SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling - sprookjes - yvandenbroek - TriplyDB

SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling

SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling

http://www.wikidata.org/entity/Q24655178

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Functional cloning of Src-like adapter protein-2 (SLAP-2), a novel inhibitor of antigen receptor signaling A novel Src homology 2 domain-containing molecule, Src-like adapter protein-2 (SLAP-2), which negatively regulates T cell receptor signaling Functional cooperation between c-Cbl and Src-like adaptor protein 2 in the negative regulation of T-cell receptor signaling.Ubiquitylation as a Rheostat for TCR Signaling: From Targeted Approaches Toward Global Profiling The Emerging and Diverse Roles of Src-Like Adaptor Proteins in Health and Disease SKAP55 recruits to lipid rafts and positively mediates the MAPK pathway upon T cell receptor activation 90-kDa ribosomal S6 kinase is a direct target for the nuclear fibroblast growth factor receptor 1 (FGFR1): role in FGFR1 signaling The Cbl interactome and its functions Role of SRC-like adaptor protein (SLAP) in immune and malignant cell signaling.SLAP displays tumour suppressor functions in colorectal cancer via destabilization of the SRC substrate EPHA2.Src-like adaptor protein (SLAP) is a negative regulator of T cell receptor signaling On-bead screening of combinatorial libraries: reduction of nonspecific binding by decreasing surface ligand density.SLAP deficiency decreases dsDNA autoantibody production Tonic ubiquitylation controls T-cell receptor:CD3 complex expression during T-cell development Sin: good or bad? A T lymphocyte perspective.The adapter molecule Sin regulates T-cell-receptor-mediated signal transduction by modulating signaling substrate availability.Beyond the RING: CBL proteins as multivalent adapters.Effect of redox balance alterations on cellular localization of LAT and downstream T-cell receptor signaling pathways SLI-1 Cbl inhibits the engulfment of apoptotic cells in C. elegans through a ligase-independent function Src-Like adaptor protein (SLAP) binds to the receptor tyrosine kinase Flt3 and modulates receptor stability and downstream signaling.Regulation of T cell receptor complex-mediated signaling by ubiquitin and ubiquitin-like modifications Negative feedback of T cell activation through inhibitory adapters and costimulatory receptors.Src-like adaptor protein (SLAP) regulates B cell receptor levels in a c-Cbl-dependent manner.c-Cbl and Cbl-b ubiquitin ligases: substrate diversity and the negative regulation of signalling responses.Mechanism of upregulation of the inhibitory regulator, src-like adaptor protein (SLAP), by glucocorticoids in mast cells.Src-like adaptor protein (SLAP) is upregulated in antigen-stimulated mast cells and acts as a negative regulator.Cbl-family proteins as regulators of cytoskeleton-dependent phenomena.Src-like adaptor protein down-regulates T cell receptor (TCR)-CD3 expression by targeting TCRzeta for degradation.Cbl promotes ubiquitination of the T cell receptor zeta through an adaptor function of Zap-70.c-Cbl-facilitated cytoskeletal effects in v-Abl-transformed fibroblasts are regulated by membrane association of c-Cbl.Negative regulation of immunoreceptor signaling by protein adapters: Shc proteins join the club.Src-like adaptor protein regulates TCR expression on thymocytes by linking the ubiquitin ligase c-Cbl to the TCR complex.SRC-like adaptor protein 2 (SLAP2) is a negative regulator of KIT-D816V-mediated oncogenic transformation.

P2860

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P2860

SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling

http://www.wikidata.org/entity/Q24655178

description

1999 nî lūn-bûn

@nan

1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

1999年の論文

@ja

1999年論文

@yue

1999年論文

@zh-hant

1999年論文

@zh-hk

1999年論文

@zh-mo

1999年論文

@zh-tw

1999年论文

@wuu

name

SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling

@ast

SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling

@en

SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling

@nl

type

label

SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling

@ast

SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling

@en

SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling

@nl

prefLabel

SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling

@ast

SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling

@en

SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling

@nl

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PNAS.96.17.9775

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Proceedings of the National Academy of Sciences of the United States of America

P1476

SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling

@en

P2093

J H Chang

http://www.w3.org/2001/XMLSchema#string

J Tang

http://www.w3.org/2001/XMLSchema#string

S J Burakoff

http://www.w3.org/2001/XMLSchema#string

S Sawasdikosol

http://www.w3.org/2001/XMLSchema#string

P2860

Characterization of a novel Src-like adapter protein that associates with the Eck receptor tyrosine kinase

Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G

Src-like adaptor protein (Slap) is a negative regulator of mitogenesis

LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation

Syk and ZAP-70 mediate recruitment of p56lck/CD4 to the activated T cell receptor/CD3/zeta complex

Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase

Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast

Direct regulation of ZAP-70 by SHP-1 in T cell antigen receptor signaling

A novel phosphotyrosine-binding domain in the N-terminal transforming region of Cbl interacts directly and selectively with ZAP-70 in T cells

The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav

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9775-80

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scholarly article

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10.1073/PNAS.96.17.9775

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17

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12849619

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10449770

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P932

22286

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