Zobrazeno 1 - 10 of 17 pro vyhledávání: '"S F Nothwehr"'
1
The yeast VPS5/GRD2 gene encodes a sorting nexin-1-like protein required for localizing membrane proteins to the late Golgi
Autor: S F, Nothwehr, A E, Hindes
Publikováno v: Journal of Cell Science. 110:1063-1072
Genetic analysis of late Golgi membrane protein localization in Saccharomyces cerevisiae has uncovered a large number of genes (called GRD) that are required for retention of A-ALP, a model late Golgi membrane protein. Here we describe one of the GRD
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f285d647c0db2172b509dd7c188642c2
https://doi.org/10.1242/jcs.110.9.1063
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2
The Newly Identified Yeast GRD Genes Are Required for Retention of Late-Golgi Membrane Proteins
Autor: S F Nothwehr, Tom H. Stevens, Nia J. Bryant
Publikováno v: Scopus-Elsevier
Processing of A-ALP, a late-Golgi membrane protein constructed by fusing the cytosolic domain of dipeptidyl aminopeptidase A to the transmembrane and lumenal domains of alkaline phosphatase (ALP), serves as a convenient assay for loss of retention of
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::feb690317edb876f8b80b37bbdd83c2b
https://doi.org/10.1128/mcb.16.6.2700
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4
Membrane protein retention in the yeast Golgi apparatus: dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues
Autor: S F Nothwehr, Tom H. Stevens, Christopher J. Roberts
Publikováno v: The Journal of Cell Biology
The mechanism by which yeast dipeptidyl aminopeptidase (DPAP) A, type II integral membrane protein, is retained in the late Golgi apparatus has been investigated. Prior work demonstrated that the 118-amino acid cytoplasmic domain is both necessary an
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c314438b7d56a5f915ec439f2f015e3
https://doi.org/10.1083/jcb.121.6.1197
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5
Membrane protein sorting in the yeast secretory pathway: evidence that the vacuole may be the default compartment
Autor: S F Nothwehr, Christopher J. Roberts, Tom H. Stevens
Publikováno v: The Journal of Cell Biology
The targeting signals of two yeast integral membrane dipeptidyl aminopeptidases (DPAPs), DPAP B and DPAP A, which reside in the vacuole and the Golgi apparatus, respectively, were analyzed. No single domain of DPAP B is required for delivery to the v
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d06e15c508970a027805d9ebb3fd5134
http://europepmc.org/articles/PMC2289628
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6
Structural features in the NH2-terminal region of a model eukaryotic signal peptide influence the site of its cleavage by signal peptidase
Autor: S F Nothwehr, J I Gordon
Publikováno v: Journal of Biological Chemistry. 265:17202-17208
The 20-amino acid signal peptide of human pre (delta pro)apolipoprotein A-II contains the tripartite domain structure typical of eukaryotic prepeptides, i.e. a positively charged NH2-terminal (n) region, a hydrophobic core (h) region, and a COOH-term
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ba73d39bcb832647e7a9324c9f3171a3
https://doi.org/10.1016/s0021-9258(17)44889-7
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7
Compartmentalization of mammalian proteins produced in Escherichia coli
Autor: P O Olins, Kristin A. Hogquist, T A Rosenwasser, S Bradford-Goldberg, Jeffrey I. Gordon, David D. Chaplin, S F Nothwehr
Publikováno v: Journal of Biological Chemistry. 265:13066-13073
We have examined the patterns of compartmentalization of several mammalian proteins in Escherichia coli which do not have signal peptides or functional signal peptide equivalents. These proteins include (i) human proapolipoprotein A-I (proapoA-I), a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1070bfa732cfbddc103f09b72f7984ab
https://doi.org/10.1016/s0021-9258(19)38268-7
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9
Structural features in the NH2-terminal region of a model eukaryotic signal peptide influence the site of its cleavage by signal peptidase
Autor: S F, Nothwehr, J I, Gordon
Publikováno v: The Journal of biological chemistry. 265(28)
The 20-amino acid signal peptide of human pre (delta pro)apolipoprotein A-II contains the tripartite domain structure typical of eukaryotic prepeptides, i.e. a positively charged NH2-terminal (n) region, a hydrophobic core (h) region, and a COOH-term
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::25afcf15790df53baf3f407b38df3320
https://pubmed.ncbi.nlm.nih.gov/2120214
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10
Compartmentalization of mammalian proteins produced in Escherichia coli
Autor: T A, Rosenwasser, K A, Hogquist, S F, Nothwehr, S, Bradford-Goldberg, P O, Olins, D D, Chaplin, J I, Gordon
Publikováno v: The Journal of biological chemistry. 265(22)
We have examined the patterns of compartmentalization of several mammalian proteins in Escherichia coli which do not have signal peptides or functional signal peptide equivalents. These proteins include (i) human proapolipoprotein A-I (proapoA-I), a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2eacb657637cc7b8eb769e6d66044866
https://pubmed.ncbi.nlm.nih.gov/2115888
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