Zobrazeno 1 - 10
of 17
pro vyhledávání: '"B G Neel"'
Publikováno v:
The Journal of Immunology. 159:4233-4243
CD22 is a B cell membrane glycoprotein that, upon Ag receptor engagement, becomes rapidly tyrosyl phosphorylated and associates with several signaling molecules including Lyn, Syk, PLCgamma1, and the protein-tyrosine phosphatase, SHP-1. Two allelic f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6028406240f6a805eeb9d1055c1a82ad
https://doi.org/10.4049/jimmunol.159.9.4233
https://doi.org/10.4049/jimmunol.159.9.4233
Publikováno v:
Molecular and Cellular Biology. 15:7050-7058
Interferons (IFNs) induce early-response genes by stimulating Janus family (Jak) tyrosine kinases, leading to tyrosine phosphorylation of Stat transcription factors. Previous studies implicated protein-tyrosine phosphatase (PTP) activity in the contr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::faba136c8d780244dd043f509ddbdedf
https://doi.org/10.1128/mcb.15.12.7050
https://doi.org/10.1128/mcb.15.12.7050
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 159(9)
CD22 is a B cell membrane glycoprotein that, upon Ag receptor engagement, becomes rapidly tyrosyl phosphorylated and associates with several signaling molecules including Lyn, Syk, PLCgamma1, and the protein-tyrosine phosphatase, SHP-1. Two allelic f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a7d6289b85ee34476b8a974fc1c90b20
https://pubmed.ncbi.nlm.nih.gov/9379018
https://pubmed.ncbi.nlm.nih.gov/9379018
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
Autor:
V I, Shifrin, B G, Neel
Publikováno v:
The Journal of biological chemistry. 268(34)
PTP-1B is a major nontransmembrane phosphotyrosine phosphatase in human cell lines and tissues, but its physiological function(s) and mechanism(s) of regulation are largely unknown. We have found that in human diploid fibroblasts a novel PTP-1B mRNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::200820e46967756ccdc59715cf4fcdee
https://pubmed.ncbi.nlm.nih.gov/8244970
https://pubmed.ncbi.nlm.nih.gov/8244970
Publikováno v:
The Journal of biological chemistry. 268(30)
A human protein tyrosine phosphatase containing two src homology 2 (SH2) domains (SH-PTP2) was expressed in Escherichia coli under T7 promoter control and purified to near homogeneity. The purified protein, with molecular mass of 68 kDa on SDS-polyac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4de4718f7f34621896ce8b3c2130b106
https://pubmed.ncbi.nlm.nih.gov/8226787
https://pubmed.ncbi.nlm.nih.gov/8226787
Autor:
R J, Lechleider, S, Sugimoto, A M, Bennett, A S, Kashishian, J A, Cooper, S E, Shoelson, C T, Walsh, B G, Neel
Publikováno v:
The Journal of biological chemistry. 268(29)
Much progress has been made in elucidating early events in signal transduction by growth factor receptors with intrinsic tyrosine kinase activity. Upon ligand addition, these receptors dimerize and activate, becoming phosphorylated at a number of tyr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c79e36c3f2f08cff077ceedc0f607de6
https://pubmed.ncbi.nlm.nih.gov/7691811
https://pubmed.ncbi.nlm.nih.gov/7691811
Publikováno v:
The Journal of biological chemistry. 268(18)
The pivotal role of tyrosine kinases in signal transduction is well established, but the role of tyrosine phosphatases remains obscure. The discovery of src homology 2 domain-containing protein tyrosine phosphatases suggested roles for these molecule
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::62077b699363306f5ac5aea1c28201c3
https://pubmed.ncbi.nlm.nih.gov/8514779
https://pubmed.ncbi.nlm.nih.gov/8514779
Publikováno v:
Oncogene. 6(10)
One of the three human retinoic acid receptors, RAR-beta, maps to a region on the short arm of chromosome 3 frequently deleted in lung cancer. Because retinoic acid is required for normal epithelial cell growth and regulation, and loss of a retinoic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b8fe77a62b2ab22ef737bbc3e14c46ae
https://pubmed.ncbi.nlm.nih.gov/1717924
https://pubmed.ncbi.nlm.nih.gov/1717924