Zobrazeno 1 - 10 of 18 pro vyhledávání: '"L V, Medved'"'
1
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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4
The interaction of fibulin-1 with fibrinogen. A potential role in hemostasis and thrombosis
Autor: H, Tran, A, Tanaka, S V, Litvinovich, L V, Medved, C C, Haudenschild, W S, Argraves
Publikováno v: The Journal of biological chemistry. 270(33)
The fibulins are an emerging family of extracellular matrix and blood proteins presently having two members designated fibulin-1 and -2. Fibulin-1 is the predominant fibulin in blood, present at a concentration of 30-40 micrograms/ml (approximately 1
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::29fb16285fc0ac55a1f02b298aa1f0e3
https://pubmed.ncbi.nlm.nih.gov/7642629
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5
The NH2-terminal fibrin-binding site of fibronectin is formed by interacting fourth and fifth finger domains. Studies with recombinant finger fragments expressed in Escherichia coli
Autor: Y V, Matsuka, L V, Medved, S A, Brew, K C, Ingham
Publikováno v: The Journal of biological chemistry. 269(13)
The NH2-terminal 29-kDa Fib-1 fragment consisting of the first five finger modules of fibronectin (F1-5) binds reversibly to fibrin and facilitates cross-linking by Factor XIII. To narrow down the fibrin-binding site within this region, we have used
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e87d3c127eacb6a830a2f997b1bad7c2
https://pubmed.ncbi.nlm.nih.gov/8144540
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6
Ca(2+)-dependent interactions between Gla and EGF domains in human coagulation factor IX
Autor: L V, Medved, A, Vysotchin, K C, Ingham
Publikováno v: Biochemistry. 33(2)
The Ca(2+)-induced interaction between the Gla and EGF domains of human factor IX was investigated by means of three fragments: 6-kDa Gla, 19-kDa (EGF)2, and 25-kDa Gla-(EGF)2. Size-exclusion chromatography and spectroscopic measurements revealed tha
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::98c468b9e4f3d2539826c7c1ce40f007
https://pubmed.ncbi.nlm.nih.gov/7904478
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7
Effect of tethered peptidylchloromethylketone inhibitors on thermal stability and domain interactions of urokinase and other serine proteases
Autor: V V, Novokhatny, L V, Medved, A, Mazar, K C, Ingham
Publikováno v: The Journal of biological chemistry. 268(23)
The melting of several serine proteases that had been reacted with different peptidylchloromethylketone (cmk) inhibitors was studied by fluorescence spectroscopy and calorimetry. These inhibitors, which cross-link the two domains of the proteases, in
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6f17803db14b0a275f0b6c4778710338
https://pubmed.ncbi.nlm.nih.gov/8349606
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8
Carboxyl-terminal portions of the alpha chains of fibrinogen and fibrin. Localization by electron microscopy and the effects of isolated alpha C fragments on polymerization
Autor: Y I, Veklich, O V, Gorkun, L V, Medved, W, Nieuwenhuizen, J W, Weisel
Publikováno v: The Journal of biological chemistry. 268(18)
The locations of the carboxyl-terminal two thirds of the A alpha chains, or the alpha C domains, were determined for fibrinogen and some of its derivatives by electron microscopy of rotary-shadowed preparations. A monoclonal antibody, G8, to the carb
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::34694c643e7e014cadf1343c8de7fa6b
https://pubmed.ncbi.nlm.nih.gov/8514790
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9
Domain structure and domain-domain interactions of recombinant tissue plasminogen activator
Autor: V V, Novokhatny, K C, Ingham, L V, Medved
Publikováno v: The Journal of biological chemistry. 266(20)
The melting of recombinant tissue plasminogen activator (rtPA) has been investigated by differential scanning calorimetry and fluorescence spectroscopy. At neutral pH, rtPA melts with only partial reversibility in a single sharp peak that can be deco
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2afd557350a7622a481793f09f49cddd
https://pubmed.ncbi.nlm.nih.gov/1906462
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10
Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin. All six modules are independently folded
Autor: S V, Litvinovich, D K, Strickland, L V, Medved, K C, Ingham
Publikováno v: Journal of molecular biology. 217(3)
The gelatin-binding region of fibronectin is isolated easily as a stable and functional 42 kDa fragment containing four type I "finger" modules and two type II "kringle-like" modules arranged in the order I6-II1-II2-I7-I8-I9. This fragment exhibits a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5f1d03d73537a59a736e624c39f9c9f4
https://pubmed.ncbi.nlm.nih.gov/1994038
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