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Lam6 Regulates the Extent of Contacts between Organelles
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
26119743
retrieved
1 December 2016
title
Lam6 Regulates the Extent of Contacts between Organelles
(English)
1 reference
stated in
PubMed
PubMed ID
26119743
retrieved
1 December 2016
main subject
Lam6p YLR072W
1 reference
stated in
GOA release 2020-03-11
author
Nils Wiedemann
series ordinal
6
0 references
Maya Schuldiner
series ordinal
8
0 references
Michal Eisenberg-Bord
series ordinal
2
0 references
author name string
Yael Elbaz-Alon
series ordinal
1
0 references
Vera Shinder
series ordinal
3
0 references
Sebastian Berthold Stiller
series ordinal
4
0 references
Eyal Shimoni
series ordinal
5
0 references
Tamar Geiger
series ordinal
7
0 references
language of work or name
English
0 references
publication date
7 July 2015
0 references
published in
Cell Reports
1 reference
stated in
PubMed
PubMed ID
26119743
retrieved
1 December 2016
volume
12
0 references
issue
1
0 references
page(s)
7-14
0 references
cites work
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Ltc1 is an ER-localized sterol transporter and a component of ER-mitochondria and ER-vacuole contacts
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Membrane contact sites, gateways for lipid homeostasis
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A dynamic interface between vacuoles and mitochondria in yeast
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Cellular metabolism regulates contact sites between vacuoles and mitochondria
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PubMed Central
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The conserved GTPase Gem1 regulates endoplasmic reticulum-mitochondria connections
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An ER-mitochondria tethering complex revealed by a synthetic biology screen
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Nucleus-vacuole junctions in Saccharomyces cerevisiae are formed through the direct interaction of Vac8p with Nvj1p
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Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
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Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications
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GRAM, a novel domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins
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Staying in touch: the molecular era of organelle contact sites
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Yeast transformation by the LiAc/SS Carrier DNA/PEG method
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Application of cryoultramicrotomy to immunocytochemistry
1 reference
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reference URL
https://pubmed.ncbi.nlm.nih.gov/26119743
retrieved
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based on heuristic
inferred from PubMed ID database lookup
Reconstitution of transport from endoplasmic reticulum to Golgi complex using endoplasmic reticulum-enriched membrane fraction from yeast
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/26119743
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1016/J.CELREP.2015.06.022
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2171845
OpenCitations bibliographic resource ID
2171845
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2171845
PMCID
4518459
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2171845
PubMed ID
26119743
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2171845
ResearchGate publication ID
279631783
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