Crystal Structure of the E2 Transactivation Domain of Human Papillomavirus Type 11 Bound to a Protein Interaction Inhibitor-Reference-Cited by-同舟云学术

Crystal Structure of the E2 Transactivation Domain of Human Papillomavirus Type 11 Bound to a Protein Interaction Inhibitor

Published:2004-02 Issue:8 Volume:279 Page:6976-6985
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Wang Yong,Coulombe René,Cameron Dale R.,Thauvette Louise,Massariol Marie-Josée,Amon Lynn M.,Fink Dominique,Titolo Steve,Welchner Ewald,Yoakim Christiane,Archambault Jacques,White Peter W.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference49 articles.

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2. Functional Interaction of the Bovine Papillomavirus E2 Transactivation Domain with TFIIB

3. Conserved interaction of the papillomavirus E2 transcriptional activator proteins with human and yeast TFIIB proteins

4. Bovine papillomavirus type 1 E2 transcriptional regulators directly bind two cellular transcription factors, TFIID and TFIIB

5. Direct interaction between Sp1 and the BPV enhancer E2 protein mediates synergistic activation of transcription

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