| pubmed-article:12829374 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12829374 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:12829374 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:12829374 | lifeskim:mentions | umls-concept:C0231448 | lld:lifeskim |
| pubmed-article:12829374 | lifeskim:mentions | umls-concept:C1254042 | lld:lifeskim |
| pubmed-article:12829374 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
| pubmed-article:12829374 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:12829374 | lifeskim:mentions | umls-concept:C1515926 | lld:lifeskim |
| pubmed-article:12829374 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:12829374 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:12829374 | pubmed:dateCreated | 2003-6-27 | lld:pubmed |
| pubmed-article:12829374 | pubmed:abstractText | Large subunits of NiFe-hydrogenases undergo a unique maturation process in which the last step consists of the endoproteolytic cleavage of the C-terminal extension after the Ni-Fe metal center has been assembled. To assess in vivo the influence of alteration of the C-terminal extension on the processing, green fluorescence protein (GFP) was fused to the C-terminus of the large subunit (HybC) of the Escherichia coli hydrogenase 2. Interestingly, no processing of HybC-GFP was observed. In addition, the chromophore of GFP was not formed, implying a nonproductive folding of the upstream HybC moiety. These results strongly suggest that the alteration of the C-terminus of the hydrogenase 2 large subunit interferes with the folding and processing of HybC. | lld:pubmed |
| pubmed-article:12829374 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12829374 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12829374 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12829374 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12829374 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12829374 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12829374 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12829374 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12829374 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12829374 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12829374 | pubmed:issn | 0300-9084 | lld:pubmed |
| pubmed-article:12829374 | pubmed:author | pubmed-author:ZhangMingM | lld:pubmed |
| pubmed-article:12829374 | pubmed:author | pubmed-author:WuLong-FeiLF | lld:pubmed |
| pubmed-article:12829374 | pubmed:author | pubmed-author:PradelNathali... | lld:pubmed |
| pubmed-article:12829374 | pubmed:author | pubmed-author:Mandrand-Bert... | lld:pubmed |
| pubmed-article:12829374 | pubmed:author | pubmed-author:YuZengliangZ | lld:pubmed |
| pubmed-article:12829374 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12829374 | pubmed:volume | 85 | lld:pubmed |
| pubmed-article:12829374 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12829374 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12829374 | pubmed:pagination | 575-9 | lld:pubmed |
| pubmed-article:12829374 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:12829374 | pubmed:meshHeading | pubmed-meshheading:12829374... | lld:pubmed |
| pubmed-article:12829374 | pubmed:meshHeading | pubmed-meshheading:12829374... | lld:pubmed |
| pubmed-article:12829374 | pubmed:meshHeading | pubmed-meshheading:12829374... | lld:pubmed |
| pubmed-article:12829374 | pubmed:meshHeading | pubmed-meshheading:12829374... | lld:pubmed |
| pubmed-article:12829374 | pubmed:meshHeading | pubmed-meshheading:12829374... | lld:pubmed |
| pubmed-article:12829374 | pubmed:meshHeading | pubmed-meshheading:12829374... | lld:pubmed |
| pubmed-article:12829374 | pubmed:meshHeading | pubmed-meshheading:12829374... | lld:pubmed |
| pubmed-article:12829374 | pubmed:meshHeading | pubmed-meshheading:12829374... | lld:pubmed |
| pubmed-article:12829374 | pubmed:meshHeading | pubmed-meshheading:12829374... | lld:pubmed |
| pubmed-article:12829374 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12829374 | pubmed:articleTitle | Effect of alteration of the C-terminal extension on the maturation and folding of the large subunit of the Escherichia coli hydrogenase-2. | lld:pubmed |
| pubmed-article:12829374 | pubmed:affiliation | Laboratoire de Chimie Bactérienne, UPR9043 CNRS, Institut de Biologie Structurale et Microbiologie, 31 chemin Joseph Aiguier, 13402 Marseille cedex 20, France. | lld:pubmed |
| pubmed-article:12829374 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12829374 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:12829374 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:945182 | entrezgene:pubmed | pubmed-article:12829374 | lld:entrezgene |
