An Accessible Hydrophobic Surface Is a Key Element of the Molecular Chaperone Action of Atp11p
Open Access
- 1 October 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (43) , 39945-39949
- https://doi.org/10.1074/jbc.m107252200
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Atp11p and Atp12p Are Assembly Factors for the F1-ATPase in Human MitochondriaJournal of Biological Chemistry, 2001
- Domain Swapping in Human αA and αB Crystallins Affects Oligomerization and Enhances Chaperone-like ActivityJournal of Biological Chemistry, 2000
- A Thermodynamic Coupling Mechanism for the Disaggregation of a Model Peptide Substrate by Chaperone SecBJournal of Biological Chemistry, 2000
- The Assembly Factor Atp11p Binds to the β-Subunit of the Mitochondrial F1-ATPaseJournal of Biological Chemistry, 2000
- Interaction of 1,1′-Bi(4-anilino)naphthalene-5,5′-Disulfonic Acid with α-CrystallinJournal of Biological Chemistry, 1998
- Identification of Functional Domains in Atp11pJournal of Biological Chemistry, 1996
- Temperature‐induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α‐crystallinFEBS Letters, 1995
- Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondriaNature, 1994
- Protein Conformational Changes Induced by 1,1'-Bis(4-anilino-5-naphthalenesulfonic acid): Preferential Binding to the Molten Globule of DnaKBiochemistry, 1994
- Preparation, crystalline structure, and spectral properties of the fluorescent probe 4,4'-bis-1-phenylamino-8-naphthalenesulfonateJournal of the American Chemical Society, 1978