Zobrazeno 1 - 10
of 92
pro vyhledávání: '"Bartholomew M. Sefton"'
Publikováno v:
Protein Science. 15:2402-2410
The Tip protein from Herpesvirus saimiri interacts with the SH3 domain from the Src-family kinase Lck via a proline-containing sequence termed LBD1. Src-family kinase SH3 domains related to Lck have been shown to be dynamic in solution and partially
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe0bdbb8f3384ad4817ca281cf7045c5
https://doi.org/10.1110/ps.052016406
https://doi.org/10.1110/ps.052016406
Publikováno v:
Journal of Computational Chemistry. 26:668-681
In several previous studies, we performed sensitivity analysis to gauge the relative importance of different atomic partial charges in determining protein-ligand binding. In this work, we gain further insights by decomposing these results into three
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b196abc0270ef4f4a69060907a3a452
https://doi.org/10.1002/jcc.20207
https://doi.org/10.1002/jcc.20207
Autor:
Roberta Schulte, Bartholomew M. Sefton
Publikováno v:
Biochemistry. 42:9424-9430
The Wiscott-Aldrich syndrome protein, WASP, is an effector through which cdc42, a Rho family GTPase, regulates the actin cytoskeleton in hematopoietic cells. We have found that WASP binds readily to a number of tyrosine protein kinases including the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c9b4ad0c109bf2a6a15f4919fd859b5
https://doi.org/10.1021/bi034519u
https://doi.org/10.1021/bi034519u
Publikováno v:
Virology. 297(2):281-288
Herpesvirus saimiri (HVS) of subgroup C efficiently induces leukemia in New World primates and transforms human lymphocytes. The viral tyrosine kinase interacting protein (Tip) binds to the tyrosine protein kinase Lck and is essential for transformat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14864a7d8db235c8d015a5be66ab934b
Autor:
Peter G. Medveczky, Bartholomew M. Sefton, David A. Hartley, Kambiz Amdjadi, Tamara R. Hurley, Troy C. Lund
Publikováno v:
Virology. 276(2):339-348
The Tip protein of Herpesvirus saimiri strain 484C binds to and activates the Lck tyrosine protein kinase. Two sequences in the Tip protein were previously shown to be involved in binding to Lck. A proline-rich region, residues 132–141, binds to th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a723b7dd40d7363c71fdb806ad61b06
Autor:
Maria M. Medveczky, Cynthia Coleman, Richard Jove, Troy C. Lund, Bartholomew M. Sefton, Peter G. Medveczky, Elizabeth Horvath
Publikováno v:
Cellular Signalling. 11:789-796
Constitutive activation of the Src-family kinase Lck has been shown to lead to transformation. Constitutive activation of the STAT pathway of transcription factors has also been shown to be involved in transformation. An oncogenic form of the prototy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6362f496d769b558c0317b3d4cfab2c7
https://doi.org/10.1016/s0898-6568(99)00045-5
https://doi.org/10.1016/s0898-6568(99)00045-5
Publikováno v:
Journal of Biological Chemistry. 272:25429-25432
Members of the Src family of non-receptor tyrosine protein kinases are known to be inhibited by the intramolecular association between a phosphorylated carboxyl-terminal tyrosine residue and the SH2 domain. We have previously shown that exposure of c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::807d93bd84ca3c599e74ef1058920613
https://doi.org/10.1074/jbc.272.41.25429
https://doi.org/10.1074/jbc.272.41.25429
Publikováno v:
Journal of Biological Chemistry. 271:12549-12554
Lck, a lymphocyte-specific tyrosine protein kinase, is bound to cellular membranes as the result of myristoylation and palmitoylation of its amino terminus. Its activity is inhibited by phosphorylation of tyrosine 394. The Tyr-505 --> Phe mutant of L
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d190b0b021118c05577de5d8c584ddd
https://doi.org/10.1074/jbc.271.21.12549
https://doi.org/10.1074/jbc.271.21.12549
Publikováno v:
Journal of Biological Chemistry. 269:13529-13535
In addition to membrane immunoglobulin (mIg), the B-cell antigen receptor contains Ig-alpha/Ig-beta heterodimers that link mIg to intracellular signaling molecules. To compare the ability of the cytoplasmic domains of Ig-alpha and Ig-beta to transduc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::51ce3ca1277a3f1475d8f7b6a97401b9
https://doi.org/10.1016/s0021-9258(17)36863-1
https://doi.org/10.1016/s0021-9258(17)36863-1