phosphotyrosine binding

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

Topic mentions per year

Topic mentions per year

1992-2018
0102019922018

Papers overview

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Highly Cited
2005
Highly Cited
2005
In eukaryotic cells, the SH2 and PTB domains mediate protein-protein interactions by recognizing phosphotyrosine residues on… (More)
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2004
2004
Ser/Thr phosphorylation of insulin receptor substrate (IRS) proteins negatively modulates insulin signaling. Therefore, the… (More)
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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… (More)
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1997
1997
The adapter protein Shc is a critical component of mitogenic signaling pathways initiated by a number of receptors. Shc can… (More)
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Highly Cited
1997
Highly Cited
1997
Two mammalian receptor tyrosine kinases (DDR1 and DDR2) have extracellular domains closely related to a D. discoideum lectin… (More)
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Highly Cited
1997
Highly Cited
1997
A 60-kDa protein that undergoes rapid tyrosine phosphorylation in response to insulin and then binds phosphatidylinositol 3… (More)
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Highly Cited
1997
Highly Cited
1997
Insulin binding to its receptor induces the phosphorylation of cytosolic substrates, insulin receptor substrate (IRS)-1 and IRS-2… (More)
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Highly Cited
1996
Highly Cited
1996
The phosphotyrosine interaction (PI) domains (also known as the PTB, or phosphotyrosine binding, domains) of Shc and IRS-1 are… (More)
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Highly Cited
1995
Highly Cited
1995
The nuclear magnetic resonance structure of the phosphotyrosine binding (PTB) domain of Shc complexed to a phosphopeptide reveals… (More)
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Highly Cited
1995
Highly Cited
1995
Fe65 is a protein mainly expressed in several districts of the mammalian nervous system. The search of protein sequence data… (More)
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