Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Josephine Schembri-King"'
Publikováno v:
The Journal of Immunology. 164:5199-5206
Lnk was originally cloned from a rat lymph node cDNA library and shown to participate in T cell signaling. Human Lnk (hLnk) was cloned by screening a Jurkat cell cDNA library. hLnk has a calculated molecular mass of 63 kDa, and its deduced amino acid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a5682917d4c9f122245a9474a286150
https://doi.org/10.4049/jimmunol.164.10.5199
https://doi.org/10.4049/jimmunol.164.10.5199
Autor:
Randall W. Barton, Josephine Schembri-King, Thomas C. Warren, Gregory W. Peet, Marilyn Kehry, Jun Li, Steven S. Pullen, Kenneth B. Marcu, Scott Jakes
Publikováno v:
Journal of Biological Chemistry. 273:30736-30741
Activation of the transcription factor NF-κB is regulated by the phosphorylation and subsequent degradation of its inhibitory subunit, IκB. A large multiprotein complex, the IκB kinase (IKK), catalyzes the phosphorylation of IκB. The two kinase c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bbabc14b5ccad59ee6794915af347b99
https://doi.org/10.1074/jbc.273.46.30736
https://doi.org/10.1074/jbc.273.46.30736
Autor:
Raj Betageri, John R. Proudfoot, Thomas C. Warren, Susan Lukas, Josephine Schembri-King, Liang Tong, Scott Jakes
Publikováno v:
Journal of Biological Chemistry. 273:20238-20242
The crystal structure of human p56lck SH2 domain in complex with an inhibitor containing the singly chargedp-(carboxymethyl)phenylalanine residue (cmF) as a phosphotyrosine (Tyr(P) or pY) replacement has been determined at 1.8 A resolution. The bindi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6fc5b6112295c5916d495df6479ad36
https://doi.org/10.1074/jbc.273.32.20238
https://doi.org/10.1074/jbc.273.32.20238
Autor:
Daniel J. Greenwood, Thomas C. Warren, Richard H. Ingraham, Mark E. Labadia, Scott Jakes, Susan Lukas, Josephine Schembri-King, Christine A. Grygon
Publikováno v:
Archives of Biochemistry and Biophysics. 342:117-125
One of the key steps involved in T-cell activation is binding of the tyrosine kinase ZAP-70 via its two SH2 domains to peptide segments termed tyrosine-based activation motifs (ITAM) which are present in three of the T-cell receptor (TCR) subunits. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::caacc39690823cac5286ac0d0eaeba6f
https://doi.org/10.1006/abbi.1997.0118
https://doi.org/10.1006/abbi.1997.0118
Autor:
Richard H. Ingraham, Josephine Schembri-King, Scott Jakes, Maurice M. Morelock, Mark E. Labadia
Publikováno v:
Journal of Leukocyte Biology. 59:740-746
The chains of the T cell receptor complex play a critical role in the initiation of proximal signaling events upon T cell activation. Three pairs of potential tyrosine phosphorylation sites are located within the cytoplasmic domains of the chains. Su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a31465c11e487b5d9a1f3a366fcd866a
https://doi.org/10.1002/jlb.59.5.740
https://doi.org/10.1002/jlb.59.5.740
Publikováno v:
Molecular immunology. 37(10)
Human Lnk (hLnk) is an adaptor protein with multiple functional domains that regulates T cell activation signaling. In order to identify cellular Lnk binding partners, a yeast two-hybrid screening of human spleen cDNA library was carried out using hu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::691aa9ab6a10ce261279d7b343960542
https://pubmed.ncbi.nlm.nih.gov/11163396
https://pubmed.ncbi.nlm.nih.gov/11163396