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Tracing putative trafficking of the glycolytic enzyme enolase via SNARE-driven unconventional secretion
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scholarly article
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PubMed
PubMed ID
22753847
retrieved
1 December 2016
title
Tracing putative trafficking of the glycolytic enzyme enolase via SNARE-driven unconventional secretion
(English)
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PubMed
PubMed ID
22753847
retrieved
1 December 2016
main subject
Tlg2p YOL018C
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GOA release 2020-03-11
author name string
Natsuko Miura
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1
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Aya Kirino
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2
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Satoshi Endo
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3
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Hironobu Morisaka
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4
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Kouichi Kuroda
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5
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Masahiro Takagi
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6
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Mitsuyoshi Ueda
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7
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language of work or name
English
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publication date
August 2012
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published in
Eukaryotic Cell
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PubMed
PubMed ID
22753847
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1 December 2016
volume
11
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issue
8
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page(s)
1075-82
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Europe PubMed Central
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11 June 2022
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https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3416056/fullTextXML
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ImageJ
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Europe PubMed Central
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11 June 2022
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https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3416056/fullTextXML
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Enolase takes part in a macromolecular complex associated to mitochondria in yeast.
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Genetic and proteomic evidences support the localization of yeast enolase in the cell surface
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Cytoplasm to vacuole trafficking of aminopeptidase I requires a t-SNARE-Sec1p complex composed of Tlg2p and Vps45p
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The glycolytic enzymes glyceraldehyde 3-phosphate dehydrogenase and enolase interact with the renal epithelial K+ channel ROMK2 and regulate its function
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Nonclassical protein secretion by Bacillus subtilis in the stationary phase is not due to cell lysis
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Enolase: a key player in the metabolism and a probable virulence factor of trypanosomatid parasites-perspectives for its use as a therapeutic target.
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Unconventional secretion: a stress on GRASP.
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α-Enolase: a promising therapeutic and diagnostic tumor target.
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Comparison of the surface coat proteins of the pine wood nematode appeared during host pine infection and in vitro culture by a proteomic approach
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Enolase, a cellular glycolytic enzyme, is required for efficient transcription of Sendai virus genome.
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27 November 2018
Autocrine motility factor enhances hepatoma cell invasion across the basement membrane through activation of beta1 integrins
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27 November 2018
Enolase is present in the cell wall of Saccharomyces cerevisiae
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/22753847
retrieved
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inferred from PubMed ID database lookup
Function of the prosequence for in vivo folding and secretion of active Rhizopus oryzae lipase in Saccharomyces cerevisiae
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/22753847
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Secretory pathway kinetics and in vivo analysis of protein traffic from the Golgi complex to the cell surface
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/22753847
retrieved
12 December 2020
based on heuristic
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Non-conventional protein secretionin yeast
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/22753847
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Anti-enolase antibodies partially protective against systemic candidiasis in mice
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/22753847
retrieved
12 December 2020
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Identifiers
DOI
10.1128/EC.00075-12
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PubMed
PubMed ID
22753847
retrieved
1 December 2016
Fatcat ID
release_aheu67tu6vachjlu47c4qlgmdm
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Fatcat
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https://api.fatcat.wiki/v0/release/aheu67tu6vachjlu47c4qlgmdm
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24 November 2022
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PMCID
3416056
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PubMed ID
22753847
1 reference
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PubMed
PubMed ID
22753847
retrieved
1 December 2016
ResearchGate publication ID
228105632
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