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Formation of a stable src-AFAP-110 complex through either an amino-terminal or a carboxy-terminal SH2-binding motif.
Mol Carcinog. 1998 Jun;22(2):110-9. doi: 10.1002/(sici)1098-2744(199806)22:2<110::aid-mc6>3.0.co;2-q.
Mol Carcinog. 1998.
PMID: 9655255
Src can regulate carboxy terminal interactions with AFAP-110, which influence self-association, cell localization and actin filament integrity.
Qian Y, Baisden JM, Westin EH, Guappone AC, Koay TC, Flynn DC.
Qian Y, et al. Among authors: guappone ac.
Oncogene. 1998 Apr 30;16(17):2185-95. doi: 10.1038/sj.onc.1201753.
Oncogene. 1998.
PMID: 9619827
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The SH3 and SH2 domains are capable of directing specificity in protein interactions between the non-receptor tyrosine kinases cSrc and cYes.
Summy JM, Guappone AC, Sudol M, Flynn DC.
Summy JM, et al. Among authors: guappone ac.
Oncogene. 2000 Jan 6;19(1):155-60. doi: 10.1038/sj.onc.1203265.
Oncogene. 2000.
PMID: 10644991
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The integrity of the SH3 binding motif of AFAP-110 is required to facilitate tyrosine phosphorylation by, and stable complex formation with, Src.
Guappone AC, Flynn DC.
Guappone AC, et al.
Mol Cell Biochem. 1997 Oct;175(1-2):243-52. doi: 10.1023/a:1006840104666.
Mol Cell Biochem. 1997.
PMID: 9350057
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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.
Flynn DC, Koay TC, Humphries CG, Guappone AC.
Flynn DC, et al. Among authors: guappone ac.
J Biol Chem. 1995 Feb 24;270(8):3894-9.
J Biol Chem. 1995.
PMID: 7876134
Free article.
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Monoclonal antibodies directed against AFAP-110 recognize species-specific and conserved epitopes.
Qian Y, Guappone AC, Baisden JM, Hill MW, Summy JM, Flynn DC.
Qian Y, et al. Among authors: guappone ac.
Hybridoma. 1999 Apr;18(2):167-75. doi: 10.1089/hyb.1999.18.167.
Hybridoma. 1999.
PMID: 10380016
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