Aggregate-Reactivation Activity of the Molecular Chaperone ClpB from Ehrlichia chaffeensis
Published 2013 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Aggregate-Reactivation Activity of the Molecular Chaperone ClpB from Ehrlichia chaffeensis
Authors
Keywords
-
Journal
PLoS One
Volume 8, Issue 5, Pages e62454
Publisher
Public Library of Science (PLoS)
Online
2013-05-08
DOI
10.1371/journal.pone.0062454
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency
- (2013) Ting Zhang et al. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
- Aggregate reactivation mediated by the Hsp100 chaperones
- (2012) Michal Zolkiewski et al. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
- Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation
- (2012) Juliane Winkler et al. JOURNAL OF CELL BIOLOGY
- Transmission Electron Microscopy Reveals Distinct Macrophage- and Tick Cell-Specific Morphological Stages of Ehrlichia chaffeensis
- (2012) Sarah E. Dedonder et al. PLoS One
- The elusive middle domain of Hsp104 and ClpB: Location and function
- (2011) Morgan E. DeSantis et al. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
- Inactivation ofclpBin the Pathogen Leptospira interrogans Reduces Virulence and Resistance to Stress Conditions
- (2011) Kristel Lourdault et al. INFECTION AND IMMUNITY
- Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation
- (2011) M. Miot et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- The M-Domain Controls Hsp104 Protein Remodeling Activity in an Hsp70/Hsp40-Dependent Manner
- (2010) Bernhard Sielaff et al. JOURNAL OF MOLECULAR BIOLOGY
- clpB, a class III heat-shock gene regulated by CtsR, is involved in thermotolerance and virulence of Enterococcus faecalis
- (2010) N. E. M. de Oliveira et al. MICROBIOLOGY-SGM
- ClgR regulation of chaperone and protease systems is essential for Mycobacterium tuberculosis parasitism of the macrophage
- (2010) M. Estorninho et al. MICROBIOLOGY-SGM
- Anaplasma phagocytophilum and Ehrlichia chaffeensis: subversive manipulators of host cells
- (2010) Yasuko Rikihisa NATURE REVIEWS MICROBIOLOGY
- Cellular strategies for controlling protein aggregation
- (2010) Jens Tyedmers et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface
- (2009) Sergio P. Acebrón et al. FEBS LETTERS
- Molecular characterization of Ehrlichia interactions with tick cells and macrophages
- (2009) Roman Reddy Ganta Frontiers in Bioscience-Landmark
- Synergistic Cooperation between Two ClpB Isoforms in Aggregate Reactivation
- (2009) Maria Nagy et al. JOURNAL OF MOLECULAR BIOLOGY
- Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB
- (2009) Maria Nagy et al. PROTEIN SCIENCE
- Molecular Chaperones in Pathogen Virulence: Emerging New Targets for Therapy
- (2008) Len Neckers et al. Cell Host & Microbe
- Characterization of a Unique ClpB Protein of Mycoplasma pneumoniae and Its Impact on Growth
- (2008) T. R. Kannan et al. INFECTION AND IMMUNITY
- Emerging and Re-emerging Tick-Transmitted Rickettsial and Ehrlichial Infections
- (2008) David H. Walker et al. MEDICAL CLINICS OF NORTH AMERICA
- The heat-shock protein ClpB of Francisella tularensis is involved in stress tolerance and is required for multiplication in target organs of infected mice
- (2008) Karin L. Meibom et al. MOLECULAR MICROBIOLOGY
- Hsp104 and ClpB: protein disaggregating machines
- (2008) Shannon M. Doyle et al. TRENDS IN BIOCHEMICAL SCIENCES
Find Funding. Review Successful Grants.
Explore over 25,000 new funding opportunities and over 6,000,000 successful grants.
ExploreCreate your own webinar
Interested in hosting your own webinar? Check the schedule and propose your idea to the Peeref Content Team.
Create Now