Výsledky vyhledávání

The development of assays for the detection of fibrin(ogen)olysis based on COOH-terminal A alpha chain epitopes

Autor: J H, Sobel, H Q, Wu, R E, Canfield

Publikováno v: Blood. 84:535-546

The COOH-terminal two-thirds of the fibrinogen A alpha chain is a substrate for both factor XIIIa and plasmin and is, therefore, a source of structural markers for the clinical detection of fibrin(ogen)olysis. Monoclonal antibodies (MoAbs) that bind

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f35664bcc9c717381246293f354f0189
https://doi.org/10.1182/blood.v84.2.535.bloodjournal842535

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Antipeptide monoclonal antibodies to defined fibrinogen Aalpha chain regions: anti-Aalpha 487-498, a structural probe for fibrinogenolysis

Autor: J H, Sobel, I, Trakht, N, Pileggi, H, Qi Wu

Publikováno v: Blood. 91(5)

The fibrinogen alphaC domain (Aalpha 220-610) is one of the earliest targets attacked by plasmin following fibrinolytic system activation. Monoclonal antibodies (MoAbs) to defined sequences within the alphaC domain provide the opportunity to explore

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ea9aaeec0ed7b4eba3f289cd7bdb3dcc
https://pubmed.ncbi.nlm.nih.gov/9473224

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Comparative structural and functional features of the human fibrinogen alpha C domain and the isolated alpha C fragment. Characterization using monoclonal antibodies to defined COOH-terminal A alpha chain regions

Autor: S, Rudchenko, I, Trakht, J H, Sobel

Publikováno v: The Journal of biological chemistry. 271(5)

The alpha C domain of fibrinogen (A alpha-(220-610)) plays a central role in maintaining hemostasis by serving as a substrate for factor XIIIa and plasmin. Monoclonal antibodies that recognize eight distinct epitopes within the COOH-terminal two-thir

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3030607bb3bb8c996a409c1d3e6df6b8
https://pubmed.ncbi.nlm.nih.gov/8576216

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Alpha-Chain cross-linking in fibrin(ogen) Marburg

Autor: J H, Sobel, I, Trakht, H Q, Wu, S, Rudchenko, R, Egbring

Publikováno v: Blood. 86(3)

The fibrinogen structural variant, Marburg (A alpha 1-460B beta gamma)2, is comprised of normal B beta and gamma chains but contains severely truncated A alpha chains that are missing approximately one half of their factor XIIIa cross-linking domain.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::88c3320685ca7fba5abcd5aba660177b
https://pubmed.ncbi.nlm.nih.gov/7620190

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Low molecular weight fibrinogen degradation products stimulate the release of growth factors from endothelial cells

Autor: R, Lorenzet, J H, Sobel, A, Bini, L D, Witte

Publikováno v: Thrombosis and haemostasis. 68(3)

Cultured porcine aortic endothelial cells (PAEC) constitutively produce and secrete in their culture medium mitogens collectively called endothelial cell-derived growth factors (EDGFs). Incubation of PAEC with fibrinogen-degradation products (FDPs) o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2aebae88e506398c93842eef2e8c01d3
https://pubmed.ncbi.nlm.nih.gov/1440505

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Immunochemical studies of A alpha chain crosslinking

Autor: J H, Sobel, R E, Canfield

Publikováno v: Advances in experimental medicine and biology. 281

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a62cbbc2a4354816a6271aa0e38dc738
https://pubmed.ncbi.nlm.nih.gov/1715122

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82. A?? chain heterogeneity and the fibrinogen lowering effect of hormone replacement therapy in postmenopausal women

Autor: S. Rudchenko, C. Tuck, J. H. Sobel

Publikováno v: Blood Coagulation & Fibrinolysis. 9:709

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a9099b5edb62fff5228306edf50445f8
https://doi.org/10.1097/00001721-199810000-00102

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Immunochemical characterization of crosslinked derivatives isolated from alpha chain oligomers formed during early stages of fibrin crosslinking

Autor: J H, Sobel, C A, Thibodeau, M A, Gawinowicz Kolks, R E, Canfield

Publikováno v: Thrombosis and haemostasis. 60(2)

Early crosslinked alpha chain oligomers (E alpha XL) that formed within 1/2 h of in vitro clot formation were isolated from preparations of reduced, carboxymethylated fibrin by gel filtration on Sepharose CL-4B. Cyanogen bromide (CNBr) digestion of E

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3e6570a1d7d6e4e862b73c371efa15a6
https://pubmed.ncbi.nlm.nih.gov/3217917

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Immunologic identification of the cleavage products from the A alpha- and B beta-chains in the early stages of plasmin digestion of fibrinogen

Autor: C Y, Liu, J H, Sobel, J I, Weitz, K L, Kaplan, H L, Nossel

Publikováno v: Thrombosis and haemostasis. 56(1)

Fragment X components (Mr 225,000 to 333,000) were distinguished on sodium dodecyl sulfate polyacrylamide gels. Western blotting with monoclonal antibodies to A alpha-chain segments demonstrated that the A alpha-chains of fibrinogen and the largest f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::43fd4f4a48ad69fbf66ce294ab45cdcc
https://pubmed.ncbi.nlm.nih.gov/2946092

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