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Adaptor Proteins, Signal Transducing
Known as:
Adapter Signaling Protein
, Signal Transducing Adaptor Protein
, Adaptor Protein
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A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having…
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National Institutes of Health
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Related topics
Related topics
49 relations
ABI1 protein, human
FRS3 protein, human
Process of secretion
SH2 domain-containing leukocyte protein, 76-kDa
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Narrower (37)
ATG13 protein, human
ATRIP protein, human
Abtb2 protein, rat
Agtrap protein, mouse
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2007
Highly Cited
2007
Regulation of NF-κB Activation in T Cells via Association of the Adapter Proteins ADAP and CARMA1
R. B. Medeiros
,
B. Burbach
,
+5 authors
Y. Shimizu
Science
2007
Corpus ID: 46443224
The adapter protein ADAP regulates T lymphocyte adhesion and activation. We present evidence for a previously unrecognized…
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Highly Cited
2002
Highly Cited
2002
Lipid Raft Heterogeneity in Human Peripheral Blood T Lymphoblasts: A Mechanism for Regulating the Initiation of TCR Signal Transduction1
A. Schade
,
A. Levine
Journal of Immunology
2002
Corpus ID: 41915444
Lateral mobility and spatial organization of proteins within the plasma membrane are likely to mediate the initial events…
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Highly Cited
2000
Highly Cited
2000
Cutting Edge: A Novel Function for the SLAP-130/FYB Adapter Protein in β1 Integrin Signaling and T Lymphocyte Migration1
Anne J. Hunter
,
Nadine C. Ottoson
,
N. Boerth
,
G. Koretzky
,
Y. Shimizu
Journal of Immunology
2000
Corpus ID: 24221421
The role of integrin-mediated signaling events in T cell function remains incompletely characterized. We report here that α4β1…
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Highly Cited
1999
Highly Cited
1999
mGrb10 Interacts with Nedd4*
A. Morrione
,
P. Plant
,
+4 authors
R. Baserga
Journal of Biological Chemistry
1999
Corpus ID: 7062706
We have utilized the yeast two-hybrid system to identify proteins interacting with mouse Grb10, an adapter protein known to…
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Highly Cited
1998
Highly Cited
1998
Neuroendocrine Synaptic Vesicles Are Formed In Vitro by Both Clathrin-dependent and Clathrin-independent Pathways
G. Shi
,
V. Faundez
,
J. Roos
,
E. C. Dell’Angelica
,
R. Kelly
Journal of Cell Biology
1998
Corpus ID: 108793
In the neuroendocrine cell line, PC12, synaptic vesicles can be generated from endosomes by a sorting and vesiculation process…
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Highly Cited
1997
Highly Cited
1997
RAFTK, a Novel Member of the Focal Adhesion Kinase Family, Is Phosphorylated and Associates with Signaling Molecules upon Activation of Mature T Lymphocytes
R. Ganju
,
W. Hatch
,
+4 authors
J. Groopman
Journal of Experimental Medicine
1997
Corpus ID: 6667742
The related adhesion focal tyrosine kinase (RAFTK), a recently discovered member of the focal adhesion kinase family, has…
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Highly Cited
1996
Highly Cited
1996
Syk-dependent Phosphorylation of Shc
Bana Jabril-Cuenod
,
Cheng Zhang
,
+4 authors
J. Kinet
Journal of Biological Chemistry
1996
Corpus ID: 817447
Antigen receptors on T- and B-cells activate Ras through a signaling pathway that results in the tyrosine phosphorylation of Shc…
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Highly Cited
1996
Highly Cited
1996
Activation-induced Association of a 145-kDa Tyrosine-phosphorylated Protein with Shc and Syk in B Lymphocytes and Macrophages (*)
M. Crowley
,
S. Harmer
,
A. DeFranco
Journal of Biological Chemistry
1996
Corpus ID: 39973748
Engagement of many cell surface receptors results in tyrosine phosphorylation of an overlapping set of protein substrates. Some…
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Highly Cited
1994
Highly Cited
1994
Interleukin (IL)-3 and granulocyte/macrophage colony-stimulating factor, but not IL-4, induce tyrosine phosphorylation, activation, and association of SHPTP2 with Grb2 and phosphatidylinositol 3…
M. Welham
,
U. Dechert
,
Kevin B. Leslie
,
F. Jirik
,
John W. Schrader
Journal of Biological Chemistry
1994
Corpus ID: 46500787
Binding of interleukin (IL)-3 and granulocyte/macrophage colony-stimulating factor (GM-CSF) to their high affinity cell surface…
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Highly Cited
1989
Highly Cited
1989
Identification of a clathrin binding subunit in the HA2 adaptor protein complex.
S. Ahle
,
Ernst UngewickellS
Journal of Biological Chemistry
1989
Corpus ID: 21303535
The HA2 adaptor complex, comprising alpha-, beta-, 50-kDa, and 16-kDa subunits, was partially dissociated into its constituents…
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