Linked Life Data

17212580

Source:http://linkedlifedata.com/resource/pubmed/id/17212580

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 1
pubmed:dateCreated
2007-1-10
pubmed:abstractText
This review focuses on recent insights into the mechanisms and the biological functions of the proteasome. This large ATP-dependent proteolytic complex is the main site for protein degradation in mammalian cells and catalyses the rapid degradation of ubiquitinated proteins, and is the source of most antigenic peptides used by the immune system to screen for viruses and cancer. ATP is required to unfold globular proteins to open the gated channel into the 20S proteasome and to facilitate protein translation into it. Inhibitors of its proteolytic activity are widely used as research tools and have proven effective in cancer therapy.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0300-5127
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12-7
pubmed:dateRevised
2010-12-3
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy.
pubmed:affiliation
Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA. alfred_goldberg@hms.harvard.edu
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't