(Q43750956)

26 November 2017

14-3-3 proteins mediate an essential anti-apoptotic signal (English)

1 reference

26 November 2017

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Masters SC

1

1 reference

PubMed ID

11577088

26 November 2017

Fu H

series ordinal

2

1 reference

PubMed ID

11577088

26 November 2017

language of work or name

English

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publication date

27 September 2001

1 reference

Journal of Biological Chemistry

26 November 2017

1 reference

26 November 2017

276

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26 November 2017

45193-45200

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26 November 2017

48

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14-3-3 proteins: structure, function, and regulation

26 November 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

The structural basis for 14-3-3:phosphopeptide binding specificity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

Expression of constitutively active Raf-1 in the mitochondria restores antiapoptotic and leukemogenic potential of a transformation-deficient BCR/ABL mutant

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

MEK kinase 1, a substrate for DEVD-directed caspases, is involved in genotoxin-induced apoptosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

Suppression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

14-3-3 proteins block apoptosis and differentially regulate MAPK cascades

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

14-3-3 proteins are required for maintenance of Raf-1 phosphorylation and kinase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

Mutations in the hydrophobic surface of an amphipathic groove of 14-3-3zeta disrupt its interaction with Raf-1 kinase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

Raf-1 kinase and exoenzyme S interact with 14-3-3zeta through a common site involving lysine 49.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

Residues of 14-3-3 zeta required for activation of exoenzyme S of Pseudomonas aeruginosa.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

14-3-3 proteins are required for the inhibition of Ras by exoenzyme S.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

PKB/Akt: connecting phosphoinositide 3-kinase to cell survival and beyond

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

Apoptosis in cancer therapy: crossing the threshold

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

p53-dependent apoptosis modulates the cytotoxicity of anticancer agents

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

The 14-3-3 proteins encoded by the BMH1 and BMH2 genes are essential in the yeast Saccharomyces cerevisiae and can be replaced by a plant homologue.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

14-3-3 protein homologs required for the DNA damage checkpoint in fission yeast.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

14-3-3 proteins: potential roles in vesicular transport and Ras signaling in Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M105971200

21 January 2018

Identifiers

DOI

10.1074/JBC.M105971200

1 reference

26 November 2017

1 reference

PubMed ID

11577088