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ZAP70 protein, human
Known as:
syk-related tyrosine kinase, human
, Zeta-Chain Associated Protein Kinase
, Zeta-Chain Associated Protein Kinase, 70kd
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Tyrosine-protein kinase ZAP-70 (619 aa, ~70 kDa) is encoded by the human ZAP70 gene. This protein plays a role in both tyrosine phosphorylation and…
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National Institutes of Health
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Related topics
Related topics
21 relations
Cell Differentiation process
Cell Proliferation
Enzyme Gene
Natural Killer Cells
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Broader (1)
ZAP-70 Kinase
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2009
Review
2009
The structure, regulation, and function of ZAP‐70
Byron B. Au-Yeung
,
S. Deindl
,
+4 authors
A. Weiss
Immunological Reviews
2009
Corpus ID: 2488987
Summary: The tyrosine ZAP‐70 (ζ‐associated protein of 70 kDa) kinase plays a critical role in activating many downstream signal…
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Highly Cited
2002
Highly Cited
2002
T cell receptor ligation induces the formation of dynamically regulated signaling assemblies
S. Bunnell
,
D. I. Hong
,
+4 authors
L. Samelson
Journal of Cell Biology
2002
Corpus ID: 2825380
Tcell antigen receptor (TCR) ligation initiates tyrosine kinase activation, signaling complex assembly, and immune synapse…
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Highly Cited
1999
Highly Cited
1999
Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase
W. Meng
,
S. Sawasdikosol
,
S. Burakoff
,
M. Eck
Nature
1999
Corpus ID: 4411124
Cbl is an adaptor protein that functions as a negative regulator of many signalling pathways that start from receptors at the…
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Highly Cited
1998
Highly Cited
1998
Tandem SH2 Domains Confer High Specificity in Tyrosine Kinase Signaling*
E. Ottinger
,
M. Botfield
,
S. Shoelson
Journal of Biological Chemistry
1998
Corpus ID: 45578326
SH2 domain proteins transmit intracellular signals initiated by activated tyrosine kinase-linked receptors. Recent three…
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Highly Cited
1998
Highly Cited
1998
Tissue Hyperplasia and Enhanced T-Cell Signalling via ZAP-70 in c-Cbl-Deficient Mice
M. A. Murphy
,
Ralf Schnall
,
+5 authors
D. Bowtell
Molecular and Cellular Biology
1998
Corpus ID: 44481034
ABSTRACT The c-Cbl protein is tyrosine phosphorylated and forms complexes with a wide range of signalling partners in response to…
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Highly Cited
1998
Highly Cited
1998
Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide.
K. Fütterer
,
Jane Wong
,
R. Grucza
,
A. Chan
,
G. Waksman
Journal of Molecular Biology
1998
Corpus ID: 23060479
The Syk family of kinases, consisting of ZAP-70 and Syk, play essential roles in a variety of immune and non-immune cells. This…
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Highly Cited
1997
Highly Cited
1997
The Cbl Phosphotyrosine-binding Domain Selects a D(N/D)XpY Motif and Binds to the Tyr292Negative Regulatory Phosphorylation Site of ZAP-70*
M. Lupher
,
Songyang Zhou
,
S. Shoelson
,
L. Cantley
,
H. Band
Journal of Biological Chemistry
1997
Corpus ID: 8179761
The Cbl protooncogene product has emerged as a novel negative regulator of receptor and non-receptor tyrosine kinases through…
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Highly Cited
1996
Highly Cited
1996
Direct Regulation of ZAP-70 by SHP-1 in T Cell Antigen Receptor Signaling
D. Plas
,
Robin D. Johnson
,
+5 authors
M. Thomas
Science
1996
Corpus ID: 41401787
The threshold at which antigen triggers lymphocyte activation is set by the enzymes that regulate tyrosine phosphorylation. Upon…
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Highly Cited
1994
Highly Cited
1994
Differential expression of ZAP-70 and Syk protein tyrosine kinases, and the role of this family of protein tyrosine kinases in TCR signaling.
Andrew C. Chan
,
N. S. C. V. Oers
,
+5 authors
Arthur Weiss
Journal of Immunology
1994
Corpus ID: 37831763
TCR stimulation results in the tyrosine phosphorylation of a number of cellular substrates. We have recently identified a 70-kDa…
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Highly Cited
1992
Highly Cited
1992
A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases.
N. X. Krueger
,
H. Saito
Proceedings of the National Academy of Sciences…
1992
Corpus ID: 45972746
Protein-tyrosine-phosphatases (PTPases, EC 3.1.3.48) play a crucial role in the regulation of protein tyrosine phosphorylation…
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