Functional Interaction of the Auxilin J Domain with the Nucleotide- and Substrate-binding Modules of Hsc70
Authors:
Open Access
- 1 August 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (31) , 19594-19600
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Interaction of Auxilin with the Molecular Chaperone, Hsc70Journal of Biological Chemistry, 1997
- Mechanism of clathrin basket dissociation: separate functions of protein domains of the DnaJ homologue auxilin.Journal of Cell Biology, 1996
- NMR Structure of the J-domain and the Gly/Phe-rich Region of theEscherichia coliDnaJ ChaperoneJournal of Molecular Biology, 1996
- Nuclear Magnetic Resonance Solution Structure of the Human Hsp40 (HDJ-1) J-domainJournal of Molecular Biology, 1996
- Solution small-angle x-ray scattering study of the molecular chaperone Hsc70 and its subfragmentsBiochemistry, 1995
- Kinetics of Nucleotide-Induced Changes in the Tryptophan Fluorescence of the Molecular Chaperone Hsc70 and Its Subfragments Suggest the ATP-Induced Conformational Change Follows Initial ATP BindingBiochemistry, 1995
- Primary Structure of the Neuronal Clathrin-Associated Protein Auxilin and its Expression in BacteriaEuropean Journal of Biochemistry, 1995
- Effect of Nucleotide on the Binding of Peptides to 70-kDa Heat Shock ProteinJournal of Biological Chemistry, 1995
- Purification of Golgi adaptor protein 1 from bovine adrenal gland and characterization of its β1 (β′) subunit by microsequencingEuropean Journal of Biochemistry, 1994
- Dissociation of clathrin coats coupled to the hydrolysis of ATP: role of an uncoating ATPase.Journal of Cell Biology, 1984