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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2010-6-17
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pubmed:abstractText |
Human cell-derived in vitro protein synthesis systems are useful for the production of recombinant proteins. Productivity can be increased by supplementation with GADD34, a protein that is difficult to express in and purify from E. coli. Deletion of the N-terminal 120 or 240 amino acids of GADD34 improves recovery of this protein from E. coli without compromising its ability to boost protein synthesis in an in vitro protein synthesis system. The use of N-terminally truncated GADD34 proteins in place of full-length GADD34 should improve the utility of human cell-based cell-free protein synthesis systems.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1573-6776
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
897-902
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:20349333-Antigens, Differentiation,
pubmed-meshheading:20349333-Cell Cycle Proteins,
pubmed-meshheading:20349333-Cell Extracts,
pubmed-meshheading:20349333-Escherichia coli,
pubmed-meshheading:20349333-Gene Expression,
pubmed-meshheading:20349333-Humans,
pubmed-meshheading:20349333-Protein Biosynthesis,
pubmed-meshheading:20349333-Protein Phosphatase 1,
pubmed-meshheading:20349333-Proteins,
pubmed-meshheading:20349333-Recombinant Proteins,
pubmed-meshheading:20349333-Sequence Deletion
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pubmed:year |
2010
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pubmed:articleTitle |
N-terminally truncated GADD34 proteins are convenient translation enhancers in a human cell-derived in vitro protein synthesis system.
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pubmed:affiliation |
RIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, 230-0045, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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