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2 subtopics

 

  • Endopeptidase Clp
  • Protease La

ATP-Dependent ProteasesFollow by RSS 

You've reached a pubget topic page. Below are the latest papers on this topic, with subtopics on the left.

keywords > Enzymes and Coenzymes > Enzymes > Hydrolases > Peptide Hydrolases > ATP-Dependent Proteases

Latest papers

Tools for the study of protein quality control systems: use of truncated homoserine trans-succinylase as a model substrate for ATP-dependent proteolysis in Escherichia coli.

Peptidyl boronates inhibit Salmonella enterica serovar Typhimurium Lon protease by a competitive ATP-dependent mechanism.

Bacterial cell division protein FtsZ is stable against degradation by AAA family protease FtsH in Escherichia coli cells.

Characterization of protomer interfaces in HslV protease; the bacterial homologue of 20S proteasome.

White leaf sectors in yellow variegated2 are formed by viable cells with undifferentiated plastids.

GTP/GDP binding stabilizes bacterial cell division protein FtsZ against degradation by FtsH protease in vitro.

Nucleotide triphosphates inhibit the degradation of unfolded proteins by HslV peptidase.

Characterization and localization of Plasmodium falciparum homolog of prokaryotic ClpQ/HslV protease.

[Characterization of the HtrA family of proteins].

ATP-dependent proteases of bacteria: recognition logic and operating principles

Porphyromonas gingivalis genes involved in community development with Streptococcus gordonii.

Characterization of mutants of the Escherichia coli AAA protease, FtsH, carrying a mutation in the central pore region

Requirement for the acetyl phosphate pathway in Escherichia coli ATP-dependent proteolysis.

Proteasome-related HslU and HslV genes typical of eubacteria are widespread in eukaryotes.

Flavodoxin, a new fluorescent substrate for monitoring proteolytic activity of FtsH lacking a robust unfolding activity.

Quality control of photosystem II. Cleavage of reaction center D1 protein in spinach thylakoids by FtsH protease under moderate heat stress.

Functional characterization of AAA family FtsH protease of Mycobacterium tuberculosis.

The Escherichia coli plasma membrane contains two PHB (prohibitin homology) domain protein complexes of opposite orientations.

An AAA protease FtsH can initiate proteolysis from internal sites of a model substrate, apo-flavodoxin.

Oligomeric structure of the ATP-dependent protease La (Lon) of Escherichia coli.

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