14-3-3 proteins in cell cycle regulation.

No abstract is available for this paper.

• Publication year

  2006

• Venue

  Seminars in Cancer Biology

• Publication date

  2006-06-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/J.SEMCANCER.2006.03.002PMID 16697662
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• DNA Damage-Induced Phosphorylation of MdmX at Serine 367 Activates p53 by Targeting MdmX for Mdm2-Dependent Degradation

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• The crystal structure of the non-liganded 14-3-3σ protein: insights into determinants of isoform specific ligand binding and dimerization

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• Comprehensive Proteomic Analysis of Interphase and Mitotic 14-3-3-binding Proteins*

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• 14-3-3 Proteins: A Number of Functions for a Numbered Protein

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• 14-3-3 suppresses the nuclear localization of threonine 157-phosphorylated p27(Kip1).

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• 14‐3‐3 suppresses the nuclear localization of threonine 157‐phosphorylated p27Kip1

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• A Role for 14-3-3τ in E2F1 Stabilization and DNA Damage-induced Apoptosis*

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• Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.

  2004cited by this paper
• 14-3-3-affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking.

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• Binding of 14-3-3β but not 14-3-3σ controls the cytoplasmic localization of CDC25B: binding site preferences of 14-3-3 subtypes and the subcellular localization of CDC25B

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• Chk1 Kinase Negatively Regulates Mitotic Function of Cdc25A Phosphatase through 14-3-3 Binding

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• Phosphorylation of p27Kip1 at Threonine 198 by p90 Ribosomal Protein S6 Kinases Promotes Its Binding to 14-3-3 and Cytoplasmic Localization*

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• Reduction of 14-3-3 Proteins Correlates with Increased Sensitivity to Killing of Human Lung Cancer Cells by Ionizing Radiation

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• Two 14-3-3 binding motifs are required for stable association of Forkhead transcription factor FOXO4 with 14-3-3 proteins and inhibition of DNA binding.

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• Akt-dependent Phosphorylation of p27Kip1Promotes Binding to 14-3-3 and Cytoplasmic Localization*

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• A nonphosphorylated 14-3-3 binding motif on exoenzyme S that is functional in vivo.

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• PKB/Akt phosphorylates p27, impairs nuclear import of p27 and opposes p27-mediated G1 arrest

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• BRCA1 Is a Selective Co-activator of 14-3-3ς Gene Transcription in Mouse Embryonic Stem Cells* 210

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• BRCA1 is a selective co-activator of 14-3-3 sigma gene transcription in mouse embryonic stem cells.

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• Positive regulation of Wee1 by Chk1 and 14-3-3 proteins.

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• Cdc25B activity is regulated by 14-3-3

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• The G2/M regulator 14-3-3sigma prevents apoptosis through sequestration of Bax.

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• The G2/M Regulator 14-3-3ς Prevents Apoptosis through Sequestration of Bax*

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• 14-3-3 proteins; bringing new definitions to scaffolding

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• 14-3-3 Proteins Mediate an Essential Anti-apoptotic Signal*

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• Cell cycle roles for two 14-3-3 proteins during Drosophila development.

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• Substitutions that compromise the ionizing radiation-induced association of p53 with 14-3-3 proteins also compromise the ability of p53 to induce cell cycle arrest.

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  1999cited by this paper
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