Linked Life Data

9822578

Source:http://linkedlifedata.com/resource/pubmed/id/9822578

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
1998-12-14
pubmed:abstractText
The kinase Tor is the target of the immunosuppressive drug rapamycin and is a member of the phosphatidylinositol kinase (PIK)-related kinase family. It plays an essential role in progression through the G1 phase of the cell cycle. The molecular details of Tor signaling remain obscure, however.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/14-3-3 Proteins, http://linkedlifedata.com/resource/pubmed/chemical/BMH1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/BMH2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Immunophilins, http://linkedlifedata.com/resource/pubmed/chemical/Ligands, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group..., http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sirolimus, http://linkedlifedata.com/resource/pubmed/chemical/TOR1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Tacrolimus Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine 3-Monooxygenase
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0960-9822
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1259-67
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:9822578-14-3-3 Proteins, pubmed-meshheading:9822578-Binding Sites, pubmed-meshheading:9822578-Drug Resistance, Microbial, pubmed-meshheading:9822578-Enzyme Inhibitors, pubmed-meshheading:9822578-Female, pubmed-meshheading:9822578-Fungal Proteins, pubmed-meshheading:9822578-Genes, Fungal, pubmed-meshheading:9822578-Humans, pubmed-meshheading:9822578-Immunophilins, pubmed-meshheading:9822578-Ligands, pubmed-meshheading:9822578-Phosphatidylinositol 3-Kinases, pubmed-meshheading:9822578-Phosphoserine, pubmed-meshheading:9822578-Phosphotransferases (Alcohol Group Acceptor), pubmed-meshheading:9822578-Proteins, pubmed-meshheading:9822578-Saccharomyces cerevisiae, pubmed-meshheading:9822578-Saccharomyces cerevisiae Proteins, pubmed-meshheading:9822578-Signal Transduction, pubmed-meshheading:9822578-Sirolimus, pubmed-meshheading:9822578-Tacrolimus Binding Proteins, pubmed-meshheading:9822578-Tyrosine 3-Monooxygenase
pubmed:year
1998
pubmed:articleTitle
The 14-3-3 proteins positively regulate rapamycin-sensitive signaling.
pubmed:affiliation
Department of Pathology Washington University School of Medicine St. Louis, Missouri, 63110, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't