Linked Life Data

17023813

Source:http://linkedlifedata.com/resource/pubmed/id/17023813

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2006-10-6
pubmed:abstractText
mRNA is made from DNA. Protein is made from mRNA. Although one might say that "DNA is forever," the same cannot be said for mRNA or protein. These molecules are made in response to the cell's present needs; once the cell's circumstances change, a whole new repertoire of proteins may be needed and the previous set of proteins may be unnecessary, perhaps even deleterious. So, the cell must be able to eliminate the characters in the previous act in favor of the actors needed for the current act. In addition, there is good evidence that the DNA to mRNA to protein flow may not be efficient; abnormal proteins, as well as damaged or misfolded proteins, are quite common and must also be eliminated. This process depends on the ability of the cell to tag the protein to be eliminated with a small protein (or chain of these proteins) that targets the protein to a special structure for digestion into its constituent amino acids for recycling into new proteins. This very common protein tag was identified in the 1970s and called "ubiquitin"--it truly was everyplace! In addition, ubiquitin is crucial to targeting normal proteins to their appropriate place in or on the cell and for recycling of proteins. Ubiqutination of proteins and what follows this tagging are crucial to the normal function of cells. The complexity of these processes is being used for therapy in oncology now and perhaps in immunology and rheumatology in the near future.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1076-1608
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
255-8
pubmed:dateRevised
2008-4-10
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Basic science for the clinician 40: ubiquitin, programmed protein degradation, and the proteasome.
pubmed:affiliation
Pharmaceutical Research Institute, Bristol-Myers Squibb, Pribceton, New Jersey 08543-4000, USA. leonard.sigal@bms.com
pubmed:publicationType
Journal Article, Review