17913468

Source:http://linkedlifedata.com/resource/pubmed/id/17913468

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0521116, umls-concept:C0805586, umls-concept:C1159339, umls-concept:C1159342
pubmed:issue	8-9
pubmed:dateCreated	2007-12-10
pubmed:abstractText	The two-partner and autotransport pathways are widely represented in Gram-negative bacteria, essentially among pathogens. Both mediate the translocation of large proteins across the outer membrane. Deciphering the molecular mechanisms of secretion machineries as well as folding of exoproteins in the course of translocation represents a current challenge.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/8907468
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones
pubmed:status	MEDLINE
pubmed:issn	0923-2508
pubmed:author	pubmed-author:HodakHélèneH, pubmed-author:Jacob-DubuissonFrançoiseF
pubmed:issnType	Print
pubmed:volume	158
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	631-7
pubmed:meshHeading	pubmed-meshheading:17913468-Bacterial Proteins, pubmed-meshheading:17913468-Biological Transport, pubmed-meshheading:17913468-Gram-Negative Bacteria, pubmed-meshheading:17913468-Molecular Chaperones, pubmed-meshheading:17913468-Periplasm, pubmed-meshheading:17913468-Protein Folding
pubmed:articleTitle	Current challenges in autotransport and two-partner protein secretion pathways.
pubmed:affiliation	INSERM U629, Institut Pasteur de Lille, IFR142, 1 Rue du Professeur Calmette, 59019 Lille Cedex, France.
pubmed:publicationType	Journal Article, Review, Research Support, Non-U.S. Gov't