4

The three-dimensional structures of aldose reductase and aldehyde reductase, members of the aldo-keto reductase superfamily, are composed of similar alpha/beta TIM-barrels. However, examination of the structures reveals that the inhibitor-binding sit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::42adf013231e17d3af93c887e5f30cc2
https://pubmed.ncbi.nlm.nih.gov/9756955

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CHAIN: a crystallographic modeling program

Autor: J S, Sack, F A, Quiocho

Publikováno v: Methods in enzymology. 277

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4c828cce59061bada2eb72f6688762b2
https://pubmed.ncbi.nlm.nih.gov/18488309

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Structural studies of aldo-keto reductase inhibition

Autor: D K, Wilson, T, Nakano, J M, Petrash, F A, Quiocho

Publikováno v: Advances in experimental medicine and biology. 414

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d8ed54e77e2af4d3e5305691ff313237
https://pubmed.ncbi.nlm.nih.gov/9059648

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Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation

Autor: Z, Chang, T P, Primm, J, Jakana, I H, Lee, I, Serysheva, W, Chiu, H F, Gilbert, F A, Quiocho

Publikováno v: The Journal of biological chemistry. 271(12)

Tuberculosis continues to be a major disease threatening millions of lives worldwide. Several antigens of Mycobacterium tuberculosis, identified by monoclonal antibodies, have been cloned and are being exploited in the development of improved vaccine

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::26380edd7b8caf292171f32c92e3f2ab
https://pubmed.ncbi.nlm.nih.gov/8636160

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Fine tuning the specificity of the periplasmic phosphate transport receptor. Site-directed mutagenesis, ligand binding, and crystallographic studies

Autor: Z, Wang, A, Choudhary, P S, Ledvina, F A, Quiocho

Publikováno v: The Journal of biological chemistry. 269(40)

Phosphorous, primarily in the form of phosphate, is a critical nutrient for the life of a cell. We have previously determined the 1.7-A resolution structure of the phosphate-binding protein, an initial receptor for the high-affinity phosphate active

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::18d7c1c024b342bf523d20c8ff643785
https://pubmed.ncbi.nlm.nih.gov/7929197

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