Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria
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Title
Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria
Authors
Keywords
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Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 115, Issue 2, Pages E273-E282
Publisher
Proceedings of the National Academy of Sciences
Online
2017-12-21
DOI
10.1073/pnas.1712051115
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- (2014) Stefanie S. Krajewski et al. ENVIRONMENTAL MICROBIOLOGY
- Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation
- (2014) Marta Carroni et al. eLife
- Molecular Chaperone Functions in Protein Folding and Proteostasis
- (2013) Yujin E. Kim et al. Annual Review of Biochemistry
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- (2013) Helen Saibil NATURE REVIEWS MOLECULAR CELL BIOLOGY
- Unraveling the Mechanism of Protein Disaggregation Through a ClpB-DnaK Interaction
- (2013) R. Rosenzweig et al. SCIENCE
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- (2013) Anthony De Soyza et al. MicrobiologyOpen
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- Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation
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- (2012) Yuki Oguchi et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
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- (2010) N. E. M. de Oliveira et al. MICROBIOLOGY-SGM
- Heat Resistance Mediated by a New Plasmid Encoded Clp ATPase, ClpK, as a Possible Novel Mechanism for Nosocomial Persistence of Klebsiella pneumoniae
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- (2009) K.G. Kerr et al. JOURNAL OF HOSPITAL INFECTION
- Pseudomonas aeruginosaPopulation Biology in Chronic Obstructive Pulmonary Disease
- (2009) Elza Rakhimova et al. JOURNAL OF INFECTIOUS DISEASES
- Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases
- (2009) Janine Kirstein et al. NATURE REVIEWS MICROBIOLOGY
- Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation
- (2008) Peter Tessarz et al. MOLECULAR MICROBIOLOGY
- 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
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- (2008) Aki Suokko et al. PROTEOMICS
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