| pubmed-article:14965779 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14965779 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:14965779 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:14965779 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:14965779 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:14965779 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:14965779 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:14965779 | pubmed:dateCreated | 2004-2-17 | lld:pubmed |
| pubmed-article:14965779 | pubmed:abstractText | In bacteria, protein expression initiates with a formyl-methionine group. Addition of the antibiotic actinonin, a known peptide deformylase inhibitor, at the time of induction of protein expression results in the retention of the formyl group by the overexpressed protein. In addition, because deformylation is a prerequisite for removal of the initiating methionine, this post-translational processing step is also prevented by actinonin, and the N-formyl methionine residue is retained by proteins from which it is normally removed. We have demonstrated the applicability of this system for obtaining N-modified forms of several different proteins and use one of these modified molecules to show that the N-terminal amino group is not required for ClpXP degradation of proteins bearing an N-terminal recognition signal. | lld:pubmed |
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| pubmed-article:14965779 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14965779 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14965779 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14965779 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14965779 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14965779 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14965779 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14965779 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14965779 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14965779 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14965779 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:14965779 | pubmed:issn | 1046-5928 | lld:pubmed |
| pubmed-article:14965779 | pubmed:author | pubmed-author:BakerTania... | lld:pubmed |
| pubmed-article:14965779 | pubmed:author | pubmed-author:SauerRobert... | lld:pubmed |
| pubmed-article:14965779 | pubmed:author | pubmed-author:TidorBruceB | lld:pubmed |
| pubmed-article:14965779 | pubmed:author | pubmed-author:FlynnJulia... | lld:pubmed |
| pubmed-article:14965779 | pubmed:author | pubmed-author:SpectorShariS | lld:pubmed |
| pubmed-article:14965779 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14965779 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:14965779 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14965779 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14965779 | pubmed:pagination | 317-22 | lld:pubmed |
| pubmed-article:14965779 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:14965779 | pubmed:meshHeading | pubmed-meshheading:14965779... | lld:pubmed |
| pubmed-article:14965779 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14965779 | pubmed:articleTitle | Expression of N-formylated proteins in Escherichia coli. | lld:pubmed |
| pubmed-article:14965779 | pubmed:affiliation | Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA. | lld:pubmed |
| pubmed-article:14965779 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14965779 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14965779 | lld:pubmed |
