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rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
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|
pubmed:dateCreated |
1996-10-17
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|
pubmed:abstractText |
The past year has brought some notable advances in our understanding of the structure and function of elongation factors (EFs) involved in protein biosynthesis. The structures of the ternary complex of aminoacylated tRNA with EF-Tu.GTP and of the complex EF-Tu.EF-Ts have been determined. Within the same period, new cryo-electron microscopy reconstructions of ribosome particles have been obtained.
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pubmed:language |
eng
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pubmed:journal |
|
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
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|
pubmed:issn |
0958-1669
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
369-75
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8768893-Bacterial Proteins,
pubmed-meshheading:8768893-Guanosine Triphosphate,
pubmed-meshheading:8768893-Hydrolysis,
pubmed-meshheading:8768893-Models, Biological,
pubmed-meshheading:8768893-Models, Molecular,
pubmed-meshheading:8768893-Peptide Chain Elongation, Translational,
pubmed-meshheading:8768893-Peptide Elongation Factor Tu,
pubmed-meshheading:8768893-Peptide Elongation Factors,
pubmed-meshheading:8768893-Protein Conformation,
pubmed-meshheading:8768893-Ribosomes
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|
pubmed:year |
1996
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|
pubmed:articleTitle |
Elongation in bacterial protein biosynthesis.
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|
pubmed:affiliation |
Department of Molecular and Structural Biology, University of Aarhus, Denmark. jnb@kemi.aau.dk
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|
