Fbw7/hCDC4 dimerization regulates its substrate interactions - Wikidata - wikimedia - TriplyDB

Fbw7/hCDC4 dimerization regulates its substrate interactions

Fbw7/hCDC4 dimerization regulates its substrate interactions

http://www.wikidata.org/entity/Q35647016

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The F-box protein Cdc4/Fbxw7 is a novel regulator of neural crest development in Xenopus laevis Cullin-RING ubiquitin ligases: global regulation and activation cycles Acetylation-dependent regulation of Skp2 function The ubiquitin ligase FBXW7 modulates leukemia-initiating cell activity by regulating MYC stability Structural basis of dimerization-dependent ubiquitination by the SCF(Fbx4) ubiquitin ligase Presenilin modulates EGFR signaling and cell transformation by regulating the ubiquitin ligase Fbw7 Parkin-dependent degradation of the F-box protein Fbw7β promotes neuronal survival in response to oxidative stress by stabilizing Mcl-1 Phosphorylation-dependent regulation of SCF(Fbx4) dimerization and activity involves a novel component, 14-3-3ɛ Isoform- and cell cycle-dependent substrate degradation by the Fbw7 ubiquitin ligase Fbxw7 Tumor Suppressor: A Vital Regulator Contributes to Human Tumorigenesis Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases Structure of the FP domain of Fbxo7 reveals a novel mode of protein-protein interaction The FP domains of PI31 and Fbxo7 have the same protein fold but very different modes of protein-protein interaction Sequential primed kinases create a damage-responsive phosphodegron on Eco1.FBW7 regulates endothelial functions by targeting KLF2 for ubiquitination and degradation FBXW7 mutations typically found in human cancers are distinct from null alleles and disrupt lung development An allosteric conduit facilitates dynamic multisite substrate recognition by the SCF(Cdc4) ubiquitin ligase Cell cycle-specific UNG2 phosphorylations regulate protein turnover, activity and association with RPA.FBXW7 missense mutation: a novel negative prognostic factor in metastatic colorectal adenocarcinoma.The Fbw7/human CDC4 tumor suppressor targets proproliferative factor KLF5 for ubiquitination and degradation through multiple phosphodegron motifs.SCF(FBXW7α) modulates the intra-S-phase DNA-damage checkpoint by regulating Polo like kinase-1 stability Transfer of Ho endonuclease and Ufo1 to the proteasome by the UbL-UbA shuttle protein, Ddi1, analysed by complex formation in vitro.Merkel cell polyomavirus small T antigen controls viral replication and oncoprotein expression by targeting the cellular ubiquitin ligase SCFFbw7.Tumor suppression by the Fbw7 ubiquitin ligase: mechanisms and opportunities.Structural assembly of cullin-RING ubiquitin ligase complexes.The Cullin-RING E3 ubiquitin ligase CRL4-DCAF1 complex dimerizes via a short helical region in DCAF1.MYC, FBXW7 and TP53 copy number variation and expression in gastric cancer.Roles of F-box proteins in cancer Proteomic screen reveals Fbw7 as a modulator of the NF-κB pathway.Cdh1 regulates osteoblast function through an APC/C-independent modulation of Smurf1.The Fbw7 and betaTRCP E3 ubiquitin ligases and their roles in tumorigenesis.Negative regulation of the stability and tumor suppressor function of Fbw7 by the Pin1 prolyl isomerase.FBW7 mutations in leukemic cells mediate NOTCH pathway activation and resistance to gamma-secretase inhibitors Stringent Control of NFE2L3 (Nuclear Factor, Erythroid 2-Like 3; NRF3) Protein Degradation by FBW7 (F-box/WD Repeat-containing Protein 7) and Glycogen Synthase Kinase 3 (GSK3).Multiple Weak Linear Motifs Enhance Recruitment and Processivity in SPOP-Mediated Substrate Ubiquitination.The ubiquitous nature of cancer: the role of the SCF(Fbw7) complex in development and transformation Mutations in Fbx4 inhibit dimerization of the SCF(Fbx4) ligase and contribute to cyclin D1 overexpression in human cancer.Substrate binding promotes formation of the Skp1-Cul1-Fbxl3 (SCF(Fbxl3)) protein complex Mechanisms and function of substrate recruitment by F-box proteins.Fbw7 dimerization determines the specificity and robustness of substrate degradation.

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Fbw7/hCDC4 dimerization regulates its substrate interactions

http://www.wikidata.org/entity/Q35647016

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2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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2007年论文

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name

Fbw7/hCDC4 dimerization regulates its substrate interactions

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Fbw7/hCDC4 dimerization regulates its substrate interactions

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Fbw7/hCDC4 dimerization regulates its substrate interactions

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Fbw7/hCDC4 dimerization regulates its substrate interactions

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Fbw7/hCDC4 dimerization regulates its substrate interactions

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Fbw7/hCDC4 dimerization regulates its substrate interactions

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Fbw7/hCDC4 dimerization regulates its substrate interactions

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Bruce E Clurman

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P2860

Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7

Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E

Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase

Distinct mechanisms control the stability of the related S-phase cyclins Clb5 and Clb6.

Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds to IkappaBalpha for signal-dependent ubiquitination

Archipelago regulates Cyclin E levels in Drosophila and is mutated in human cancer cell lines

Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line

Multisite phosphorylation by Cdk2 and GSK3 controls cyclin E degradation

Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication

Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase

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7

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scholarly article

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10.1186/1747-1028-2-7

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2

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2007-02-13T00:00:00Z

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6506078

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1052023948

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17298674

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1802738

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