Search Results - "Fretto, L J"

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    A functional soluble extracellular region of the platelet-derived growth factor (PDGF) beta-receptor antagonizes PDGF-stimulated responses by Duan, D S, Pazin, M J, Fretto, L J, Williams, L T

    Published in The Journal of biological chemistry (05-01-1991)
    “…The platelet-derived growth factor beta-receptor (PDGFr) is a 180-kDa transmembrane glycoprotein which binds BB-PDGF with high affinity. We have expressed the…”
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    Substructure of human von Willebrand factor by FOWLER, W. E, FRETTO, L. J, HAMILTON, K. K, ERICKSON, H. P, MCKEE, P. A

    Published in The Journal of clinical investigation (01-10-1985)
    “…Using electron microscopy, we have visualized the substructure of human von Willebrand factor (vWf) purified by two different approaches. vWf multimers, which…”
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  4. 4

    Mechanism of platelet-derived growth factor (PDGF) AA, AB, and BB binding to alpha and beta PDGF receptor by FRETTO, L. J, SNAPE, A. J, TOMLINSON, J. E, SEROOGY, J. J, WOLF, D. L, LAROCHELLE, W. J, GIESE, N. A

    Published in The Journal of biological chemistry (15-02-1993)
    “…The biological effects of platelet-derived growth factor (PDGF) are mediated by cell surface alpha and beta PDGF receptors, which, as a result of ligand…”
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    Substructure of human von Willebrand factor. Proteolysis by V8 and characterization of two functional domains by Fretto, L J, Fowler, W E, McCaslin, D R, Erickson, H P, McKee, P A

    Published in The Journal of biological chemistry (25-11-1986)
    “…The effects of Staphylococcus aureus V8 protease (V8) on the multimeric structure of human von Willebrand factor (vWF) were studied to test and expand our…”
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    The effects of fibrinogen and its cleavage products on the kinetics of plasminogen activation by urokinase and subsequent plasmin activity by Lucas, M A, Straight, D L, Fretto, L J, McKee, P A

    Published in The Journal of biological chemistry (25-10-1983)
    “…The effects of fibrinogen and its plasmic cleavage fragments on the activation of Glu-, Lys-, and Val442- plasminogen by urokinase were investigated. A…”
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    Effects of plasmin on von Willebrand factor multimers: degradation in vitro and stimulation of release in vivo by HAMILTON, K. K, FRETTO, L. J, GRIERSON, D. S, MCKEE, P. A

    Published in The Journal of clinical investigation (01-07-1985)
    “…von Willebrand factor (vWF), a multimeric protein that mediates platelet adhesion, circulates in association with the procoagulant Factor VIII (FVIII). In…”
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    A re-examination of the cleavage of fibrinogen and fibrin by plasmin by Ferguson, E W, Fretto, L J, McKee, P A

    Published in The Journal of biological chemistry (25-09-1975)
    “…Three Fragment D species (D1, D2, D3) were isolated with time from a plasmin digest of fibrinogen and had molecular weights of 92,999, 86,000 and 82,000 by…”
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    Functional importance of platelet-derived growth factor (PDGF) receptor extracellular immunoglobulin-like domains. Identification of PDGF binding site and neutralizing monoclonal antibodies by Lokker, N A, O'Hare, J P, Barsoumian, A, Tomlinson, J E, Ramakrishnan, V, Fretto, L J, Giese, N A

    Published in The Journal of biological chemistry (26-12-1997)
    “…The biological effects of platelet-derived growth factor (PDGF) are mediated by alpha- and beta-PDGF receptors (PDGFR), which have an intracellular tyrosine…”
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    Localization of the alpha-chain cross-link acceptor sites of human fibrin by Fretto, L J, Ferguson, E W, Steinman, H M, McKee, P A

    Published in The Journal of biological chemistry (10-04-1978)
    “…The potential cross-link acceptor sites of fibrin were specifically labeled with the fluorescent, substitute cross-link donor monodansyl cadaverine (MDC)…”
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    Acidic and basic fibroblast growth factors stimulate tyrosine kinase activity in vivo by Coughlin, S R, Barr, P J, Cousens, L S, Fretto, L J, Williams, L T

    Published in The Journal of biological chemistry (15-01-1988)
    “…We assessed the ability of acidic and basic fibroblast growth factor (FGF) to stimulate tyrosine kinase activity in intact cells. Immunoblot with polyclonal…”
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    Novel tricyclic benzothiazolo[2,3-c]thiadiazine antagonists of the platelet ADP receptor (P2Y12) by SCARBOROUGH, Robert M, LAIBELMAN, Alan M, CLIZBE, Lane A, FRETTO, Larry J, CONLEY, Pamela B, REYNOLDS, Elwood E, SEDLOCK, David M, JANTZEN, Hans-Michael

    Published in Bioorganic & medicinal chemistry letters (23-07-2001)
    “…Novel non-nucleoside tricyclic platelet ADP receptor (P2Y(12)) antagonists have been discovered that bind reversibly and with high affinity to the platelet…”
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    Structure of alpha-polymer from in vitro and in vivo highly cross-linked human fibrin by Fretto, L J, McKee, P A

    Published in The Journal of biological chemistry (25-09-1978)
    “…Peptides derived from plasmic and cyanogen bromide (CNBr) cleavage of highly cross-linked fibrin were isolated and characterized by sodium dodecyl sulfate-gel…”
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    Electron Microscopy of Human Factor VIII/Von Willebrand Glycoprotein: Effect of Reducing Reagents on Structure and Function by Ohmori, Keizo, Fretto, Larry J., Harrison, Robert L., Mary Ellen P. Switzer, Erickson, Harold P., McKee, Patrick A.

    Published in The Journal of cell biology (01-11-1982)
    “…The structure of native and progressively reduced human factor VIII/von Willebrand factor (FVIII/vWF) was examined by electron microscopy and SDS gel…”
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    A novel monoclonal antibody dependent on domain 5 of the platelet-derived growth factor beta receptor inhibits ligand binding and receptor activation by Ramakrishnan, V, Escobedo, M A, Fretto, L J, Seroogy, J J, Tomlinson, J E, Wolf, D L

    “…Platelet derived growth factor (PDGF) induces activation of the protein tyrosine kinase domain of the PDGF receptor, resulting in receptor dimerization and the…”
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    Electron microsocpy of plasmic fragments of human fibrinogen as related to trinodular structure of the intact molecule by Fowler, W E, Fretto, L J, Erickson, H P, McKee, P A

    Published in The Journal of clinical investigation (01-07-1980)
    “…We have examined rotary shadowed, purified plasmic fragments of human fibrinogen with the electron microscope and have determined the relation of these…”
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