14-3-3 Proteins

Known as: 14 3 3 Proteins, 14-3-3 Proteins [Chemical/Ingredient], Protein 14-3-3 
A large family of signal-transducing adaptor proteins present in wide variety of eukaryotes. They are PHOSPHOSERINE and PHOSPHOTHREONINE binding… (More)
National Institutes of Health

Topic mentions per year

Topic mentions per year

1980-2017
010020019802017

Papers overview

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Review
2016
Review
2016
14-3-3 proteins regulate intracellular signaling pathways, such as signal transduction, protein trafficking, cell cycle, and… (More)
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Highly Cited
2004
Highly Cited
2004
Targeted gene disruption studies have established that the c-Jun NH2-terminal kinase (JNK) is required for the stress-induced… (More)
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Highly Cited
2001
Highly Cited
2001
The 14-3-3 proteins are a family of highly conserved eukaryotic regulatory molecules that play important roles in many biological… (More)
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Highly Cited
2000
Highly Cited
2000
The Bcl-2 homology 3 (BH3) domain of prodeath Bcl-2 family members mediates their interaction with prosurvival Bcl-2 family… (More)
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Highly Cited
1997
Highly Cited
1997
Human Cdc25C is a dual-specificity protein phosphatase that controls entry into mitosis by dephosphorylating the protein kinase… (More)
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Highly Cited
1997
Highly Cited
1997
The 14-3-3 family of proteins mediates signal transduction by binding to phosphoserine-containing proteins. Using phosphoserine… (More)
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Highly Cited
1996
Highly Cited
1996
Extracellular survival factors alter a cell's susceptibility to apoptosis, often through posttranslational mechanisms. However… (More)
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Highly Cited
1996
Highly Cited
1996
The highly conserved and ubiquitously expressed 14-3-3 family of proteins bind to a variety of proteins involved in signal… (More)
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Highly Cited
1994
Highly Cited
1994
THE protein Raf-1, a key mediator of mitogenesis and differentia-tion, associates with p21*"a5 (refs 1-3). However, the… (More)
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Highly Cited
1994
Highly Cited
1994
To identify proteins that may participate in the activation of the protein kinase Raf, proteins that interact with Raf were… (More)
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