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WFRF:(Vanselow Katja)
 

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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003072naa a2200505 4500
001oai:DiVA.org:kth-93008
003SwePub
008120410s2012 | |||||||||||000 ||eng|
024a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-930082 URI
024a https://doi.org/10.1074/mcp.M111.0140352 DOI
040 a (SwePub)kth
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Dengjel, Joern4 aut
2451 0a Identification of Autophagosome-associated Proteins and Regulators by Quantitative Proteomic Analysis and Genetic Screens
264 1c 2012
338 a print2 rdacarrier
500 a QC 20120411
520 a Autophagy is one of the major intracellular catabolic pathways, but little is known about the composition of autophagosomes. To study the associated proteins, we isolated autophagosomes from human breast cancer cells using two different biochemical methods and three stimulus types: amino acid deprivation or rapamycin or concanamycin A treatment. The autophagosome- associated proteins were dependent on stimulus, but a core set of proteins was stimulus- independent. Remarkably, proteasomal proteins were abundant among the stimulus- independent common autophagosome- associated proteins, and the activation of autophagy significantly decreased the cellular proteasome level and activity supporting interplay between the two degradation pathways. A screen of yeast strains defective in the orthologs of the human genes encoding for a common set of autophagosome- associated proteins revealed several regulators of autophagy, including subunits of the retromer complex. The combined spatiotemporal proteomic and genetic data sets presented here provide a basis for further characterization of autophagosome biogenesis and cargo selection.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
700a Hoyer-Hansen, Maria4 aut
700a Nielsen, Maria O.4 aut
700a Eisenberg, Tobias4 aut
700a Harder, Lea M.4 aut
700a Schandorff, Soren4 aut
700a Farkas, Thomas4 aut
700a Kirkegaard, Thomas4 aut
700a Becker, Andrea C.4 aut
700a Schroeder, Sabrina4 aut
700a Vanselow, Katja4 aut
700a Lundberg, Emmau KTH,Proteomik,Science for Life Laboratory, SciLifeLab4 aut0 (Swepub:kth)u12bylj1
700a Nielsen, Mogens M.4 aut
700a Kristensen, Anders R.4 aut
700a Akimov, Vyacheslav4 aut
700a Bunkenborg, Jakob4 aut
700a Madeo, Frank4 aut
700a Jaattela, Marja4 aut
700a Andersen, Jens S.4 aut
710a KTHb Proteomik4 org
773t Molecular & Cellular Proteomicsg 11:3q 11:3x 1535-9476x 1535-9484
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-93008
8564 8u https://doi.org/10.1074/mcp.M111.014035

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