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phosphotyrosine binding

Interacting selectively and non-covalently with a phosphorylated tyrosine residue within a protein. [PMID:14636584]
National Institutes of Health

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Highly Cited
2008
Highly Cited
2008
Created with both in vitro and in vivo data, NetPhorest is an atlas of consensus sequence motifs for 179 kinases and 104… Expand
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Highly Cited
2008
Highly Cited
2008
The activation of integrin adhesion receptors from low to high affinity in response to intracellular cues controls cell adhesion… Expand
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Highly Cited
2007
Highly Cited
2007
To the editor: Protein phosphorylation is a covalent posttranslational modification event that is essential for regulation and… Expand
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Highly Cited
2006
Highly Cited
2006
Although epidermal growth factor receptor (EGFR; also called ErbB1) and its relatives initiate one of the most well-studied… Expand
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Highly Cited
2006
Highly Cited
2006
Adiponectin, also known as Acrp30, is an adipose tissue-derived hormone with anti-atherogenic, anti-diabetic and insulin… Expand
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Highly Cited
2003
Highly Cited
2003
The binding of cytoplasmic proteins, such as talin, to the cytoplasmic domains of integrin adhesion receptors mediates… Expand
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Highly Cited
2001
Highly Cited
2001
Atherogenic low density lipoproteins are cleared from the circulation by hepatic low density lipoprotein receptors (LDLR). Two… Expand
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Highly Cited
1999
Highly Cited
1999
Protein tyrosine phosphatases act in conjunction with protein kinases to regulate the tyrosine phosphorylation events that… Expand
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Highly Cited
1997
Highly Cited
1997
We have previously identified a 160-kDa protein in human embryonic kidney (HEK) 293 cells that undergoes rapid tyrosine… Expand
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Highly Cited
1997
Highly Cited
1997
Here, we identify a mouse homolog of the Drosophila Disabled (Dab) protein, mDab1, and show it is an adaptor molecule functioning… Expand
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