Inhibition of transcription elongation by the VHL tumor suppressor protein
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 testisTIP120A associates with cullins and modulates ubiquitin ligase activityThe 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 ligasesElongin (SIII): a multisubunit regulator of elongation by RNA polymerase IIBinding of the von Hippel-Lindau tumor suppressor protein to Elongin B and CRegulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2Transcription-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 proteinsDown-regulation of transmembrane carbonic anhydrases in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgenesIdentification of Jade1, a gene encoding a PHD zinc finger protein, in a gene trap mutagenesis screen for genes involved in anteroposterior axis developmentThe 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 functionThe structure and regulation of Cullin 2 based E3 ubiquitin ligases and their biological functionsContribution of the Type II Chaperonin, TRiC/CCT, to OncogenesisThe metabolic basis of kidney cancerComputational and experimental characterization of dVHL establish a Drosophila model of VHL syndromeStructural basis of intersubunit recognition in elongin BC-cullin 5-SOCS box ubiquitin-protein ligase complexesRequirement 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 CElongin from Saccharomyces cerevisiae.ELL2, a new member of an ELL family of RNA polymerase II elongation factorsPhysical interaction and functional antagonism between the RNA polymerase II elongation factor ELL and p53Identification and biochemical characterization of a novel transcription elongation factor, Elongin A3Structure and function of RNA polymerase II elongation factor ELL. Identification of two overlapping ELL functional domains that govern its interaction with polymerase and the ternary elongation complexInteraction of elongation factors TFIIS and elongin A with a human RNA polymerase II holoenzyme capable of promoter-specific initiation and responsive to transcriptional activatorsHaemangioblastoma of the central nervous system in von Hippel-Lindau disease. French VHL Study GroupThe inducible elongin A elongation activation domain: structure, function and interaction with the elongin BC complexpVHL function is essential for endothelial extracellular matrix deposition.Inactivation of the arylhydrocarbon receptor nuclear translocator (Arnt) suppresses von Hippel-Lindau disease-associated vascular tumors in mice.CUL-4A is critical for early embryonic development
P2860
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P2860
Inhibition of transcription elongation by the VHL tumor suppressor protein
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
Inhibition of transcription elongation by the VHL tumor suppressor protein
@ast
Inhibition of transcription elongation by the VHL tumor suppressor protein
@en
Inhibition of transcription elongation by the VHL tumor suppressor protein
@en-gb
Inhibition of transcription elongation by the VHL tumor suppressor protein
@nl
type
label
Inhibition of transcription elongation by the VHL tumor suppressor protein
@ast
Inhibition of transcription elongation by the VHL tumor suppressor protein
@en
Inhibition of transcription elongation by the VHL tumor suppressor protein
@en-gb
Inhibition of transcription elongation by the VHL tumor suppressor protein
@nl
prefLabel
Inhibition of transcription elongation by the VHL tumor suppressor protein
@ast
Inhibition of transcription elongation by the VHL tumor suppressor protein
@en
Inhibition of transcription elongation by the VHL tumor suppressor protein
@en-gb
Inhibition of transcription elongation by the VHL tumor suppressor protein
@nl
P2093
P2860
P3181
P356
P1433
P1476
Inhibition of transcription elongation by the VHL tumor suppressor protein
@en
P2093
J W Conaway
K P Garrett
R C Conaway
R D Klausner
W H Burgess
W M Linehan
P2860
P304
P3181
P356
10.1126/SCIENCE.7660122
P407
P577
1995-09-08T00:00:00Z