Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins. - sprookjes - yvandenbroek - TriplyDB

Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins.

Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins.

http://www.wikidata.org/entity/Q36850952

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The NEDD8 modification pathway in plants Regulation of Cullin-RING ubiquitin ligase 1 by Spliceosome-associated protein 130 (SAP130)TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes The Role of the COP9 Signalosome and Neddylation in DNA Damage Signaling and Repair Building and remodelling Cullin-RING E3 ubiquitin ligases Cullin-RING ubiquitin E3 ligase regulation by the COP9 signalosome Poxviral ankyrin proteins Ubiquitylation, neddylation and the DNA damage response Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation A Trichomonas vaginalis Rhomboid Protease and Its Substrate Modulate Parasite Attachment and Cytolysis of Host Cells Distinct outcomes of CRL-Nedd8 pathway inhibition reveal cancer cell plasticity Ribosomal proteins produced in excess are degraded by the ubiquitin-proteasome system Control of plant stem cell function by conserved interacting transcriptional regulators.A Mighty "Protein Extractor" of the Cell: Structure and Function of the p97/CDC48 ATPase.Degradation of the deubiquitinating enzyme USP33 is mediated by p97 and the ubiquitin ligase HERC2.Protein neddylation: beyond cullin-RING ligases.Targeting Cullin-RING E3 ubiquitin ligases for drug discovery: structure, assembly and small-molecule modulation.Composition, roles, and regulation of cullin-based ubiquitin e3 ligases.Cullin E3 ligases and their rewiring by viral factors Glycosylation of Skp1 promotes formation of Skp1-cullin-1-F-box protein complexes in dictyostelium.Caspase-1 promotes Epstein-Barr virus replication by targeting the large tegument protein deneddylase to the nucleus of productively infected cells.The COP9 signalosome and cullin-RING ligases in the heart The COP9 signalosome is vital for timely repair of DNA double-strand breaks.Skp1 Independent Function of Cdc53/Cul1 in F-box Protein Homeostasis Inhibition of SCF ubiquitin ligases by engineered ubiquitin variants that target the Cul1 binding site on the Skp1-F-box interface.Characterisation of the Cullin-3 mutation that causes a severe form of familial hypertension and hyperkalaemia.The pineal gland: A model for adrenergic modulation of ubiquitin ligases JNK-associated Leucine Zipper Protein Functions as a Docking Platform for Polo-like Kinase 1 and Regulation of the Associating Transcription Factor Forkhead Box Protein K1.HSP90 regulates temperature-dependent seedling growth in Arabidopsis by stabilizing the auxin co-receptor F-box protein TIR1.Time-resolved proteomic analysis of quorum sensing in Vibrio harveyi.Structural and kinetic analysis of the COP9-Signalosome activation and the cullin-RING ubiquitin ligase deneddylation cycle.The emerging family of CULLIN3-RING ubiquitin ligases (CRL3s): cellular functions and disease implications.Beyond ubiquitination: the atypical functions of Fbxo7 and other F-box proteins.Substrate binding promotes formation of the Skp1-Cul1-Fbxl3 (SCF(Fbxl3)) protein complex Mechanisms and function of substrate recruitment by F-box proteins.Regulation of the MEI-1/MEI-2 Microtubule-Severing Katanin Complex in Early Caenorhabditis elegans Development.Targeted inhibition of the COP9 signalosome for treatment of cancer ZRF1 mediates remodeling of E3 ligases at DNA lesion sites during nucleotide excision repair.CUL4A ubiquitin ligase: a promising drug target for cancer and other human diseases A snapshot of ubiquitin chain elongation: lysine 48-tetra-ubiquitin slows down ubiquitination.

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P2860

Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins.

http://www.wikidata.org/entity/Q36850952

description

2013 nî lūn-bûn

@nan

2013年の論文

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2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

2013年论文

@zh

2013年论文

@zh-cn

name

Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins.

@en

type

label

Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins.

@en

prefLabel

Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins.

@en

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J.CELL.2013.02.024

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P1476

Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins.

@en

P2093

Bruce E Clurman

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

Elizabeth A Larimore

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

J Eugene Lee

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

Michael J Sweredoski

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

Michael Rome

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

Nathan W Pierce

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

Ning Zheng

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

Raymond J Deshaies

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

Robert L J Graham

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

Shu-ou Shan

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

P2860

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

SCFFbxl3 controls the oscillation of the circadian clock by directing the degradation of cryptochrome proteins

Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases

Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation

NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases

CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex

Regulation of cullin RING E3 ubiquitin ligases by CAND1 in vivo

Recognition of the polyubiquitin proteolytic signal

Arabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in multiple developmental pathways controlled by ubiquitin/proteasome-mediated protein Degradation

K11-linked ubiquitin chains as novel regulators of cell division

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206-215

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scholarly article

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10.1016/J.CELL.2013.02.024

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1

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3656483

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