Source:http://linkedlifedata.com/resource/pubmed/id/17618624
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
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pubmed:dateCreated |
2007-7-19
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pubmed:abstractText |
Autophagy depends on the activity of phosphoinositide-3 kinase class III to generate PI(3)P. We identified the human WIPI protein family of PI(3)P-binding factors and showed that WIPI-1 (Atg18) is linked to autophagy in human cells. Induction of autophagy by rapamycin, gleevec, thapsigargin and amino acid deprivation led to an accumulation of WIPI-1 at LC3-positive membrane structures (WIPI-1 puncta-formation), suggested to represent autophagosomal isolation membranes. WIPI-1 puncta-formation is inhibited by wortmannin and LY294002, and PI(3)P-binding-deficient WIPI-1 is puncta-formation-incompetent. Quantification of WIPI-1 puncta should be suitable to assay mammalian autophagy.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
581
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3396-404
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:17618624-Amino Acid Sequence,
pubmed-meshheading:17618624-Autophagy,
pubmed-meshheading:17618624-Carrier Proteins,
pubmed-meshheading:17618624-Cell Line, Tumor,
pubmed-meshheading:17618624-Cell Membrane,
pubmed-meshheading:17618624-Genes, Reporter,
pubmed-meshheading:17618624-Humans,
pubmed-meshheading:17618624-Microscopy, Electron, Transmission,
pubmed-meshheading:17618624-Microscopy, Immunoelectron,
pubmed-meshheading:17618624-Molecular Sequence Data,
pubmed-meshheading:17618624-Mutation,
pubmed-meshheading:17618624-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:17618624-Protein Binding,
pubmed-meshheading:17618624-Sirolimus
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pubmed:year |
2007
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pubmed:articleTitle |
Human WIPI-1 puncta-formation: a novel assay to assess mammalian autophagy.
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pubmed:affiliation |
Autophagy Laboratory, Department of Molecular Biology, University of Tuebingen, Auf der Morgenstelle 15, 72076 Tuebingen, Germany. tassula.proikas-cezanne@uni-tuebingen.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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