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Journal Abstract Search
231 related items for PubMed ID: 8226767
1. SH2 domains of the protein-tyrosine kinases Blk, Lyn, and Fyn(T) bind distinct sets of phosphoproteins from B lymphocytes. Malek SN, Desiderio S. J Biol Chem; 1993 Oct 25; 268(30):22557-65. PubMed ID: 8226767 [Abstract] [Full Text] [Related]
2. Tyrosine phosphorylation of Blk and Fyn Src homology 2 domain-binding proteins occurs in response to antigen-receptor ligation in B cells and constitutively in pre-B cells. Aoki Y, Isselbacher KJ, Cherayil BJ, Pillai S. Proc Natl Acad Sci U S A; 1994 May 10; 91(10):4204-8. PubMed ID: 7514299 [Abstract] [Full Text] [Related]
3. The SH2 domains of Src family kinases associate with Syk. Aoki Y, Kim YT, Stillwell R, Kim TJ, Pillai S. J Biol Chem; 1995 Jun 30; 270(26):15658-63. PubMed ID: 7797565 [Abstract] [Full Text] [Related]
4. The three-dimensional solution structure of the SH2 domain from p55blk kinase. Metzler WJ, Leiting B, Pryor K, Mueller L, Farmer BT. Biochemistry; 1996 May 21; 35(20):6201-11. PubMed ID: 8639560 [Abstract] [Full Text] [Related]
5. Specific binding of Fyn and phosphatidylinositol 3-kinase to the B cell surface glycoprotein CD19 through their src homology 2 domains. Chalupny NJ, Aruffo A, Esselstyn JM, Chan PY, Bajorath J, Blake J, Gilliland LK, Ledbetter JA, Tepper MA. Eur J Immunol; 1995 Oct 21; 25(10):2978-84. PubMed ID: 7589101 [Abstract] [Full Text] [Related]
7. Mapping of sites on the Src family protein tyrosine kinases p55blk, p59fyn, and p56lyn which interact with the effector molecules phospholipase C-gamma 2, microtubule-associated protein kinase, GTPase-activating protein, and phosphatidylinositol 3-kinase. Pleiman CM, Clark MR, Gauen LK, Winitz S, Coggeshall KM, Johnson GL, Shaw AS, Cambier JC. Mol Cell Biol; 1993 Sep 21; 13(9):5877-87. PubMed ID: 8395016 [Abstract] [Full Text] [Related]
8. Association of p59(fyn) with the T lymphocyte costimulatory receptor CD2. Binding of the Fyn Src homology (SH) 3 domain is regulated by the Fyn SH2 domain. Lin H, Hutchcroft JE, Andoniou CE, Kamoun M, Band H, Bierer BE. J Biol Chem; 1998 Jul 31; 273(31):19914-21. PubMed ID: 9677430 [Abstract] [Full Text] [Related]
9. Association of 75/80-kDa phosphoproteins and the tyrosine kinases Lyn, Fyn, and Lck with the B cell molecule CD20. Evidence against involvement of the cytoplasmic regions of CD20. Deans JP, Kalt L, Ledbetter JA, Schieven GL, Bolen JB, Johnson P. J Biol Chem; 1995 Sep 22; 270(38):22632-8. PubMed ID: 7545683 [Abstract] [Full Text] [Related]
10. In vivo and in vitro specificity of protein tyrosine kinases for immunoglobulin G receptor (FcgammaRII) phosphorylation. Bewarder N, Weinrich V, Budde P, Hartmann D, Flaswinkel H, Reth M, Frey J. Mol Cell Biol; 1996 Sep 22; 16(9):4735-43. PubMed ID: 8756631 [Abstract] [Full Text] [Related]
11. Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1. Richard S, Yu D, Blumer KJ, Hausladen D, Olszowy MW, Connelly PA, Shaw AS. Mol Cell Biol; 1995 Jan 22; 15(1):186-97. PubMed ID: 7799925 [Abstract] [Full Text] [Related]
12. Molecular cloning of SKAP55, a novel protein that associates with the protein tyrosine kinase p59fyn in human T-lymphocytes. Marie-Cardine A, Bruyns E, Eckerskorn C, Kirchgessner H, Meuer SC, Schraven B. J Biol Chem; 1997 Jun 27; 272(26):16077-80. PubMed ID: 9195899 [Abstract] [Full Text] [Related]
13. Binding of src-like kinases to the beta-subunit of the interleukin-3 receptor. Burton EA, Hunter S, Wu SC, Anderson SM. J Biol Chem; 1997 Jun 27; 272(26):16189-95. PubMed ID: 9195918 [Abstract] [Full Text] [Related]
16. Reconstitution of the B cell antigen receptor signaling components in COS cells. Saouaf SJ, Kut SA, Fargnoli J, Rowley RB, Bolen JB, Mahajan S. J Biol Chem; 1995 Nov 10; 270(45):27072-8. PubMed ID: 7592958 [Abstract] [Full Text] [Related]
17. Interactions of Lyn with the antigen receptor during B cell activation. Burg DL, Furlong MT, Harrison ML, Geahlen RL. J Biol Chem; 1994 Nov 11; 269(45):28136-42. PubMed ID: 7525568 [Abstract] [Full Text] [Related]