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[Bacterial ClpX protease structure and function--a review].

Authors: Lin, Wang; Jianping, Xie;

[Bacterial ClpX protease structure and function--a review].

Abstract

ClpX is a member of Hsp100 (heat-shock protein) family which is conserved among organisms. Hsp100/ Clp implicates in stress resistance, intracellular protein turn-over, DNA replication and regulation of gene expression. Tuberculosis remains one of the major threats to human health. In pathogens, ClpX protease plays an important role in the gene expression regulation, pathogenesis, and resistance of immune stress. The structure, substrates and target genes of ClpX are summarized in this study. The biological function of M. tuberculosis ClpX, such as gene expression regulation, pathogenesis, intracellular survival and persistence, evolution and structural feature, substrates is the focus of this summary.

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Keywords

Adenosine Triphosphatases, Hydrolases, Protein Conformation, Escherichia coli Proteins, Molecular Sequence Data, Serine Endopeptidases, Endopeptidase Clp, Gene Expression Regulation, Bacterial, Blotting, Northern, Escherichia coli, ATPases Associated with Diverse Cellular Activities, Humans, Amino Acid Sequence, Heat-Shock Proteins, Molecular Chaperones

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
0
Average
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