Zobrazeno 1 - 10
of 28
pro vyhledávání: '"S E, Shoelson"'
Publikováno v:
The Journal of Immunology. 157:110-116
Crk is a Src homology 2 (SH2)/Src homology 3 (SH3)-containing adapter protein that has been implicated in intracellular signaling in fibroblasts and PC12 pheochromocytoma cells. Crk has been shown to bind to a tyrosine-phosphorylated protein of 116 k
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9e70f74a36581e013b9515ded4566b8b
https://doi.org/10.4049/jimmunol.157.1.110
https://doi.org/10.4049/jimmunol.157.1.110
Publikováno v:
International journal of obesity and related metabolic disorders : journal of the International Association for the Study of Obesity. 27
Antidiabetic effects associated with salicylates have been known for years, although the underlying mechanisms were not understood. We have been reinvestigating these effects in the light of recent discoveries in the areas of signal transduction and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6acd279c140f1758c9dd451b5f4e0435
https://pubmed.ncbi.nlm.nih.gov/14704745
https://pubmed.ncbi.nlm.nih.gov/14704745
Publikováno v:
The Journal of biological chemistry. 272(5)
cDNA clones encoding human (h) Grb7 and a previously unknown protein with high homology to hGrb-IR and mGrb10 (where m indicates mouse) were found by screening expressed sequence tag data bases. hGrb7 mRNA expression is greatest in pancreas and restr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2787584e72f4aa75ad5a1a84ac0371de
https://pubmed.ncbi.nlm.nih.gov/9006901
https://pubmed.ncbi.nlm.nih.gov/9006901
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 157(1)
Crk is a Src homology 2 (SH2)/Src homology 3 (SH3)-containing adapter protein that has been implicated in intracellular signaling in fibroblasts and PC12 pheochromocytoma cells. Crk has been shown to bind to a tyrosine-phosphorylated protein of 116 k
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0f5de2fc3c45ecc8373f614cd6db6a8e
https://pubmed.ncbi.nlm.nih.gov/8683103
https://pubmed.ncbi.nlm.nih.gov/8683103
Autor:
T, Fukazawa, K A, Reedquist, T, Trub, S, Soltoff, G, Panchamoorthy, B, Druker, L, Cantley, S E, Shoelson, H, Band
Publikováno v:
The Journal of biological chemistry. 270(32)
Previously, we have identified p120 as a Fyn/Lck SH3 and SH2 domain-binding protein that is tyrosine phosphorylated rapidly after T cell receptor triggering. Here, we used direct protein purification, amino acid sequence analysis, reactivity with ant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ec416fb1f6960b7c4529b42eefbe4863
https://pubmed.ncbi.nlm.nih.gov/7642581
https://pubmed.ncbi.nlm.nih.gov/7642581
Publikováno v:
The Journal of biological chemistry. 269(48)
Phosphorylation of c-Src at carboxyl-terminal Tyr-527 suppresses tyrosine kinase activity and transforming potential, presumably by facilitating the intramolecular interaction of the C terminus of Src with its SH2 domain. In addition, it has been sho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0b1686b616fd843893df064b5b3192ee
https://pubmed.ncbi.nlm.nih.gov/7527032
https://pubmed.ncbi.nlm.nih.gov/7527032
Autor:
S, Xiao, D W, Rose, T, Sasaoka, H, Maegawa, T R, Burke, P P, Roller, S E, Shoelson, J M, Olefsky
Publikováno v:
The Journal of biological chemistry. 269(33)
Syp (SH-PTP2) was recently identified as a phosphotyrosine phosphatase containing two SH2 domains within its primary structure. In response to appropriate growth factor stimulation, Syp becomes phosphorylated on tyrosine residues and associates with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::29b53246c39a4c8ec82d07f4edb17000
https://pubmed.ncbi.nlm.nih.gov/8063747
https://pubmed.ncbi.nlm.nih.gov/8063747
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 91(10), 4135-4139. National Academy of Sciences
Scopus-Elsevier
Scopus-Elsevier
Tyrosine phosphorylation of cellular proteins is the earliest identifiable event following T-cell antigen receptor (TCR) stimulation and is essential for activating downstream signaling machinery. Two Src-family protein-tyrosine kinases, the TCR-asso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95e882e456af694dc5be9abae2993fd5
https://europepmc.org/articles/PMC43739/
https://europepmc.org/articles/PMC43739/
Publikováno v:
The Journal of biological chemistry. 269(18)
The cytoplasmic insulin receptor substrate-1 (IRS-1), which is multiply phosphorylated in vivo on tyrosine residues, is a known binding protein for the tandem src homology 2 (SH2) domain-containing protein tyrosine phosphatase, SH-PTP2. Eleven phosph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dda5f9d3090a38b7d20ff652b646fe70
https://pubmed.ncbi.nlm.nih.gov/7513703
https://pubmed.ncbi.nlm.nih.gov/7513703
Publikováno v:
The Journal of biological chemistry. 269(14)
Signaling by tyrosine kinases involves direct associations between proteins with Src homology 2 (SH2) domains and sites of tyrosine phosphorylation. Specificity in signaling pathways results in part from inherent selectivity in interactions between p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::86664d5878b63c887a761fc676411c4b
https://pubmed.ncbi.nlm.nih.gov/8144631
https://pubmed.ncbi.nlm.nih.gov/8144631