Linked Life Data

18637512

Source:http://linkedlifedata.com/resource/pubmed/id/18637512

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2008-7-21
pubmed:abstractText
Caspase-dependent apoptosis has an important role in controlling viruses, and as a result, viruses often encode proteins that target this pathway. Caspase-dependent apoptosis can be activated from within the infected cell as an intrinsic response to replication-associated stresses or through death-inducing signals produced extrinsically by immune cells. Cytomegaloviruses (CMVs) encode a mitochondria-localized inhibitor of apoptosis, vMIA, and a viral inhibitor of caspase activation, vICA, the functional homologs of Bcl-2 related and c-FLIP proteins, respectively. Evidence from viral mutants deleting either vMIA or vICA suggests that each is necessary and sufficient to promote survival of infected cells undergoing caspase-dependent apoptosis. Additional proteins, including pUL38, IE1(491a), and IE2(579aa), can prevent apoptosis induced by various stimuli, while viruses with deletions of UL38, M45, or m41 undergo apoptosis. The viral RNA, beta2.7, binds mitochondrial respiratory complex I, maintains ATP production late in infection, and prevents death induced by a mitochondrial poison. Thus, CMV alters cell intrinsic defenses employing apoptosis, and multiple viral gene products together control death-inducing stimuli to promote survival.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0070-217X
pubmed:author
pubmed:issnType
Print
pubmed:volume
325
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
281-95
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Control of apoptosis by human cytomegalovirus.
pubmed:affiliation
Department of Microbiology & Immunology, Emory Vaccine Center, Emory University Atlanta, GA 30322, USA. louise.mccormick@emory.edu
pubmed:publicationType
Journal Article, Review