The hexamerization domain of N-ethylmaleimide-sensitive factor: structural clues to chaperone function
- 15 February 1999
- Vol. 7 (2) , R19-R23
- https://doi.org/10.1016/s0969-2126(99)80015-x
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATPNature Structural & Molecular Biology, 1998
- The AAA team: related ATPases with diverse functionsTrends in Cell Biology, 1998
- Crystal Structure of the δ′ Subunit of the Clamp-Loader Complex of E. coli DNA Polymerase IIICell, 1997
- DnaA initiator—also a transcription factorMolecular Microbiology, 1997
- Protein quality control: triage by chaperones and proteases.Genes & Development, 1997
- Unusual Oligomerization Required for Activity of NtrC, a Bacterial Enhancer-Binding ProteinScience, 1997
- Promotion of Mitochondrial Membrane Complex Assembly by a Proteolytically Inactive Yeast LonScience, 1996
- The mechanism of Rubisco activase: Insights from studies of the properties and structure of the enzymePhotosynthesis Research, 1996
- Rubisco Activase, a Possible New Member of the Molecular Chaperone FamilyBiochemistry, 1995
- The P-loop — a common motif in ATP- and GTP-binding proteinsTrends in Biochemical Sciences, 1990