Dimerization of the Human E3 Ligase CHIP via a Coiled-coil Domain Is Essential for Its Activity
Open Access
- 1 January 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (4) , 2673-2678
- https://doi.org/10.1074/jbc.m311112200
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- AtCHIP, a U-Box-Containing E3 Ubiquitin Ligase, Plays a Critical Role in Temperature Stress Tolerance in ArabidopsisPlant Physiology, 2003
- Protein quality control: U-box-containing E3 ubiquitin ligases join the foldTrends in Biochemical Sciences, 2002
- CHIP Is a U-box-dependent E3 Ubiquitin LigaseJournal of Biological Chemistry, 2001
- U Box Proteins as a New Family of Ubiquitin-Protein LigasesJournal of Biological Chemistry, 2001
- Folding of Newly Translated Proteins In Vivo: The Role of Molecular ChaperonesAnnual Review of Biochemistry, 2001
- Coiled coils: a highly versatile protein folding motifTrends in Cell Biology, 2001
- The RING Heterodimer BRCA1-BARD1 Is a Ubiquitin Ligase Inactivated by a Breast Cancer-derived MutationJournal of Biological Chemistry, 2001
- Structure of TPR Domain–Peptide ComplexesCell, 2000
- Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometryNature, 1996
- Predicting Coiled Coils from Protein SequencesScience, 1991