@article{9dddb1e0a02c11dd889c000ea68e967b,
title = "Characterization of mouse Clpp protease cDNA, gene, and protein.",
abstract = "Mutations that cause accumulation or rapid degradation owing to protein misfolding are a frequent cause of inherited disease in humans. In Escherichia coli, Clpp protease is one of the components of the protein quality control system that handles misfolded proteins. In the present study, we have characterized the mouse Clpp cDNA sequence, the organization of the mouse gene, the chromosomal localization, and the tissue-specific expression pattern. Moreover. the cellular localization and processing of mouse Clpp was studied by overexpression in transfected eukaryotic cells. Our results indicate that mouse and human Clpp have similar roles, and they provide the molecular basis for establishing a Clpp knockout mouse and to study its phenotype, thereby shedding light on a possible role of Clpp in human disease.",
keywords = "Adenosine Triphosphatases, Animals, Base Sequence, Chromosome Mapping, DNA Primers, DNA, Complementary, Endopeptidase Clp, Exons, Humans, Introns, Mice, Mice, Inbred C57BL, Molecular Sequence Data, Recombinant Proteins, Serine Endopeptidases",
author = "Andresen, {B S} and Corydon, {T J} and M Wilsbech and P Bross and Hindkjaer, {T F} and L Bolund and N Gregersen and Schroeder, {L D}",
year = "2000",
language = "English",
volume = "11",
pages = "275--80",
journal = "Mammalian Genome",
issn = "0938-8990",
publisher = "Springer",
number = "4",
}