Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-10-25
pubmed:abstractText
Protein variations in Listeria monocytogenes were analyzed by 2-D electrophoresis. Bacteria were grown either in a rich medium or in a chemically defined medium. Three proteins, which are more expressed in the chemically defined medium than in the rich medium, were identified by mass spectrometry. They are closely related to AppA, Ctc and YvyD. After an osmotic shock, according to the medium and the NaCl concentration, the synthesis rate (P<0.05) of 59 proteins is altered by salinity. Half of them were more expressed, some of these proteins were closely related to Ctc, GbuA and the 30S ribosomal protein S6. Among the proteins which were down-expressed in the presence of salt, two were similar to AckA and PdhD.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0378-1097
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
215
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
183-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
A proteomic analysis of the salt stress response of Listeria monocytogenes.
pubmed:affiliation
Station de Recherches sur la Viande, Institut National de la Recherche Agronomique, 63122, Saint-Genès Champanelle, France.
pubmed:publicationType
Journal Article