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Functional implications of mitofusin 2-mediated mitochondrial-SR tethering
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title
Functional implications of mitofusin 2-mediated mitochondrial-SR tethering
(English)
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author name string
Gerald W. Dorn
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1
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Moshi Song
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2
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Kenneth Walsh
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3
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language of work or name
English
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publication date
January 2015
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published in
Journal of Molecular and Cellular Cardiology
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volume
78
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PubMed
page(s)
123-8
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PubMed
cites work
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PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria
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Mitofusin 2 tethers endoplasmic reticulum to mitochondria
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Mitofusin 2 in POMC neurons connects ER stress with leptin resistance and energy imbalance.
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Mitofusin-2 maintains mitochondrial structure and contributes to stress-induced permeability transition in cardiac myocytes
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Endocardial cushion and myocardial defects after cardiac myocyte-specific conditional deletion of the bone morphogenetic protein receptor ALK3
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28 September 2017
Rapid changes of mitochondrial Ca2+ revealed by specifically targeted recombinant aequorin
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28 September 2017
Mitofusin 2-containing mitochondrial-reticular microdomains direct rapid cardiomyocyte bioenergetic responses via interorganelle Ca(2+) crosstalk
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Elevated cytosolic Na+ decreases mitochondrial Ca2+ uptake during excitation-contraction coupling and impairs energetic adaptation in cardiac myocytes
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31 May 2018
Mitofusin 2 is necessary for striatal axonal projections of midbrain dopamine neurons.
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28 November 2018
Mitochondrial fusion protects against neurodegeneration in the cerebellum.
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28 November 2018
The mitochondrial calcium uniporter is a highly selective ion channel.
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Spatially and functionally distinct Ca2+ stores in sarcoplasmic and endoplasmic reticulum
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7 January 2021
Mitochondrial fusion directs cardiomyocyte differentiation via calcineurin and Notch signaling
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7 January 2021
The Ca2+-induced membrane transition in mitochondria
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Crossref
reference URL
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retrieved
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Identifiers
DOI
10.1016/J.YJMCC.2014.09.015
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2853986
OpenCitations bibliographic resource ID
2853986
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2853986
PMC publication ID
4268321
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2853986
PubMed publication ID
25252175
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2853986
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