XPD Mutations Prevent TFIIH-Dependent Transactivation by Nuclear Receptors and Phosphorylation of RARα
- 1 April 2002
- Vol. 109 (1) , 125-135
- https://doi.org/10.1016/s0092-8674(02)00692-x
Abstract
No abstract availableKeywords
This publication has 52 references indexed in Scilit:
- Nuclear receptors coordinate the activities of chromatin remodeling complexes and coactivators to facilitate initiation of transcriptionOncogene, 2001
- TFIIH Interacts with the Retinoic Acid Receptor γ and Phosphorylates Its AF-1-activating Domain through cdk7Journal of Biological Chemistry, 2000
- Activation of Estrogen Receptor ? by S118 Phosphorylation Involves a Ligand-Dependent Interaction with TFIIH and Participation of CDK7Molecular Cell, 2000
- Nucleotide excision repair and human syndromesCarcinogenesis: Integrative Cancer Research, 2000
- Crystal Structure of a Heterodimeric Complex of RAR and RXR Ligand-Binding DomainsMolecular Cell, 2000
- Serine 157, a Retinoic Acid Receptor α Residue Phosphorylated by Protein Kinase C in Vitro, Is Involved in RXR·RARα Heterodimerization and Transcriptional ActivityJournal of Biological Chemistry, 1999
- Mutations in XPB and XPD helicases found in xeroderma pigmentosum patients impair the transcription function of TFIIHThe EMBO Journal, 1999
- Phosphorylation of Human Estrogen Receptor α by Protein Kinase A Regulates DimerizationMolecular and Cellular Biology, 1999
- Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIHNature Genetics, 1998
- Reversible Phosphorylation of the C-terminal Domain of RNA Polymerase IIJournal of Biological Chemistry, 1996