Linked Life Data

20599291

Source:http://linkedlifedata.com/resource/pubmed/id/20599291

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2010-8-23
pubmed:abstractText
In controlling the switch from latency to lytic infection, the immediate early (IE) genes lie at the core of herpesvirus pathogenesis. To image the 72kDa human cytomegalovirus (HCMV) major IE protein (IE1-72K), a recombinant virus encoding IE1 fused with EGFP was constructed. Using this construct, the IE1-EGFP fusion was detected at ND10 (PML-bodies) within 2h post infection (p.i.) and the complete disruption of ND10 imaged through to 6h p.i. HCMV genomes and IE2-86K protein could be detected adjacent to the slowly degrading IE1-72K/ND10 foci. IE1-72K associates with metaphase chromatin, recruiting both PML and STAT2. hDaxx, STAT1 and IE2-86K did not re-locate to metaphase chromatin; the fate of hDaxx is particularly important as this protein contributes to an intrinsic barrier to HCMV infection. While IE1-72K participates in a complex with chromatin, PML, STAT2 and Sp100, IE1-72K releases hDaxx from ND10 yet does not appear to remain associated with it.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Nuclear, http://linkedlifedata.com/resource/pubmed/chemical/Autoantigens, http://linkedlifedata.com/resource/pubmed/chemical/Chromatin, http://linkedlifedata.com/resource/pubmed/chemical/IE1 protein, cytomegalovirus, http://linkedlifedata.com/resource/pubmed/chemical/IE2 protein, Cytomegalovirus, http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/PML protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/STAT2 Transcription Factor, http://linkedlifedata.com/resource/pubmed/chemical/STAT2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Sp100 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/nuclear dot protein 52, human
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1618-1298
pubmed:author
pubmed:copyrightInfo
Copyright (c) 2010 Elsevier GmbH. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
89
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
757-68
pubmed:meshHeading
pubmed-meshheading:20599291-Antigens, Nuclear, pubmed-meshheading:20599291-Autoantigens, pubmed-meshheading:20599291-Chromatin, pubmed-meshheading:20599291-Cytomegalovirus, pubmed-meshheading:20599291-Cytomegalovirus Infections, pubmed-meshheading:20599291-HeLa Cells, pubmed-meshheading:20599291-Humans, pubmed-meshheading:20599291-Image Processing, Computer-Assisted, pubmed-meshheading:20599291-Immediate-Early Proteins, pubmed-meshheading:20599291-Metaphase, pubmed-meshheading:20599291-Microscopy, Fluorescence, pubmed-meshheading:20599291-Microscopy, Video, pubmed-meshheading:20599291-Nuclear Proteins, pubmed-meshheading:20599291-Recombinant Fusion Proteins, pubmed-meshheading:20599291-STAT2 Transcription Factor, pubmed-meshheading:20599291-Trans-Activators, pubmed-meshheading:20599291-Transcription Factors, pubmed-meshheading:20599291-Tumor Suppressor Proteins
pubmed:year
2010
pubmed:articleTitle
Differential relocation and stability of PML-body components during productive human cytomegalovirus infection: detailed characterization by live-cell imaging.
pubmed:affiliation
Department of Virology, Faculty of Medicine, University of Crete, Heraklion 71003, Crete, Greece.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't