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Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae
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scholarly article
1 reference
stated in
PubMed
PubMed ID
9199164
retrieved
1 December 2016
title
Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae
(English)
1 reference
stated in
PubMed
PubMed ID
9199164
retrieved
1 December 2016
main subject
Saccharomyces cerevisiae
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Amino acid permease GAP1 YKR039W
1 reference
stated in
GOA release 2020-03-11
membrane proteins
1 reference
based on heuristic
inferred from title
author name string
K J Roberg
series ordinal
1
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N Rowley
series ordinal
2
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C A Kaiser
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3
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language of work or name
English
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publication date
30 June 1997
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published in
Journal of Cell Biology
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stated in
PubMed
PubMed ID
9199164
retrieved
1 December 2016
volume
137
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page(s)
1469-82
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issue
7
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describes a project that uses
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stated in
Europe PubMed Central
retrieved
11 June 2022
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/PMC2137817/fullTextXML
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inferred from PubMed Central ID database lookup
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Targeting of the yeast plasma membrane [H+]ATPase: a novel gene AST1 prevents mislocalization of mutant ATPase to the vacuole
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Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane
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Order of events in the yeast secretory pathway
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The histidine permease gene (HIP1) of Saccharomyces cerevisiae
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SHR3: a novel component of the secretory pathway specifically required for localization of amino acid permeases in yeast.
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Transcriptional and posttranslational regulation of the general amino acid permease of Saccharomyces cerevisiae
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Golgi and vacuolar membrane proteins reach the vacuole in vps1 mutant yeast cells via the plasma membrane.
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Parallel secretory pathways to the cell surface in yeast
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Vacuolar biogenesis in yeast: sorting out the sorting proteins.
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29 September 2017
Protein transport to the yeast vacuole
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PubMed Central
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Proline transport in Saccharomyces cerevisiae.
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PEP4 gene function is required for expression of several vacuolar hydrolases in Saccharomyces cerevisiae
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Ammonia regulation of amino acid permeases in Saccharomyces cerevisiae
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Multiplicity of the Amino Acid Permeases in Saccharomyces cerevisiae IV. Evidence for a General Amino Acid Permease
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29 September 2017
Nucleotide sequence of the Saccharomyces cerevisiae PUT4 proline-permease-encoding gene: similarities between CAN1, HIP1 and PUT4 permeases
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29 September 2017
Topography of glycosylation in yeast: characterization of GDPmannose transport and lumenal guanosine diphosphatase activities in Golgi-like vesicles
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29 September 2017
Membrane insertion of uracil permease, a polytopic yeast plasma membrane protein
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29 September 2017
Membrane protein sorting in the yeast secretory pathway: evidence that the vacuole may be the default compartment
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PubMed Central
reference URL
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29 September 2017
Cloning and sequencing of the Saccharomyces cerevisiae gene LYP1 coding for a lysine-specific permease
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PubMed Central
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2 June 2018
Substrate specificities of active transport systems for amino acids in vacuolar-membrane vesicles of Saccharomyces cerevisiae. Evidence of seven independent proton/amino acid antiport systems
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2 June 2018
Molecular characterization of the CAN1 locus in Saccharomyces cerevisiae. A transmembrane protein without N-terminal hydrophobic signal sequence.
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2 June 2018
GAP1, the general amino acid permease gene of Saccharomyces cerevisiae. Nucleotide sequence, protein similarity with the other bakers yeast amino acid permeases, and nitrogen catabolite repression
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2 June 2018
Active transport of basic amino acids driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9199164
retrieved
12 December 2020
based on heuristic
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Amino acid transport in eucaryotic microorganisms
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9199164
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Stimulation-associated redistribution of H+-K+-ATPase activity in isolated gastric glands
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9199164
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Endocytosis and degradation of the yeast uracil permease under adverse conditions
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9199164
retrieved
12 December 2020
based on heuristic
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Identifiers
DOI
10.1083/JCB.137.7.1469
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PMCID
2137817
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PubMed ID
9199164
1 reference
stated in
PubMed
PubMed ID
9199164
retrieved
1 December 2016
ResearchGate publication ID
274436711
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