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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… 
National Institutes of Health

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14-3-3 Protein, epsilon Isoform14-3-3 Protein, eta IsoformGRF5 protein, ArabidopsisSFN protein, human
In BloodProcess of secretionYWHAE wt Alleleagonists

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2005
Review
2005
14-3-3 proteins—an update
ABSTRACT14-3-3 is a highly conserved acidic protein family, composed of seven isoforms in mammals. 14-3-3 protein can interact… 
Highly Cited
2005
Highly Cited
2005
JNK antagonizes Akt-mediated survival signals by phosphorylating 14-3-3
Life and death decisions are made by integrating a variety of apoptotic and survival signals in mammalian cells. Therefore, there… 
Review
2004
Review
2004
Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes.
14-3-3 proteins exert an extraordinarily widespread influence on cellular processes in all eukaryotes. They operate by binding to… 
Highly Cited
2004
Highly Cited
2004
JNK promotes Bax translocation to mitochondria through phosphorylation of 14‐3‐3 proteins
Targeted gene disruption studies have established that the c‐Jun NH2‐terminal kinase (JNK) is required for the stress‐induced… 
Review
2004
Review
2004
Unlocking the code of 14-3-3
One of the most striking `rags to riches' stories in the protein world is that of 14-3-3, originally identified in 1967 as merely… 
Highly Cited
2003
Highly Cited
2003
Identification of a Proline-rich Akt Substrate as a 14-3-3 Binding Partner*
Akt (also called protein kinase B) is one of the major downstream targets of the phosphatidylinositol 3-kinase pathway. This… 
Highly Cited
2001
Highly Cited
2001
14-3-3 Proteins Mediate an Essential Anti-apoptotic Signal*
The 14-3-3 proteins are a family of highly conserved eukaryotic regulatory molecules that play important roles in many biological… 
Highly Cited
2001
Highly Cited
2001
Positive regulation of Wee1 by Chk1 and 14-3-3 proteins.
Wee1 inactivates the Cdc2-cyclin B complex during interphase by phosphorylating Cdc2 on Tyr-15. The activity of Wee1 is highly… 
Highly Cited
1999
Highly Cited
1999
α-Synuclein Shares Physical and Functional Homology with 14-3-3 Proteins
α-Synuclein has been implicated in the pathophysiology of many neurodegenerative diseases, including Parkinson’s disease (PD) and… 
Highly Cited
1999
Highly Cited
1999
Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display.
The 14-3-3 proteins interact with diverse cellular molecules involved in various signal transduction pathways controlling cell… 
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