Linked Life Data

15787194

Source:http://linkedlifedata.com/resource/pubmed/id/15787194

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2005-3-24
pubmed:abstractText
Listeria monocytogenes is a ubiquitous gram-positive, rod-shaped, widespread in nature, facultative intracellular human and animal pathogen that causes infections collectively termed listeriosis. L. monocytogenes EGD encodes a total of 133 surface proteins, the abundance of which, as well as the variety of anchoring systems, probably reflects the ability of this bacterium to survive in diverse environments and to interact with many kinds of eukaryotic cells. The group of surface proteins also includes proteins with murein hydrolase activity-autolysins. To date, five L. monocytogenes autolysins have been identified: p60, P45, Ami, MurA and Auto. These enzymes are involved in numerous cellular processes including cell growth, cell wall turnover, peptidoglycan maturation, cell division and separation, formation of flagella, sporulation, chemotaxis and biofilm formation, genetic competence, protein secretion, the lytic action of some antibiotics and pathogenicity. We have recently identified a putative sixth listerial peptidoglycan-degrading enzyme, which has surprisingly been identified as FlaA, a flagellar protein of L. monocytogenes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1733-1331
pubmed:author
pubmed:issnType
Print
pubmed:volume
53 Suppl
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29-34
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Analysis of the peptidoglycan hydrolases of Listeria monocytogenes: multiple enzymes with multiple functions.
pubmed:affiliation
Department of Bacterial Physiology, Institute of Microbiology, Warsaw University 02-096 Warsaw, Poland. magdapop@biol.uw.edu.pl
pubmed:publicationType
Journal Article, Review