CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex
about
The NEDD8 modification pathway in plantsCullin-RING ubiquitin ligases: global regulation and activation cyclesAssociation of SAP130/SF3b-3 with Cullin-RING ubiquitin ligase complexes and its regulation by the COP9 signalosomeImpaired DNA damage checkpoint response in MIF-deficient miceCSN controls NF-kappaB by deubiquitinylation of IkappaBalphaProteolytic targeting of transcriptional regulator TIP120B by a HECT domain E3 ligaseA unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathwayThe conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiaeThe glomuvenous malformation protein Glomulin binds Rbx1 and regulates cullin RING ligase-mediated turnover of Fbw7Identification of FBXO25-interacting proteins using an integrated proteomics approachStructural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugationCOMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) bindingE2-RING expansion of the NEDD8 cascade confers specificity to cullin modificationSCCRO (DCUN1D1) is an essential component of the E3 complex for neddylationRegulation of Cullin-RING ubiquitin ligase 1 by Spliceosome-associated protein 130 (SAP130)Regulation of cullin RING E3 ubiquitin ligases by CAND1 in vivoArabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in multiple developmental pathways controlled by ubiquitin/proteasome-mediated protein DegradationControl of cell growth by the SCF and APC/C ubiquitin ligasesTargeted silencing of Jab1/Csn5 in human cells downregulates SCF activity through reduction of F-box protein levels.Cullin-RING ligases in regulation of autophagyBuilding and remodelling Cullin-RING E3 ubiquitin ligasesStructure of a Glomulin-RBX1-CUL1 Complex: Inhibition of a RING E3 Ligase through Masking of Its E2-Binding SurfaceN-Terminal Acetylation Acts as an Avidity Enhancer Within an Interconnected Multiprotein ComplexCullin neddylation and substrate-adaptors counteract SCF inhibition by the CAND1-like protein Lag2 in Saccharomyces cerevisiae.A longevity protein, Lag2, interacts with SCF complex and regulates SCF functionUbiquitylation, neddylation and the DNA damage responseFunction and regulation of cullin-RING ubiquitin ligasesDEN1 is a dual function protease capable of processing the C terminus of Nedd8 and deconjugating hyper-neddylated CUL1Substrate-mediated regulation of cullin neddylationNeurospora COP9 signalosome integrity plays major roles for hyphal growth, conidial development, and circadian functionTissue-specific expression of ALA synthase-1 and heme oxygenase-1 and their expression in livers of rats chronically exposed to ethanolDisruption of the COP9 signalosome Csn2 subunit in mice causes deficient cell proliferation, accumulation of p53 and cyclin E, and early embryonic deathOxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1Ubiquitin, hormones and biotic stress in plantsThe COP9 signalosome regulates the Neurospora circadian clock by controlling the stability of the SCFFWD-1 complexNovel Cul3 binding proteins function to remodel E3 ligase complexes.Nedd8 on cullin: building an expressway to protein destruction.Targeting Cullin-RING E3 ubiquitin ligases for drug discovery: structure, assembly and small-molecule modulation.COPing with hypoxia
P2860
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P2860
CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex
description
2002 nî lūn-bûn
@nan
2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի դեկտեմբերին 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
CAND1 binds to unneddylated CU ...... CF ubiquitin E3 ligase complex
@ast
CAND1 binds to unneddylated CU ...... CF ubiquitin E3 ligase complex
@en
CAND1 binds to unneddylated CU ...... CF ubiquitin E3 ligase complex
@en-gb
CAND1 binds to unneddylated CU ...... CF ubiquitin E3 ligase complex
@nl
type
label
CAND1 binds to unneddylated CU ...... CF ubiquitin E3 ligase complex
@ast
CAND1 binds to unneddylated CU ...... CF ubiquitin E3 ligase complex
@en
CAND1 binds to unneddylated CU ...... CF ubiquitin E3 ligase complex
@en-gb
CAND1 binds to unneddylated CU ...... CF ubiquitin E3 ligase complex
@nl
prefLabel
CAND1 binds to unneddylated CU ...... CF ubiquitin E3 ligase complex
@ast
CAND1 binds to unneddylated CU ...... CF ubiquitin E3 ligase complex
@en
CAND1 binds to unneddylated CU ...... CF ubiquitin E3 ligase complex
@en-gb
CAND1 binds to unneddylated CU ...... CF ubiquitin E3 ligase complex
@nl
P2093
P3181
P1433
P1476
CAND1 binds to unneddylated CU ...... CF ubiquitin E3 ligase complex
@en
P2093
Jennifer M Harrell
Jianyu Zheng
Karin Lykke-Andersen
Ryuji Kobayashi
Sophia Ryzhikov
Xiaoming Yang
P304
P3181
P356
10.1016/S1097-2765(02)00784-0
P407
P50
P577
2002-12-01T00:00:00Z