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CSK protein, human
Known as:
Protein-Tyrosine Kinase CYL
, EC 2.7.1.112
, CSK Protein Kinase
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Tyrosine-protein kinase CSK (450 aa, ~51 kDa) is encoded by the human CSK gene. This protein plays a role in tyrosine phosphorylation, signal…
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National Institutes of Health
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Related topics
Related topics
24 relations
B Cell Receptor Signaling Pathway
CSK gene
Cell Cycle Control
Cell Differentiation process
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Broader (2)
Protein Tyrosine Kinase
protein-tyrosine kinase c-src
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2012
Highly Cited
2012
LYP inhibits T cell activation when dissociated from CSK
T. Vang
,
Wallace H. Liu
,
+15 authors
L. Tautz
Nature Chemical Biology
2012
Corpus ID: 14641522
Lymphoid tyrosine phosphatase (LYP) and C-terminal Src kinase (CSK) are negative regulators of signaling mediated through the T…
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Highly Cited
2012
Highly Cited
2012
CSK regulatory polymorphism is associated with systemic lupus erythematosus and influences B cell signaling and activation
Nataly Manjarrez-Orduño
,
E. Marasco
,
+20 authors
P. Gregersen
Nature Genetics
2012
Corpus ID: 5861333
The c-Src tyrosine kinase, Csk, physically interacts with the intracellular phosphatase Lyp (encoded by PTPN22) and can modify…
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Highly Cited
2008
Highly Cited
2008
The ancestral symbiont sensor kinase CSK links photosynthesis with gene expression in chloroplasts
Sujith Puthiyaveetil
,
T. Kavanagh
,
+7 authors
J. Allen
Proceedings of the National Academy of Sciences…
2008
Corpus ID: 4977043
We describe a novel, typically prokaryotic, sensor kinase in chloroplasts of green plants. The gene for this chloroplast sensor…
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Review
2005
Review
2005
C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK)—endogenous negative regulators of Src-family protein kinases
Y. Chong
,
T. Mulhern
,
Heung-Chin Cheng
Growth Factors
2005
Corpus ID: 38227036
C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK) are endogenous inhibitors of the Src-family protein tyrosine kinases…
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Review
2002
Review
2002
Models of cytoskeletal mechanics of adherent cells
D. Stamenović
,
D. Ingber
Biomechanics and Modeling in Mechanobiology
2002
Corpus ID: 7986228
Abstract Adherent cells sense their mechanical environment, which, in turn, regulates their functions. During the past decade, a…
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Highly Cited
1999
Highly Cited
1999
The role of prestress and architecture of the cytoskeleton and deformability of cytoskeletal filaments in mechanics of adherent cells: a quantitative analysis.
D. Stamenović
,
M. Coughlin
Journal of Theoretical Biology
1999
Corpus ID: 44648053
Mechanical properties of adherent cells were investigated using methods of engineering mechanics. The cytoskeleton (CSK) was…
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Highly Cited
1995
Highly Cited
1995
The nonreceptor protein-tyrosine kinase CSK complexes directly with the GTPase-activating protein-associated p62 protein in cells expressing v-Src or activated c-Src
K. Neet
,
T. Hunter
Molecular and Cellular Biology
1995
Corpus ID: 45527976
CSK is a predominantly cytosolic protein-tyrosine kinase (PTK) that negatively regulates Src family PTKs by phosphorylation of a…
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Highly Cited
1995
Highly Cited
1995
35H, a Sequence Isolated as a Protein Kinase C Binding Protein, Is a Novel Member of the Adducin Family (*)
Liqun Dong
,
C. Chapline
,
+4 authors
S. Jaken
Journal of Biological Chemistry
1995
Corpus ID: 23419157
We recently cloned a partial cDNA (35H) for a protein kinase C (PKC) binding protein from a rat kidney cDNA library and…
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Highly Cited
1993
Highly Cited
1993
Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae
S. Murphy
,
M. Bergman
,
David O. Morgan
Molecular and Cellular Biology
1993
Corpus ID: 43011217
The kinase activity of c-Src is normally repressed in vertebrate cells by extensive phosphorylation of Y-527. C-terminal Src…
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Highly Cited
1991
Highly Cited
1991
CSK: a protein-tyrosine kinase involved in regulation of src family kinases.
M. Okada
,
S. Nada
,
Y. Yamanashi
,
Tadashi Yamamoto
,
H. Nakagawa
Journal of Biological Chemistry
1991
Corpus ID: 38781937
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