The association of small heat shock protein Hsp16.3 with the plasma membrane of Mycobacterium tuberculosis: Dissociation of oligomers is a prerequisite
- 1 May 2005
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 330 (4) , 1055-1061
- https://doi.org/10.1016/j.bbrc.2005.03.092
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- A Dual Role for the N-terminal Region of Mycobacterium tuberculosis Hsp16.3 in Self-oligomerization and Binding Denaturing Substrate ProteinsJournal of Biological Chemistry, 2005
- Truncated hemoglobin o of Mycobacterium tuberculosis: the oligomeric state change and the interaction with membrane componentsBiochemical and Biophysical Research Communications, 2004
- Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosisBiochemical and Biophysical Research Communications, 2004
- Mycobacterium tuberculosisPhagosome Maturation Arrest: Mycobacterial Phosphatidylinositol Analog Phosphatidylinositol Mannoside Stimulates Early Endosomal FusionMolecular Biology of the Cell, 2004
- Subunit Exchange, Conformational Stability, and Chaperone-like Function of the Small Heat Shock Protein 16.5 fromMethanococcus jannaschiiJournal of Biological Chemistry, 2002
- Monodisperse Hsp16.3 Nonamer Exhibits Dynamic Dissociation and Reassociation, with the Nonamer Dissociation Prerequisite for Chaperone-like ActivityJournal of Molecular Biology, 2002
- Association of HSPB2, a Member of the Small Heat Shock Protein Family, with MitochondriaExperimental Cell Research, 2001
- Immunology of TuberculosisAnnual Review of Immunology, 2001
- The Dynamics of Hsp25 Quaternary StructureJournal of Biological Chemistry, 1999
- ANTIGENIC DIVERSITY OF MYCOBACTERIUM TUBERCULOSIS AND MYCOBACTERIUM BOVIS DETECTED BY MEANS OF MONOCLONAL ANTIBODIESThe Lancet, 1981