ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
about
Cullin-RING ubiquitin ligases: global regulation and activation cyclesThe western painted turtle genome, a model for the evolution of extreme physiological adaptations in a slowly evolving lineage.ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanismThe role of cullin 5-containing ubiquitin ligasesGenetically engineered mouse models for functional studies of SKP1-CUL1-F-box-protein (SCF) E3 ubiquitin ligasesMolecular Architecture of the Ankyrin SOCS Box Family of Cul5-Dependent E3 Ubiquitin LigasesMultimeric Complexes among Ankyrin-Repeat and SOCS-box Protein 9 (ASB9), ElonginBC, and Cullin 5: Insights into the Structure and Assembly of ECS-type Cullin-RING E3 Ubiquitin LigasesThe SOCS2 ubiquitin ligase complex regulates growth hormone receptor levelsSAG/RBX2 E3 ligase complexes with UBCH10 and UBE2S E2s to ubiquitylate β-TrCP1 via K11-linkage for degradationASB9 interacts with ubiquitous mitochondrial creatine kinase and inhibits mitochondrial functionExpression of ankyrin repeat and suppressor of cytokine signaling box protein 4 (Asb-4) in proopiomelanocortin neurons of the arcuate nucleus of mice produces a hyperphagic, lean phenotypeEssential role for the d-Asb11 cul5 Box domain for proper notch signaling and neural cell fate decisions in vivo.Filamins in mechanosensing and signaling.Ankyrin repeat and SOCS box containing protein 4 (Asb-4) colocalizes with insulin receptor substrate 4 (IRS4) in the hypothalamic neurons and mediates IRS4 degradationGene expression profiling in gastric mucosa from Helicobacter pylori-infected and uninfected patients undergoing chronic superficial gastritisRefined mapping of a quantitative trait locus on chromosome 1 responsible for mouse embryonic death.Filamins but not Janus kinases are substrates of the ASB2α cullin-ring E3 ubiquitin ligase in hematopoietic cells.Cullin E3 ligases and their rewiring by viral factorsThe ubiquitin ligase ASB4 promotes trophoblast differentiation through the degradation of ID2The E3 ubiquitin ligase specificity subunit ASB2α targets filamins for proteasomal degradation by interacting with the filamin actin-binding domainHow the ankyrin and SOCS box protein, ASB9, binds to creatine kinaseECSASB2 mediates MLL degradation during hematopoietic differentiationPositional plasticity in regenerating Amybstoma mexicanum limbs is associated with cell proliferation and pathways of cellular differentiation.ASB2 targets filamins A and B to proteasomal degradation.Ankyrin repeat and suppressor of cytokine signaling box containing protein-10 is associated with ubiquitin-mediated degradation pathways in trabecular meshwork cells.ASB2α, an E3 ubiquitin ligase specificity subunit, regulates cell spreading and triggers proteasomal degradation of filamins by targeting the filamin calponin homology 1 domainA Genome-Wide Association Meta-Analysis of Attention-Deficit/Hyperactivity Disorder Symptoms in Population-Based Pediatric Cohorts.Conserved principles of mammalian transcriptional regulation revealed by RNA half-lifeThe loss-of-function mutations and down-regulated expression of ASB3 gene promote the growth and metastasis of colorectal cancer cells.The SOCS box-adapting proteins for ubiquitination and proteasomal degradation.Functional characterization of SAG/RBX2/ROC2/RNF7, an antioxidant protein and an E3 ubiquitin ligase.Cutting Edge: A Cullin-5-TRAF6 Interaction Promotes TRAF6 Polyubiquitination and Lipopolysaccharide Signaling.Working your SOCS off: The role of ASB10 and protein degradation pathways in glaucoma.ASB7 regulates spindle dynamics and genome integrity by targeting DDA3 for proteasomal degradation.A label-free quantitative proteomics strategy to identify E3 ubiquitin ligase substrates targeted to proteasome degradation.asb11 is a regulator of embryonic and adult regenerative myogenesis.Protein interaction screening for the ankyrin repeats and suppressor of cytokine signaling (SOCS) box (ASB) family identify Asb11 as a novel endoplasmic reticulum resident ubiquitin ligase.Model of the Ankyrin and SOCS Box Protein, ASB9, E3 Ligase Reveals a Mechanism for Dynamic Ubiquitin Transfer.Notch-induced Asb2 expression promotes protein ubiquitination by forming non-canonical E3 ligase complexes.Osteopathia striata congenita with cranial sclerosis and intellectual disability due to contiguous gene deletions involving the WTX locus.
P2860
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P248
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P2860
ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
description
2005 nî lūn-bûn
@nan
2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
@ast
ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
@en
ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
@en-gb
ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
@nl
type
label
ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
@ast
ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
@en
ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
@en-gb
ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
@nl
prefLabel
ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
@ast
ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
@en
ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
@en-gb
ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
@nl
P2093
P2860
P921
P1433
P1476
ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
@en
P2093
Junya Kohroki
Takaaki Nakamura
Takehiro Nishiyama
Yasuhiko Masuho
P2860
P304
P356
10.1016/J.FEBSLET.2005.11.016
P407
P577
2005-12-19T00:00:00Z