Add to ORKGThe heat-shock protein DegP is essential for the survival of Escherichia coli cells at elevated temperatures.As a protease to degrade misfolded proteins in the periplasm,DegP is proposed to have chaperone activity as well.However,the mechanisms regulating this dual-function are poorly understood.Her...The heat-shock protein DegP is essential for the survival of Escherichia coli cells at elevated temperatures.As a protease to degrade misfolded proteins in the periplasm,DegP is proposed to have chaperone activity as well.However,the mechanisms regulating this dual-function are poorly understood.Her...中国化学会
DegP is a heat shock protein from high temperature requirement protease A family, which reacts to th...
Intracellular proteases combat proteotoxic stress by degrading damaged proteins, but their activity ...
Aberrant proteins represent an extreme hazard to cells. Therefore, molecular chaperones and protease...
DegP (also designated as HtrA) and its homologs are found in prokaryotic cells and such eukaryotic o...
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...
Cells use molecular chaperones and proteases to implement the essential quality control mechanism of...
DegP is a heat-shock protein which is localized in the periplasm of Escherichia coli. It is a common...
The DegP (or HtrA) is a highly conserved family of proteins functioning in all living organisms. It ...
The protein quality control machinery is a delicate and integrated network of molecular tools workin...
Cells use molecular chaperones and proteases to implement the essential quality control mechanism of...
Protein quality control in cells involves molecular chaperones that promote folding and proteases th...
Escherichia coli DegP protein is a periplasmic protein that functions both as a protease and as a ch...
AbstractMisfolding or unfolding of polypeptides can occur as a consequence of environmental stress a...
In contrast to protein folding in the cytoplasm of Escherichia coli the folding of proteins in the p...
DegP is a heat shock protein from high temperature requirement protease A family, which reacts to th...
Intracellular proteases combat proteotoxic stress by degrading damaged proteins, but their activity ...
Aberrant proteins represent an extreme hazard to cells. Therefore, molecular chaperones and protease...
DegP (also designated as HtrA) and its homologs are found in prokaryotic cells and such eukaryotic o...
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...
Cells use molecular chaperones and proteases to implement the essential quality control mechanism of...
DegP is a heat-shock protein which is localized in the periplasm of Escherichia coli. It is a common...
The DegP (or HtrA) is a highly conserved family of proteins functioning in all living organisms. It ...
The protein quality control machinery is a delicate and integrated network of molecular tools workin...
Cells use molecular chaperones and proteases to implement the essential quality control mechanism of...
Protein quality control in cells involves molecular chaperones that promote folding and proteases th...
Escherichia coli DegP protein is a periplasmic protein that functions both as a protease and as a ch...
AbstractMisfolding or unfolding of polypeptides can occur as a consequence of environmental stress a...
In contrast to protein folding in the cytoplasm of Escherichia coli the folding of proteins in the p...
DegP is a heat shock protein from high temperature requirement protease A family, which reacts to th...
Intracellular proteases combat proteotoxic stress by degrading damaged proteins, but their activity ...
Aberrant proteins represent an extreme hazard to cells. Therefore, molecular chaperones and protease...