Search Results - "GUAPPONE, A. C"

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  1. 1

    The SH3 and SH2 domains are capable of directing specificity in protein interactions between the non-receptor tyrosine kinases cSrc and cYes by SUMMY, J. M, GUAPPONE, A. C, SUDOL, M, FLYNN, D. C

    Published in Oncogene (06-01-2000)
    “…The c-src and c-yes proto-oncogenes encode 60 000 and 62 000 Dalton non-receptor tyrosine kinases of the Src family, pp60c-src and pp62c-yes, respectively…”
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  2. 2

    The integrity of the SH3 binding motif of AFAP-110 is required to facilitate tyrosine phosphorylation by, and stable complex formation with, Src by Guappone, A C, Flynn, D C

    Published in Molecular and cellular biochemistry (01-10-1997)
    “…The actin filament-associated protein AFAP-110 forms a stable complex with activated variants of Src in chick embryo fibroblast cells. Stable complex formation…”
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  3. 3

    Src can regulate carboxy terminal interactions with AFAP-110, which influence self-association, cell localization and actin filament integrity by Qian, Y, Baisden, J M, Westin, E H, Guappone, A C, Koay, T C, Flynn, D C

    Published in Oncogene (30-04-1998)
    “…The SH2 and SH3 binding partner AFAP-110 is a tyrosine phosphorylated substrate of Src. AFAP-110 has been hypothesized to link Src to actin filaments, which…”
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  4. 4

    Formation of a stable src-AFAP-110 complex through either an amino-terminal or a carboxy-terminal SH2-binding motif by Guappone, Anne C., Weimer, Tracy, Flynn, Daniel C.

    Published in Molecular carcinogenesis (01-06-1998)
    “…The actin‐filament–associated protein (AFAP‐110) forms a stable complex with activated variants of the Pp60c‐src (Src) non‐receptor tyrosine kinase through SH2…”
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  5. 5

    Monoclonal antibodies directed against AFAP-110 recognize species-specific and conserved epitopes by Qian, Y, Guappone, A C, Baisden, J M, Hill, M W, Summy, J M, Flynn, D C

    Published in Hybridoma (01-04-1999)
    “…The actin filament-associated protein, AFAP-110, is a Src SH2/SH3 binding partner that can modulate changes in actin filament structure. AFAP-110 contains a…”
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  6. 6

    AFAP-120. A variant form of the Src SH2/SH3-binding partner AFAP-110 is detected in brain and contains a novel internal sequence which binds to a 67-kDa protein by Flynn, D C, Koay, T C, Humphries, C G, Guappone, A C

    Published in The Journal of biological chemistry (24-02-1995)
    “…SH2 and SH3 domains have been characterized as functional domains that mediate protein-protein interactions in signal transduction. Recently, the cDNA sequence…”
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