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α-Synuclein and mitochondria: partners in crime?
scientific article published on July 2013
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scholarly article
1 reference
stated in
Europe PubMed Central
PMCID
3701775
retrieved
17 August 2017
title
α-Synuclein and mitochondria: partners in crime?
(English)
1 reference
stated in
Europe PubMed Central
PMCID
3701775
retrieved
17 August 2017
main subject
Synuclein
1 reference
based on heuristic
inferred from title
author name string
Ken Nakamura
series ordinal
1
1 reference
stated in
Europe PubMed Central
PMCID
3701775
retrieved
17 August 2017
publication date
1 July 2013
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stated in
Europe PubMed Central
PMCID
3701775
retrieved
17 August 2017
published in
Neurotherapeutics
1 reference
stated in
Europe PubMed Central
PMCID
3701775
retrieved
17 August 2017
volume
10
1 reference
stated in
Europe PubMed Central
PMCID
3701775
retrieved
17 August 2017
page(s)
391-399
1 reference
stated in
Europe PubMed Central
PMCID
3701775
retrieved
17 August 2017
issue
3
1 reference
stated in
Europe PubMed Central
PMCID
3701775
retrieved
17 August 2017
exact match
https://scigraph.springernature.com/pub.10.1007/s13311-013-0182-9
0 references
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Selective binding of nuclear alpha-synuclein to the PGC1alpha promoter under conditions of oxidative stress may contribute to losses in mitochondrial function: implications for Parkinson's disease
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Alpha-synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson's disease
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PINK1- and Parkin-mediated mitophagy at a glance
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α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer
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LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1
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α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
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Neuroprotection of α-synuclein under acute and chronic rotenone and maneb treatment is abolished by its familial Parkinson's disease mutations A30P, A53T and E46K.
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Functional alterations to the nigrostriatal system in mice lacking all three members of the synuclein family
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Direct membrane association drives mitochondrial fission by the Parkinson disease-associated protein alpha-synuclein
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The lipid peroxidation products 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote the formation of α-synuclein oligomers with distinct biochemical, morphological, and functional properties
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29 September 2017
αβγ-Synuclein triple knockout mice reveal age-dependent neuronal dysfunction
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29 September 2017
Lipid classes and fatty acid patterns are altered in the brain of γ-synuclein null mutant mice
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29 September 2017
PGC-1α, a potential therapeutic target for early intervention in Parkinson's disease
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29 September 2017
Inhibition of mitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1.
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29 September 2017
Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro
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Essential regulation of cell bioenergetics by constitutive InsP3 receptor Ca2+ transfer to mitochondria.
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A pathologic cascade leading to synaptic dysfunction in alpha-synuclein-induced neurodegeneration.
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29 September 2017
Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
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Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis
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29 September 2017
Alpha-synuclein overexpression and aggregation exacerbates impairment of mitochondrial functions by augmenting oxidative stress in human neuroblastoma cells
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29 September 2017
Cardiolipin acts as a mitochondrial signalling platform to launch apoptosis.
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29 September 2017
alpha-Synuclein is differentially expressed in mitochondria from different rat brain regions and dose-dependently down-regulates complex I activity
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Clustering of alpha-synuclein on supported lipid bilayers: role of anionic lipid, protein, and divalent ion concentration
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The effect of alpha-synuclein knockdown on MPP+ toxicity in models of human neurons
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Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery
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Mitochondrial translocation of alpha-synuclein is promoted by intracellular acidification
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29 September 2017
Mitochondrial association of alpha-synuclein causes oxidative stress
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29 September 2017
Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain
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29 September 2017
The PINK1/Parkin pathway regulates mitochondrial morphology
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29 September 2017
Brain neutral lipids mass is increased in alpha-synuclein gene-ablated mice
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29 September 2017
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29 September 2017
Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
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29 September 2017
Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
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High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease
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Mice lacking alpha-synuclein are resistant to mitochondrial toxins
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29 September 2017
Mitochondrial lipid abnormality and electron transport chain impairment in mice lacking alpha-synuclein
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29 September 2017
Disruption of fusion results in mitochondrial heterogeneity and dysfunction
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Structure and dynamics of micelle-bound human alpha-synuclein
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29 September 2017
Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling
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Phospholipid scramblase 3 controls mitochondrial structure, function, and apoptotic response
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Alpha-synuclein expression in HEK293 cells enhances the mitochondrial sensitivity to rotenone
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Regulation of alpha-synuclein by bFGF in cultured ventral midbrain dopaminergic neurons
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α-Synuclein protects neurons from apoptosis downstream of free-radical production through modulation of the MAPK signalling pathway.
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4 September 2018
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4 September 2018
Alpha-synuclein induced membrane depolarization and loss of phosphorylation capacity of isolated rat brain mitochondria: implications in Parkinson's disease.
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4 September 2018
Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core.
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4 September 2018
Optical reporters for the conformation of alpha-synuclein reveal a specific interaction with mitochondria
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4 September 2018
Functional mitochondria are required for alpha-synuclein toxicity in aging yeast.
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Parkinson's disease genetic mutations increase cell susceptibility to stress: mutant alpha-synuclein enhances H2O2- and Sin-1-induced cell death.
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3701775
retrieved
4 September 2018
Parkinson's disease alpha-synuclein transgenic mice develop neuronal mitochondrial degeneration and cell death.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3701775
retrieved
4 September 2018
Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3701775
retrieved
4 September 2018
Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3701775
retrieved
4 September 2018
Accumulation of phosphorylated alpha-synuclein in aging human brain.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3701775
retrieved
4 September 2018
Human alpha-synuclein over-expression increases intracellular reactive oxygen species levels and susceptibility to dopamine.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3701775
retrieved
4 September 2018
Prevalence of Parkinson's disease in Europe: A collaborative study of population-based cohorts. Neurologic Diseases in the Elderly Research Group
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3701775
retrieved
20 October 2018
Alpha-synuclein overexpression in PC12 and chromaffin cells impairs catecholamine release by interfering with a late step in exocytosis
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/23512373
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Burden of parkinsonism: a population-based study
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/23512373
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Lipid topology and physical properties of the outer mitochondrial membrane of the yeast, Saccharomyces cerevisiae
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/23512373
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Phospholipid asymmetry of the outer membrane of rat liver mitochondria
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/23512373
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1007/S13311-013-0182-9
1 reference
stated in
Europe PubMed Central
PMCID
3701775
retrieved
17 August 2017
PMCID
3701775
1 reference
stated in
Europe PubMed Central
PMCID
3701775
retrieved
17 August 2017
PubMed ID
23512373
1 reference
stated in
Europe PubMed Central
PMCID
3701775
retrieved
17 August 2017
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