Protease La

"Protease La" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, which enables searching at various levels of specificity.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

A prokaryotic ATP-dependent protease that plays a role in the degradation of many abnormal proteins. It is a tetramer of 87-kDa subunits, each of which contains a proteolytic site and a ATP-binding site.

Descriptor ID

D049070

MeSH Number(s)

D08.811.277.656.149.099.750

D08.811.277.656.300.065.750

Concept/Terms

Protease La

Below are MeSH descriptors whose meaning is more general than "Protease La".

Chemicals and Drugs [D]
Enzymes and Coenzymes [D08]
Enzymes [D08.811]
Hydrolases [D08.811.277]
Peptide Hydrolases [D08.811.277.656]
ATP-Dependent Proteases [D08.811.277.656.149]
ATP-Dependent Endopeptidases [D08.811.277.656.149.099]
Protease La [D08.811.277.656.149.099.750]
Endopeptidases [D08.811.277.656.300]
ATP-Dependent Endopeptidases [D08.811.277.656.300.065]
Protease La [D08.811.277.656.300.065.750]

Below are MeSH descriptors whose meaning is related to "Protease La".

Below are MeSH descriptors whose meaning is more specific than "Protease La".

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Protease La" by people in Harvard Catalyst Profiles by year, and whether "Protease La" was a major or minor topic of these publication.

Bar chart showing 4 publications over 4 distinct years, with a maximum of 1 publications in 1998 and 1999 and 2007 and 2016

To see the data from this visualization as text, click here.

Year	Major Topic	Total
1998	1	1
1999	1	1
2007	1	1
2016	1	1

Below are the most recent publications written about "Protease La" by people in Profiles.

Emerging role of Lon protease as a master regulator of mitochondrial functions. Biochim Biophys Acta. 2016 Aug; 1857(8):1300-1306.

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Roles of Lon protease and its substrate MarA during sodium salicylate-mediated growth reduction and antibiotic resistance in Escherichia coli. Microbiology (Reading). 2016 05; 162(5):764-776.

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Nutritional Control of DNA Replication Initiation through the Proteolysis and Regulated Translation of DnaA. PLoS Genet. 2015 Jul; 11(7):e1005342.

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Proteotoxic stress induces a cell-cycle arrest by stimulating Lon to degrade the replication initiator DnaA. Cell. 2013 Aug 01; 154(3):623-36.

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Regulated proteolysis of a transcription factor complex is critical to cell cycle progression in Caulobacter crescentus. Mol Microbiol. 2013 Mar; 87(6):1277-89.

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Escherichia coli toxin/antitoxin pair MqsR/MqsA regulate toxin CspD. Environ Microbiol. 2010 May; 12(5):1105-21.

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Evidence that two ATP-dependent (Lon) proteases in Borrelia burgdorferi serve different functions. PLoS Pathog. 2009 Nov; 5(11):e1000676.

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[Effect of RNA interference for Lon gene silencing on growth and apoptosis of human breast cancer MCF7 cells]. Nan Fang Yi Ke Da Xue Xue Bao. 2007 Jun; 27(6):870-4.

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ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli. FEBS Lett. 1999 Jul 30; 456(1):211-4.

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LonR9 carrying a single Glu614 to Lys mutation inhibits the ATP-dependent protease La (Lon) by forming mixed oligomeric complexes. Biochem Biophys Res Commun. 1998 Sep 08; 250(1):32-5.

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