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Sec59 encodes a membrane protein required for core glycosylation in Saccharomyces cerevisiae
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
2657387
retrieved
1 December 2016
title
Sec59 encodes a membrane protein required for core glycosylation in Saccharomyces cerevisiae
(English)
1 reference
stated in
PubMed
PubMed ID
2657387
retrieved
1 December 2016
main subject
Saccharomyces cerevisiae
0 references
dolichol kinase, putative
1 reference
stated in
GeneDB
retrieved
6 February 2019
dolichol kinase, putative
1 reference
stated in
GeneDB
retrieved
6 February 2019
dolichol kinase, putative
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dolichol kinase, putative
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dolichol kinase, putative
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dolichol kinase, putative
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Dolichol kinase YMR013C
1 reference
stated in
GOA release 2020-03-11
glycosylation
1 reference
based on heuristic
inferred from title
membrane protein
1 reference
based on heuristic
inferred from title
author
Randy Schekman
series ordinal
3
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author name string
M Bernstein
series ordinal
1
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F Kepes
series ordinal
2
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language of work or name
English
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publication date
March 1989
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published in
Molecular and Cellular Biology
1 reference
stated in
PubMed
PubMed ID
2657387
retrieved
1 December 2016
volume
9
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page(s)
1191-9
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issue
3
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cites work
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Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole
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Yeast mutants deficient in protein glycosylation
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Genes required for completion of import of proteins into the endoplasmic reticulum in yeast
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Transformation of intact yeast cells treated with alkali cations
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Characterization of a gene product (Sec53p) required for protein assembly in the yeast endoplasmic reticulum
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The histidine permease gene (HIP1) of Saccharomyces cerevisiae
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The yeast SEC53 gene encodes phosphomannomutase.
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SEC11 is required for signal peptide processing and yeast cell growth
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DNA sequencing with chain-terminating inhibitors
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Two differentially regulated mRNAs with different 5' ends encode secreted with intracellular forms of yeast invertase
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A Critical Evaluation of the Nitrogen Assimilation Tests Commonly Used in the Classification of Yeasts.
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Protein localization and membrane traffic in yeast
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Invertase signal and mature sequence substitutions that delay intercompartmental transport of active enzyme
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Secretory protein translocation in a yeast cell-free system can occur posttranslationally and requires ATP hydrolysis
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Coincident localization of secretory and plasma membrane proteins in organelles of the yeast secretory pathway
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Studies on the microsomal electron-transport system of anaerobically grown yeast. V. Purification and characterization of NADPH-cytochrome c reductase
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Molecular characterization of the CAN1 locus in Saccharomyces cerevisiae. A transmembrane protein without N-terminal hydrophobic signal sequence.
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1 reference
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PubMed
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Transmembrane movement of oligosaccharide-lipids during glycoprotein synthesis
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1 reference
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Early steps in processing of yeast glycoproteins
1 reference
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reference URL
https://pubmed.ncbi.nlm.nih.gov/2657387
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Glycosylation and processing of prepro-alpha-factor through the yeast secretory pathway
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/2657387
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Product of SEC53 is required for folding and glycosylation of secretory proteins in the lumen of the yeast endoplasmic reticulum
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/2657387
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
In vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent posttranslational translocation of the prepro-alpha-factor
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/2657387
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/MCB.9.3.1191
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PMCID
362710
0 references
PubMed ID
2657387
1 reference
stated in
PubMed
PubMed ID
2657387
retrieved
1 December 2016
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