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AUT3, a serine/threonine kinase gene, is essential for autophagocytosis in Saccharomyces cerevisiae
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scholarly article
1 reference
stated in
PubMed
PubMed ID
9190802
retrieved
1 December 2016
title
AUT3, a serine/threonine kinase gene, is essential for autophagocytosis in Saccharomyces cerevisiae
(English)
1 reference
stated in
PubMed
PubMed ID
9190802
retrieved
1 December 2016
main subject
Saccharomyces cerevisiae
0 references
Serine/threonine protein kinase ATG1 YGL180W
1 reference
stated in
GOA release 2020-03-11
author name string
M Straub
series ordinal
1
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M Bredschneider
series ordinal
2
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M Thumm
series ordinal
3
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language of work or name
English
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publication date
June 1997
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published in
Journal of Bacteriology
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stated in
PubMed
PubMed ID
9190802
retrieved
1 December 2016
volume
179
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page(s)
3875-83
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issue
12
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cites work
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A receptor for the selective uptake and degradation of proteins by lysosomes
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end3 and end4: two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae
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Vesicle-mediated protein transport: regulatory interactions between the Vps15 protein kinase and the Vps34 PtdIns 3-kinase essential for protein sorting to the vacuole in yeast
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Lysosomal (vacuolar) proteinases of yeast are essential catalysts for protein degradation, differentiation, and cell survival
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Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase
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Aminopeptidase I of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway
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New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
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Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway
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Yeast endocytosis
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PubMed Central
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Autophagy and related mechanisms of lysosome-mediated protein degradation
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Receptor-mediated protein sorting to the vacuole in yeast: roles for a protein kinase, a lipid kinase and GTP-binding proteins
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Ultrastructural analysis of the autophagic process in yeast: detection of autophagosomes and their characterization
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Caenorhabditis elegans unc-51 gene required for axonal elongation encodes a novel serine/threonine kinase.
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The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases
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PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors
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Studies on the mechanisms of autophagy: maturation of the autophagic vacuole
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2 June 2018
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Analysis of mitochondrial protein import pathway in Saccharomyces cerevisiae with translocation intermediates
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Tracing intracellular proteolytic pathways. Proteolysis of fatty acid synthase and other cytoplasmic proteins in the yeast Saccharomyces cerevisiae
1 reference
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https://pubmed.ncbi.nlm.nih.gov/9190802
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12 December 2020
based on heuristic
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Immunocytochemical study of the surrounding envelope of autophagic vacuoles in cultured rat hepatocytes
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9190802
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
64 Yeast secretory mutants: Isolation and characterization
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9190802
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Membrane markers of endoplasmic reticulum preserved in autophagic vacuolar membranes isolated from leupeptin-administered rat liver
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9190802
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9190802
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Endocytosis in yeast: Several of the yeast secretory mutants are defective in endocytosis
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9190802
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/JB.179.12.3875-3883.1997
0 references
OpenCitations bibliographic resource ID
1291488
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1291488
PMCID
179195
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1291488
PubMed ID
9190802
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1291488
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