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Membrane transport: ubiquitylation in endosomal sorting.
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Skp1p and the F-box protein Rcy1p form a non-SCF complex involved in recycling of the SNARE Snc1p in yeast.
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The yeast actin-related protein Arp2p is required for the internalization step of endocytosis.
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A yeast t-SNARE involved in endocytosis.
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Ubiquitin and endocytic internalization in yeast and animal cells.
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The F-box protein Rcy1p is involved in endocytic membrane traffic and recycling out of an early endosome in Saccharomyces cerevisiae.
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Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: crucial role of Doa4p ubiquitin isopeptidase.
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Membrane insertion of uracil permease, a polytopic yeast plasma membrane protein.
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14
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A deletion that includes the signal peptidase cleavage site impairs processing, glycosylation, and secretion of cell surface yeast acid phosphatase.
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A PEST-like sequence mediates phosphorylation and efficient ubiquitination of yeast uracil permease.
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NH4+-induced down-regulation of the Saccharomyces cerevisiae Gap1p permease involves its ubiquitination with lysine-63-linked chains.
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17
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BCMAp: an integral membrane protein in the Golgi apparatus of human mature B lymphocytes.
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18
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Casein kinase I-dependent phosphorylation within a PEST sequence and ubiquitination at nearby lysines signal endocytosis of yeast uracil permease.
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Localization of the Rsp5p ubiquitin-protein ligase at multiple sites within the endocytic pathway.
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A novel EH domain protein of Saccharomyces cerevisiae, Ede1p, involved in endocytosis.
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The yeast plasma membrane uracil permease is stabilized against stress induced degradation by a point mutation in a cyclin-like "destruction box".
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In vitro biosynthesis and membrane insertion of gamma-glutamyl transpeptidase.
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The HECT ubiquitin ligase Rsp5p is required for proper nuclear export of mRNA in Saccharomyces cerevisiae.
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Replacement of Lys by Glu in a transmembrane segment strongly impairs the function of the uracil permease from Saccharomyces cerevisiae.
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Membrane topology of the yeast uracil permease.
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The novel protein Ccz1p required for vacuolar assembly in Saccharomyces cerevisiae functions in the same transport pathway as Ypt7p.
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The yeast acid phosphatase can enter the secretory pathway without its N-terminal signal sequence.
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'ER degradation' of a mutant yeast plasma membrane protein by the ubiquitin-proteasome pathway.
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Unmasking of an essential thiol during function of the membrane bound enzyme II of the phosphoenolpyruvate glucose phosphotransferase system of Escherichia coli.
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A deletion that includes the segment coding for the signal peptidase cleavage site delays release of Saccharomyces cerevisiae acid phosphatase from the endoplasmic reticulum.
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Changes in accessibility of the membrane bound transport enzyme glucose phosphotransferase of E. coli to protein group reagents in presence of substrate or absence of energy source.
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Different sidedness of functionally homologous essential thiols in two membrane-bound phosphotransferase enzymes of Escherichia coli detected by permeant and nonpermeant thiol reagents.
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Endocytose and degradation of the uracil permease of S. cerevisiae under stress conditions: possible role of ubiquitin.
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Solubilization by proteolysis of an activated form of rat liver membrane guanylate cyclase.
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Trypsin solubilization of rat liver membrane-bound guanylate cyclase results in a form kinetically distinct from the cytosolic enzyme.
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Functional analysis of the signal-sequence processing site of yeast acid phosphatase.
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In vivo translocation of the cell wall acid phosphatase across the yeast endoplasmic reticulum membrane: are there multiple signals for the targeting process?
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The role of enzyme I in the unmasking of an essential thiol of the membrane-bound enzyme II of the phosphoenolpyruvate-glucose phosphotransferase system of Escherichia coli.
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Unmasking of an essential thiol during function of the membrane-bound enzyme II of the phosphenolpyruvate beta-glucoside phosphotransferase system of Escherichia coli.
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Disruption of six novel genes from the left arm of chromosome XV of Saccharomyces cerevisiae and basic phenotypic analysis of the generated mutants.
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