Linked Life Data

17645437

Source:http://linkedlifedata.com/resource/pubmed/id/17645437

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2007-9-12
pubmed:abstractText
HIV and many other enveloped viruses encode a late budding domain (L-domain) that recruits the cellular machinery that mediates the separation of the nascent virion from the infected cell. The ubiquitin-proteasome system has been implicated in the L-domain activity, but the exact role of ubiquitin transfer and ubiquitin-binding proteins in the last step of viral replication remains elusive. It is now widely accepted that the class E vacuolar protein sorting pathway mediates both viral budding and vesicle budding into the multivesicular bodies and, remarkably, both budding events share the same topology and similar requirements for ubiquitin. In this review, the role of ubiquitin in viral budding is discussed in the light of recent advances in the understanding of the cellular mechanisms that assist the last step of HIV-1 release.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1398-9219
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1297-303
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
The role of ubiquitin in retroviral egress.
pubmed:affiliation
Department of Infectious Diseases, 2nd Floor New Guy's House, Guy's Hospital, King's College London School of Medicine at Guy's, King's College and St Thomas' Hospitals, London, SE1 9RT, UK. juan.martin_serrano@kcl.ac.uk
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't