Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
about
VHL type 2B mutations retain VBC complex form and functionIdentification and characterization of Elongin A2, a new member of the Elongin family of transcription elongation factors, specifically expressed in the testisTracheal development and the von Hippel-Lindau tumor suppressor homolog in DrosophilaRegulation of STRA13 by the von Hippel-Lindau tumor suppressor protein, hypoxia, and the UBC9/ubiquitin proteasome degradation pathwayTIP120A associates with cullins and modulates ubiquitin ligase activityRegulation of receptor for activated C kinase 1 protein by the von Hippel-Lindau tumor suppressor in IGF-I-induced renal carcinoma cell invasivenessThe von Hippel-Lindau tumor suppressor stabilizes novel plant homeodomain protein Jade-1Nuclear receptor binding protein 1 regulates intestinal progenitor cell homeostasis and tumour formationVHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligasesInhibition of transcription elongation by the VHL tumor suppressor proteinAn intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammalian cells.Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2Ankyrin repeat and SOCS box 3 (ASB3) mediates ubiquitination and degradation of tumor necrosis factor receptor IITranscription-dependent nuclear-cytoplasmic trafficking is required for the function of the von Hippel-Lindau tumor suppressor proteinRegulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1.Analysis of the adenovirus E1B-55K-anchored proteome reveals its link to ubiquitination machinery.von Hippel-Lindau protein binds hyperphosphorylated large subunit of RNA polymerase II through a proline hydroxylation motif and targets it for ubiquitinationSynthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau proteinThe von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteinsHECT and RING finger families of E3 ubiquitin ligases at a glanceMetabolism of kidney cancer: from the lab to clinical practiceIdentification of Ror2 as a hypoxia-inducible factor target in von Hippel-Lindau-associated renal cell carcinomaThe VHL tumor suppressor: master regulator of HIFDown-regulation of transmembrane carbonic anhydrases in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgenesThe conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradationIdentification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complexActivation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complexStudying interactions of four proteins in the yeast two-hybrid system: structural resemblance of the pVHL/elongin BC/hCUL-2 complex with the ubiquitin ligase complex SKP1/cullin/F-box proteinConjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau tumor suppressor functionpVHL acts as an adaptor to promote the inhibitory phosphorylation of the NF-kappaB agonist Card9 by CK2WSB1: from homeostasis to hypoxiaThe structure and regulation of Cullin 2 based E3 ubiquitin ligases and their biological functionsContribution of the Type II Chaperonin, TRiC/CCT, to OncogenesisOxygen sensing in retinal health and diseaseRINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesisMechanisms of chemical carcinogenesis in the kidneysThe metabolic basis of kidney cancerComputational and experimental characterization of dVHL establish a Drosophila model of VHL syndromeRequirement of ELC1 for RNA polymerase II polyubiquitylation and degradation in response to DNA damage in Saccharomyces cerevisiaeBinding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C
P2860
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P2860
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
description
1995 nî lūn-bûn
@nan
1995 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
@ast
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
@en
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
@en-gb
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
@nl
type
label
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
@ast
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
@en
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
@en-gb
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
@nl
prefLabel
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
@ast
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
@en
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
@en-gb
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
@nl
P2093
P2860
P3181
P356
P1433
P1476
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
@en
P2093
J A DeCaprio
O Iliopoulos
P2860
P304
P3181
P356
10.1126/SCIENCE.7660130
P407
P577
1995-09-08T00:00:00Z