Three different binding sites of Cks1 are required for p27-ubiquitin ligation - sprookjes - yvandenbroek - TriplyDB

Three different binding sites of Cks1 are required for p27-ubiquitin ligation

Three different binding sites of Cks1 are required for p27-ubiquitin ligation

http://www.wikidata.org/entity/Q28215946

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A negatively charged amino acid in Skp2 is required for Skp2-Cks1 interaction and ubiquitination of p27Kip1 Protein-protein interactions involved in the recognition of p27 by E3 ubiquitin ligase Specific small molecule inhibitors of Skp2-mediated p27 degradation Role of Cks1 overexpression in oral squamous cell carcinomas: cooperation with Skp2 in promoting p27 degradation Role of conformational heterogeneity in domain swapping and adapter function of the Cks proteins The SCF ubiquitin ligase: insights into a molecular machine Optimal ligand descriptor for pocket recognition based on the Beta-shape Information theoretical quantification of cooperativity in signalling complexes.CKS proteins protect mitochondrial genome integrity by interacting with mitochondrial single-stranded DNA-binding protein.High-throughput screening AlphaScreen assay for identification of small-molecule inhibitors of ubiquitin E3 ligase SCFSkp2-Cks1 Differentially expressed proteins identified in overexpressed let-7a gastric carcinoma cells by two-dimensional polyacrylamide gel electrophoresis.Regulation of neddylation and deneddylation of cullin1 in SCFSkp2 ubiquitin ligase by F-box protein and substrate Comprehensive analysis of loops at protein-protein interfaces for macrocycle design.Artemis interacts with the Cul4A-DDB1DDB2 ubiquitin E3 ligase and regulates degradation of the CDK inhibitor p27 Direct role for proliferating cell nuclear antigen in substrate recognition by the E3 ubiquitin ligase CRL4Cdt2.The ubiquitin system for protein degradation and some of its roles in the control of the cell division cycle.Clinical significance of overexpressed cyclin-dependent kinase subunits 1 and 2 in esophageal carcinoma Noncatalytic requirement for cyclin A-cdk2 in p27 turnover Cyclin-dependent kinase regulatory subunit 1 promotes cell proliferation by insulin regulation.TGF-β activates APC through Cdh1 binding for Cks1 and Skp2 proteasomal destruction stabilizing p27kip1 for normal endometrial growth.Loss of cks1 homeostasis deregulates cell division cycle.The CDK subunit CKS2 counteracts CKS1 to control cyclin A/CDK2 activity in maintaining replicative fidelity and neurodevelopment.Cks1: Structure, Emerging Roles and Implications in Multiple Cancers Flipping the switch from g1 to s phase with e3 ubiquitin ligases Direct interactions with both p27 and Cdk2 regulate Spy1-mediated proliferation in vivo and in vitro.Impact of siRNA targeting pirh2 on proliferation and cell cycle control of the lung adenocarcinoma cell line A549.The cyclin dependent kinase subunit Cks1 is required for infection-associated development of the rice blast fungus Magnaporthe oryzae.Skp2 contains a novel cyclin A binding domain that directly protects cyclin A from inhibition by p27Kip1.Negative regulation of SCFSkp2 ubiquitin ligase by TGF-beta signaling.COP9-Signalosome deneddylase activity is enhanced by simultaneous neddylation: insights into the regulation of an enzymatic protein complex.Molecular and biochemical characterization of the Skp2-Cks1 binding interface.Substrate recognition and ubiquitination of SCFSkp2/Cks1 ubiquitin-protein isopeptide ligase.Ubiquitination of p27Kip1 requires physical interaction with cyclin E and probable phosphate recognition by SKP2.

P2860

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P2860

Three different binding sites of Cks1 are required for p27-ubiquitin ligation

http://www.wikidata.org/entity/Q28215946

description

2002 nî lūn-bûn

@nan

2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Three different binding sites of Cks1 are required for p27-ubiquitin ligation

@ast

Three different binding sites of Cks1 are required for p27-ubiquitin ligation

@en

Three different binding sites of Cks1 are required for p27-ubiquitin ligation

@nl

type

label

Three different binding sites of Cks1 are required for p27-ubiquitin ligation

@ast

Three different binding sites of Cks1 are required for p27-ubiquitin ligation

@en

Three different binding sites of Cks1 are required for p27-ubiquitin ligation

@nl

prefLabel

Three different binding sites of Cks1 are required for p27-ubiquitin ligation

@ast

Three different binding sites of Cks1 are required for p27-ubiquitin ligation

@en

Three different binding sites of Cks1 are required for p27-ubiquitin ligation

@nl

P1433

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P1433

Journal of Biological Chemistry

P1476

Three different binding sites of Cks1 are required for p27-ubiquitin ligation

@en

P2093

Danielle Sitry

http://www.w3.org/2001/XMLSchema#string

Dvora Ganoth

http://www.w3.org/2001/XMLSchema#string

Laura S Itzhaki

http://www.w3.org/2001/XMLSchema#string

Sadie E Breward

http://www.w3.org/2001/XMLSchema#string

Tun K Ko

http://www.w3.org/2001/XMLSchema#string

P2860

Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex

Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex

p19Skp1 and p45Skp2 are essential elements of the cyclin A-CDK2 S phase kinase

Human CksHs2 atomic structure: a role for its hexameric assembly in cell cycle control

Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1

Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex

Association of human CUL-1 and ubiquitin-conjugating enzyme CDC34 with the F-box protein p45(SKP2): evidence for evolutionary conservation in the subunit composition of the CDC34-SCF pathway

Role of the F-box protein Skp2 in lymphomagenesis

Crystal structure and mutational analysis of the Saccharomyces cerevisiae cell cycle regulatory protein Cks1: implications for domain swapping, anion binding and protein interactions

Crystal structure of the human cell cycle protein CksHs1: single domain fold with similarity to kinase N-lobe domain

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42233-40

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scholarly article

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10.1074/JBC.M205254200

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P433

44

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P478

277

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P50

Markus A Seeliger

P577

2002-11-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

12140288

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