Structure of the catalytic domain of the human mitochondrial Lon protease: Proposed relation of oligomer formation and activity-Reference-Cited by-同舟云学术

Structure of the catalytic domain of the human mitochondrial Lon protease: Proposed relation of oligomer formation and activity

Published:2010-03-10 Issue:5 Volume:19 Page:987-999
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

García-Nafría Javier,Ondrovičová Gabriela,Blagova Elena,Levdikov Vladimir M.,Bauer Jacob A.,Suzuki Carolyn K.,Kutejová Eva,Wilkinson Anthony J.,Wilson Keith S.

Funder

Bratislava by the Slovak Grant Agency

Slovak Research and Development Agency

York by European Commission Funding

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.376/fullpdf

Reference46 articles.

1. Regulation by proteolysis: energy-dependent proteases and their targets;Gottesman;Microbiol Rev,1992

2. Identification of the gene Lon (capR) product as a 94-kilodalton polypeptide by cloning and deletion analysis;Schoemaker;J Bacteriol,1981

3. Multiple intracellular locations of Lon protease in Arabidopsis: evidence for the localization of AtLon4 to chloroplasts;Ostersetzer;Plant Cell Physiol,2007

4. A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease;Wang;Proc Natl Acad Sci USA,1993

5. Proteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon protease;Kikuchi;J Biol Chem,2004

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