Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2007-7-26
pubmed:abstractText
To clarify whether the activation of double-stranded RNA-dependent protein kinase (PKR) participates in the cell death induced by endoplasmic reticulum (ER) stress, the authors used cultured retinal ganglion cells (RGC-5, a rat ganglion cell line transformed with the E1A virus) in vitro and the effect of a PKR inhibitor (an imidazolo-oxindole derivative) on N-methyl-D-aspartate (NMDA)-induced retinal damage in mice in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0146-0404
pubmed:author
pubmed:issnType
Print
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3729-36
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:17652745-Animals, pubmed-meshheading:17652745-Animals, Outbred Strains, pubmed-meshheading:17652745-Antiviral Agents, pubmed-meshheading:17652745-Apoptosis, pubmed-meshheading:17652745-Cell Line, Transformed, pubmed-meshheading:17652745-Endoplasmic Reticulum, pubmed-meshheading:17652745-Excitatory Amino Acid Agonists, pubmed-meshheading:17652745-Heat-Shock Proteins, pubmed-meshheading:17652745-Mice, pubmed-meshheading:17652745-Molecular Chaperones, pubmed-meshheading:17652745-N-Methylaspartate, pubmed-meshheading:17652745-Phosphorylation, pubmed-meshheading:17652745-RNA, Small Interfering, pubmed-meshheading:17652745-Rats, pubmed-meshheading:17652745-Retinal Ganglion Cells, pubmed-meshheading:17652745-Transcription Factor CHOP, pubmed-meshheading:17652745-Tunicamycin, pubmed-meshheading:17652745-eIF-2 Kinase
pubmed:year
2007
pubmed:articleTitle
Involvement of double-stranded RNA-dependent protein kinase in ER stress-induced retinal neuron damage.
pubmed:affiliation
Department of Biofunctional Molecules, Gifu Pharmaceutical University, Gifu, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't