Zobrazeno 1 - 10 of 11 pro vyhledávání: '"V C, Yee"'
1
Pharmacogenetics of the mycophenolic acid targets inosine monophosphate dehydrogenases IMPDH1 and IMPDH2: gene sequence variation and functional genomics
Autor: T-Y, Wu, Y, Peng, L L, Pelleymounter, I, Moon, B W, Eckloff, E D, Wieben, V C, Yee, R M, Weinshilboum
Publikováno v: British journal of pharmacology. 161(7)
Inosine monophosphate dehydrogenases, encoded by IMPDH1 and IMPDH2, are targets for the important immunosuppressive drug, mycophenolic acid (MPA). Variation in MPA response may result, in part, from genetic variation in IMPDH1 and IMPDH2.We resequenc
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4765331eacc3a606ca224ed6247de5dd
https://pubmed.ncbi.nlm.nih.gov/20718729
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3
Crystal structure of the human prion protein reveals a mechanism for oligomerization
Autor: K J, Knaus, M, Morillas, W, Swietnicki, M, Malone, W K, Surewicz, V C, Yee
Publikováno v: Nature structural biology. 8(9)
The pathogenesis of transmissible encephalopathies is associated with the conversion of the cellular prion protein, PrP(C), into a conformationally altered oligomeric form, PrP(Sc). Here we report the crystal structure of the human prion protein in d
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::25af8044d4003b2a2a47500ac60c226d
https://pubmed.ncbi.nlm.nih.gov/11524679
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4
Identification of the binding site for fibrinogen recognition peptide gamma 383-395 within the alpha(M)I-domain of integrin alpha(M)beta2
Autor: V P, Yakubenko, D A, Solovjov, L, Zhang, V C, Yee, E F, Plow, T P, Ugarova
Publikováno v: The Journal of biological chemistry. 276(17)
The leukocyte integrin alpha(M)beta(2) (Mac-1, CD11b/CD18) is a cell surface adhesion receptor for fibrinogen. The interaction between fibrinogen and alpha(M)beta(2) mediates a range of adhesive reactions during the immune-inflammatory response. The
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f307487a73bdf56036a1c70f5aafb7ae
https://pubmed.ncbi.nlm.nih.gov/11278633
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5
Interaction of the factor XIII activation peptide with alpha -thrombin. Crystal structure of its enzyme-substrate analog complex
Autor: C, Sadasivan, V C, Yee
Publikováno v: The Journal of biological chemistry. 275(47)
The serine protease thrombin proteolytically activates blood coagulation factor XIII by cleavage at residue Arg(37); factor XIII in turn cross-links fibrin molecules and gives mechanical stability to the blood clot. The 2.0-A resolution x-ray crystal
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f13c5edf40b54ceda94be3c5c34401ae
https://pubmed.ncbi.nlm.nih.gov/10956659
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7
Identification of a novel recognition sequence for integrin alphaM beta2 within the gamma-chain of fibrinogen
Autor: T P, Ugarova, D A, Solovjov, L, Zhang, D I, Loukinov, V C, Yee, L V, Medved, E F, Plow
Publikováno v: The Journal of biological chemistry. 273(35)
The interaction of leukocyte integrin alphaMbeta2 (CD11b/CD18, Mac-1) with fibrinogen has been implicated in the inflammatory response by contributing to leukocyte adhesion to the endothelium and subsequent transmigration. Previously, it has been dem
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::aad176f1a75d8f064f742b4b24b7631a
https://pubmed.ncbi.nlm.nih.gov/9712878
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8
Coagulation factor XIIIa undergoes a conformational change evoked by glutamine substrate. Studies on kinetics of inhibition and binding of XIIIA by a cross-reacting antifibrinogen antibody
Autor: O V, Mitkevich, J R, Shainoff, P M, DiBello, V C, Yee, D C, Teller, G B, Smejkal, P D, Bishop, I S, Kolotushkina, K, Fickenscher, G P, Samokhin
Publikováno v: The Journal of biological chemistry. 273(23)
Coagulation factor XIIIa, plasma transglutaminase (endo-gamma-glutamine:epsilon-lysine transferase EC 2.3.2.13) catalyzes isopeptide bond formation between glutamine and lysine residues and rapidly cross-links fibrin clots. A monoclonal antibody (5A2
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a00117cae504dadc542da963f58d87d5
https://pubmed.ncbi.nlm.nih.gov/9603949
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9
The corn inhibitor of blood coagulation factor XIIa. Crystallization and preliminary crystallographic analysis
Autor: L C, Pedersen, V C, Yee, G, von Dassow, M, Hazeghazam, G R, Reeck, R E, Stenkamp, D C, Teller
Publikováno v: Journal of molecular biology. 236(1)
A 13.6 kDa protein from corn seeds is known to be a highly selective inhibitor of human blood coagulation Factor XIIa (or activated Hageman factor). We have crystallized this inhibitor at 23 degrees C and pH 7.5 from a solution of 30% polyethylene gl
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ea1f8f71a252c9222305c69d66d6195e
https://pubmed.ncbi.nlm.nih.gov/8107123
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