Linked Life Data

18292779

Source:http://linkedlifedata.com/resource/pubmed/id/18292779

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-2-22
pubmed:abstractText
Ribosomes, which are central to protein synthesis and convert transcribed mRNAs into polypeptide chains, have been the focus of structural and biochemical studies for more than 50 years. The structure of its larger subunit revealed that the ribosome is a ribozyme with RNA at the heart of its enzymatic activity that catalyses peptide bond formation. Numerous initiation, elongation and release factors ensure that protein synthesis occurs progressively and with high specificity. In the past few years, high-resolution structures have provided molecular snapshots of different intermediates in ribosome-mediated translation in atomic detail. Together, these studies have revolutionized our understanding of the mechanism of protein synthesis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1471-0080
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
242-53
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
A structural understanding of the dynamic ribosome machine.
pubmed:affiliation
Department of Molecular Biophysics and Biochemistry, Department of Chemistry, Yale University, and the Howard Hughes Medical Institute, New Haven, Connecticut 06520-8114, USA. peggy.eatherton@yale.edu
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't