DegP is both an ATP-independent protease and chaperone in the E. coli periplasm. In a new structural model of DegP recently published in Nature, Krojer et al. suggest that DegP carries out these seemingly opposing roles by assembling into enormous spherical multimers
Aberrant proteins represent an extreme hazard to cells. Therefore, molecular chaperones and protease...
International audienceThe chaperone/protease DegP belongs to the HtrA superfamily and is involved in...
Molecular chaperones and proteases monitor the folded state of other proteins. In addition to recog...
DegP is both an ATP-independent protease and chaperone in the E. coli periplasm. In a new structural...
All organisms have to monitor the folding state of cellular proteins precisely. The heat-shock prote...
DegP (a.k.a. HtrA) is an essential heat-shock protein in the periplasm of Escherichia coli. Recently...
Protein quality control in cells involves molecular chaperones that promote folding and proteases th...
The heat-shock protein DegP is essential for the survival of Escherichia coli cells at elevated temp...
Structure-function analysis of DegP revealed a novel mechanism for protease and chaperone regulation...
The protein quality control machinery is a delicate and integrated network of molecular tools workin...
The DegP (or HtrA) is a highly conserved family of proteins functioning in all living organisms. It ...
DegP is a heat-shock protein which is localized in the periplasm of Escherichia coli. It is a common...
Cells use molecular chaperones and proteases to implement the essential quality control mechanism of...
DegP (also designated as HtrA) and its homologs are found in prokaryotic cells and such eukaryotic o...
Cells use molecular chaperones and proteases to implement the essential quality control mechanism of...
Aberrant proteins represent an extreme hazard to cells. Therefore, molecular chaperones and protease...
International audienceThe chaperone/protease DegP belongs to the HtrA superfamily and is involved in...
Molecular chaperones and proteases monitor the folded state of other proteins. In addition to recog...
DegP is both an ATP-independent protease and chaperone in the E. coli periplasm. In a new structural...
All organisms have to monitor the folding state of cellular proteins precisely. The heat-shock prote...
DegP (a.k.a. HtrA) is an essential heat-shock protein in the periplasm of Escherichia coli. Recently...
Protein quality control in cells involves molecular chaperones that promote folding and proteases th...
The heat-shock protein DegP is essential for the survival of Escherichia coli cells at elevated temp...
Structure-function analysis of DegP revealed a novel mechanism for protease and chaperone regulation...
The protein quality control machinery is a delicate and integrated network of molecular tools workin...
The DegP (or HtrA) is a highly conserved family of proteins functioning in all living organisms. It ...
DegP is a heat-shock protein which is localized in the periplasm of Escherichia coli. It is a common...
Cells use molecular chaperones and proteases to implement the essential quality control mechanism of...
DegP (also designated as HtrA) and its homologs are found in prokaryotic cells and such eukaryotic o...
Cells use molecular chaperones and proteases to implement the essential quality control mechanism of...
Aberrant proteins represent an extreme hazard to cells. Therefore, molecular chaperones and protease...
International audienceThe chaperone/protease DegP belongs to the HtrA superfamily and is involved in...
Molecular chaperones and proteases monitor the folded state of other proteins. In addition to recog...
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