Linked Life Data

20018937

Source:http://linkedlifedata.com/resource/pubmed/id/20018937

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2010-2-19
pubmed:abstractText
Heat shock protein 70s (Hsp70s) are molecular chaperones that protect cells from damage in response to various stress stimuli. However, the functions and mechanisms in endothelial cells (ECs) have not been examined. Herein, we investigate the role of Hsp70s, including heat shock cognate protein 70 (Hsc70), which is constitutively expressed in nonstressed cells (ie, ECs).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1524-4636
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
491-7
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:20018937-Animals, pubmed-meshheading:20018937-Benzhydryl Compounds, pubmed-meshheading:20018937-Cell Movement, pubmed-meshheading:20018937-Cells, Cultured, pubmed-meshheading:20018937-Disease Models, Animal, pubmed-meshheading:20018937-Endothelium, Vascular, pubmed-meshheading:20018937-HSC70 Heat-Shock Proteins, pubmed-meshheading:20018937-Hindlimb, pubmed-meshheading:20018937-Humans, pubmed-meshheading:20018937-Ischemia, pubmed-meshheading:20018937-Male, pubmed-meshheading:20018937-Mice, pubmed-meshheading:20018937-Mice, Inbred C57BL, pubmed-meshheading:20018937-Neovascularization, Physiologic, pubmed-meshheading:20018937-Nitric Oxide Synthase Type III, pubmed-meshheading:20018937-Phosphatidylinositol 3-Kinases, pubmed-meshheading:20018937-Phosphorylation, pubmed-meshheading:20018937-Proto-Oncogene Proteins c-akt, pubmed-meshheading:20018937-Pyrrolidinones, pubmed-meshheading:20018937-Signal Transduction, pubmed-meshheading:20018937-Vascular Endothelial Growth Factor A
pubmed:year
2010
pubmed:articleTitle
Heat shock cognate protein 70 is essential for Akt signaling in endothelial function.
pubmed:affiliation
Department of Pharmacology, Osaka City University Medical School, 1-4-3 Asahi-machi, Abeno-ku, Osaka 545-8585, Japan. sio@med.osaka-cu.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't