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extensive molecular analyses unveiled that wild-type TFIIH (show GTF2H4 Proteins) cooperated in an ATP-dependent manner with PGC1-alpha as well as with the deacetylase SIRT1 (show SIRT1 Proteins), thereby contributing to the PGC1-a deacetylation by SIRT1 (show SIRT1 Proteins)
Mutations in TFIIH (show GTF2H4 Proteins) causing trichothiodystrophy are responsible for defects in ribosomal RNA production and processing.
Data show that that B2 RNA, when present with Pol II in promoter-bound complexes, specifically represses CTD phosphorylation by TFIIH (show GTF2H4 Proteins).
Molecular analyses performed on the mice brain tissue demonstrate that TFIIH (show GTF2H4 Proteins) is required for the stabilization of thyroid hormone (show PTH Proteins) receptors (TR) to their DNA-responsive elements.
interface variants between the p34 (show CCNH Proteins) and p44 (show GTF2H2 Proteins) subunits only mildly affected the association between the full length proteins and did not impinge on TFIIH (show GTF2H1 Proteins) activities due to the presence of an additional interface involving the C4 domain of p34 (show CCNH Proteins).
This gene encodes a member of the TFB4 family. The encoded protein is a subunit of the core-TFIIH basal transcription factor and localizes to the nucleus. The encoded protein is involved in RNA transcription by RNA polymerase II and nucleotide excision repair and associates with the Cdk-activating kinase complex. Alternative splicing results in multiple transcript variants. A related pseudogene has been identified on chromosome 14.
general transcription factor IIH subunit 3
, TFIIH basal transcription factor complex p34 subunit
, basic transcription factor 2 34 kDa subunit
, general transcription factor IIH, polypeptide 3, 34kDa
, general transcription factor IIH polypeptide 3