Linked Life Data

9638789

Source:http://linkedlifedata.com/resource/pubmed/id/9638789

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-7-23
pubmed:abstractText
The ubiquitin-proteasome proteolytic pathway has recently been reported to be of major importance in the breakdown of skeletal muscle proteins. The first step in this pathway is the covalent attachment of polyubiquitin chains to the targeted protein. Polyubiquitylated proteins are then recognized and degraded by the 26S proteasome complex. In this review, we critically analyse recent findings in the regulation of this pathway, both in animal models of muscle wasting and in some human diseases. The identification of regulatory steps of ubiquitin conjugation to protein substrates and/or of the proteolytic activities of the proteasome should lead to new concepts that can be used to manipulate muscle protein mass. Such concepts are essential for the development of anti-cachectic therapies for many clinical situations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0926-5287
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
153-65
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Ubiquitin-proteasome-dependent proteolysis in skeletal muscle.
pubmed:affiliation
Centre de recherche en nutrition humaine de Clermont-Ferrand, Ceyrat, France. attaix@clermont.inra.fr
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't