%D8%B1%D8%A7%D9%86%D8%AF%D9%8A_%D8%B4%D9%8A%D9%83%D9%85%D8%A7%D9%86%D8%B1%D9%86%D8%AF%DB%8C_%D8%B4%DA%A9%D9%85%D9%86%D0%A0%D1%8D%D0%BD%D0%B4%D0%B7%D1%96_%D0%A8%D1%8D%D0%BA%D0%BC%D1%8D%D0%BD%D0%A0%D0%B0%D0%BD%D0%B4%D0%B8_%D0%A8%D0%B5%D0%BA%D0%BC%D0%B0%D0%BD%E0%A6%B0%E2%80%8D%E0%A7%8D%E0%A6%AF%E0%A6%BE%E0%A6%A8%E0%A7%8D%E0%A6%A1%E0%A6%BF_%E0%A6%93%E0%A6%AF%E0%A6%BC%E0%A7%87%E0%A6%87%E0%A6%A8_%E0%A6%B6%E0%A7%87%E0%A6%95%E0%A6%AE%E0%A7%8D%E0%A6%AF%E0%A6%BE%E0%A6%A8Category:Randy_SchekmanRandy_SchekmanRandy_SchekmanRandy_SchekmanRandy_Schekman%D8%B1%D9%86%D8%AF%DB%8C_%D8%B4%DA%A9%D9%85%D9%86Randy_SchekmanRandy_SchekmanRandy_Schekman%D7%A8%D7%A0%D7%93%D7%99_%D7%A9%D7%A7%D7%9E%D7%9F%E0%A4%B0%E0%A5%88%E0%A4%82%E0%A4%A1%E0%A5%80_%E0%A4%B6%E0%A5%87%E0%A4%95%E0%A4%AE%E0%A5%88%E0%A4%A8Randy_SchekmanRandy_SchekmanRandy_Wayne_SchekmanRandy_Schekman%E3%83%A9%E3%83%B3%E3%83%87%E3%82%A3%E3%83%BB%E3%82%B7%E3%82%A7%E3%82%AF%E3%83%9E%E3%83%B3%D0%A0%D1%8D%D0%BD%D0%B4%D0%B8_%D0%A8%D0%B5%D0%BA%D0%BC%D0%B0%D0%BD%EB%9E%9C%EB%94%94_%EC%85%B0%ED%81%AC%EB%A8%BCRandy_Schekman%E0%B4%B1%E0%B4%BE%E0%B5%BB%E0%B4%A1%E0%B4%BF_%E0%B4%A1%E0%B4%AC%E0%B5%8D%E0%B4%B2%E0%B5%8D%E0%B4%AF%E0%B5%82_%E0%B4%B7%E0%B5%86%E0%B4%95%E0%B5%8D%E0%B4%95%E0%B5%8D%E0%B4%AE%E0%B4%BE%E0%B5%BBRandy_SchekmanRandy_Wayne_SchekmanRandy_SchekmanRandy_W._SchekmanRandy_SchekmanRandy_Schekman%D8%B1%DB%8C%D9%86%DA%88%DB%8C_%D8%B4%DB%8C%DA%A9%D9%85%D8%A7%D9%86Randy_SchekmanRandy_Schekman%D0%A8%D0%B5%D0%BA%D0%BC%D0%B0%D0%BD,_%D0%A0%D1%8D%D0%BD%D0%B4%D0%B8Randy_Schekman%E0%B6%BB%E0%B7%90%E0%B6%B1%E0%B7%8A%E0%B6%A9%E0%B7%92_%E0%B7%82%E0%B7%99%E0%B6%9A%E0%B7%8A%E0%B6%B8%E0%B6%B1%E0%B7%8ARandy_SchekmanRandy_SchekmanRandy_Schekman
about
P185
Reforming research assessmentGuidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)Ubiquitin-dependent regulation of COPII coat size and functionCloning and functional characterization of mammalian homologues of the COPII component Sec23TANGO1 facilitates cargo loading at endoplasmic reticulum exit sitesRole of Vma21p in assembly and transport of the yeast vacuolar ATPaseA year in the life of eLifeSEC11 is required for signal peptide processing and yeast cell growthThe nine lives of Daniel E. Koshland, Jr. (1920-2007)The structure of the COPII transport-vesicle coat assembled on membranesDifferential trafficking and timed localization of two chitin synthase proteins, Chs2p and Chs3pActin from Saccharomyces cerevisiaeSec59 encodes a membrane protein required for core glycosylation in Saccharomyces cerevisiaeSec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex.Pho86p, an endoplasmic reticulum (ER) resident protein in Saccharomyces cerevisiae, is required for ER exit of the high-affinity phosphate transporter Pho84p.Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation.The yeast SEC17 gene product is functionally equivalent to mammalian alpha-SNAP protein.COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum.The yeast SEC53 gene encodes phosphomannomutase.A membrane glycoprotein, Sec12p, required for protein transport from the endoplasmic reticulum to the Golgi apparatus in yeast.Surface structure of the COPII-coated vesicle.Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum.Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway.Cytosolic Sec13p complex is required for vesicle formation from the endoplasmic reticulum in vitro.The engagement of Sec61p in the ER dislocation process.Avl9p, a member of a novel protein superfamily, functions in the late secretory pathway.Genes required for completion of import of proteins into the endoplasmic reticulum in yeast.Order of events in the yeast secretory pathway.The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins.Yeast beta- and beta'-coat proteins (COP). Two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein traffic.Reconstitution of retrograde transport from the Golgi to the ER in vitro.SEC21 is a gene required for ER to Golgi protein transport that encodes a subunit of a yeast coatomer.Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle.Chs1p and Chs3p, two proteins involved in chitin synthesis, populate a compartment of the Saccharomyces cerevisiae endocytic pathway.BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum.Characterization of a gene product (Sec53p) required for protein assembly in the yeast endoplasmic reticulumepsilon-COP is a structural component of coatomer that functions to stabilize alpha-COPSec16p potentiates the action of COPII proteins to bud transport vesiclesExpression, purification, and assay of Sec12p: a Sar1p-specific GDP dissociation stimulator.Concentrative sorting of secretory cargo proteins into COPII-coated vesicles.
P50
description
Amerikaans biochemicus
@nl
Nobel prize winning American cell biologist
@en
amerikanischer Biochemiker
@de
biologiste cellulaire américain
@fr
biologo statunitense
@it
biólogo celular e investigador científico estadounidense
@es
dokter asal Amerika Serikat
@id
nobelprisvinner i medisin 2013
@nb
নোবেলজয়ী মার্কিন কোষবিজ্ঞানী
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Randy Schekman
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Randy Schekman
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Randy Schekman
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Randy Schekman
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Randy Schekman
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Randy Schekman
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Randy Schekman
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Randy Schekman
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Randy Schekman
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Randy Schekman
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Randy Schekman
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R Schekman
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R W Schekman
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R. Schekman
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R. W. Schekman
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Randy W Schekman
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Randy W. Schekman
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Randy Wayne Schekman
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Randy Wayne Schekman
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Randy Wayne Schekman
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Randy Wayne Schekman
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Randy Schekman
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Randy Schekman
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