Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog
about
A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2Identification and characterization of Elongin A2, a new member of the Elongin family of transcription elongation factors, specifically expressed in the testisMammalian mediator subunit mMED8 is an Elongin BC-interacting protein that can assemble with Cul2 and Rbx1 to reconstitute a ubiquitin ligase.Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1VHL-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 proteinElongin (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 Cul2Analysis of the adenovirus E1B-55K-anchored proteome reveals its link to ubiquitination machinery.Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau proteinThe HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factorUV-induced ubiquitination of RNA polymerase II: a novel modification deficient in Cockayne syndrome cellsThe conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradationActivation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complexThe structure and regulation of Cullin 2 based E3 ubiquitin ligases and their biological functionsThe rub family of ubiquitin-like proteins. Crystal structure of Arabidopsis rub1 and expression of multiple rubs in ArabidopsisIntegrated molecular analysis of clear-cell renal cell carcinoma.Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin CElongin from Saccharomyces cerevisiae.The ubiquitin-homology protein, DAP-1, associates with tumor necrosis factor receptor (p60) death domain and induces apoptosisIdentification and biochemical characterization of a novel transcription elongation factor, Elongin A3The inducible elongin A elongation activation domain: structure, function and interaction with the elongin BC complexdELL, a drosophila homologue of transcription elongation factor ELL (Eleven-nineteen Lysine rich Leukemia), is required for early development.Protective function of von Hippel-Lindau protein against impaired protein processing in renal carcinoma cellsGene expression profiling in gastric mucosa from Helicobacter pylori-infected and uninfected patients undergoing chronic superficial gastritisThe von Hippel-Lindau tumor suppressor protein is a component of an E3 ubiquitin-protein ligase activity.The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat familiesAssembly of the Elongin A Ubiquitin Ligase Is Regulated by Genotoxic and Other StressesThe Role of Elongin BC-Containing Ubiquitin Ligases.The Ubp6 family of deubiquitinating enzymes contains a ubiquitin-like domain: SUb.Interactions between HIV-1 Vif and human ElonginB-ElonginC are important for CBF-β binding to Vif.Proteasome-mediated processing of Def1, a critical step in the cellular response to transcription stressTranscription syndromes and the role of RNA polymerase II general transcription factors in human disease.In vivo requirement of the RNA polymerase II elongation factor elongin A for proper gene expression and development.Nuclear/cytoplasmic localization of the von Hippel-Lindau tumor suppressor gene product is determined by cell density.Interleukin-6: a multifunctional targetable cytokine in human prostate cancer.Cockayne syndrome B protein regulates recruitment of the Elongin A ubiquitin ligase to sites of DNA damage.Mammalian Elongin A complex mediates DNA-damage-induced ubiquitylation and degradation of Rpb1.The von Hippel-Lindau tumor suppressor gene product promotes, but is not essential for, NEDD8 conjugation to cullin-2.
P2860
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P2860
Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog
description
1995 nî lūn-bûn
@nan
1995 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի օգոստոսին 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
Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog
@ast
Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog
@en
Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog
@nl
type
label
Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog
@ast
Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog
@en
Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog
@nl
prefLabel
Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog
@ast
Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog
@en
Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog
@nl
P2093
P2860
P3181
P356
P1476
Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog
@en
P2093
J N Bradsher
J W Conaway
K P Garrett
R C Conaway
S I Foundling
P2860
P304
P3181
P356
10.1073/PNAS.92.16.7172
P407
P577
1995-08-01T00:00:00Z