The PINK1 kinase-driven ubiquitin ligase Parkin promotes mitochondrial protein import through the presequence pathway in living cells |
Jacoupy |
2019 |
PD-MitoQUANT |
https://doi.org/10.1038/s41598-019-47352-9 |
Basic science research paper, Parkinson's disease, disease mechanism, mitochondria, ubiquitinylation, in vitro |
|
α-synuclein oligomers and fibrils: a spectrum of species, a spectrum of toxicities |
Alam |
2019 |
PD-MitoQUANT |
http://doi.org/10.1111/jnc.14808 |
Review article, Parkinson's disease, neurobiology, chemistry, alpha-synuclein, fibrils, proteins |
|
α-Synuclein conformational strains spread, seed and target neuronal cells differentially after injection into the olfactory bulb |
Rey |
2019 |
PD-MitoQUANT |
https://doi.org/10.1186/s40478-019-0859-3 |
Alpha-synuclein, Strains, Fibrils, Prion-like spreading, Olfactory bulb |
|
AMPK Preferentially Depresses Retrograde Transport of Axonal Mitochondria during Localized Nutrient Deprivation |
Watters |
2020 |
PD-MitoQUANT |
https://doi.org/10.1523/JNEUROSCI.2067-19.2020 |
mitochondrial transport, metabolic stress, axonal injury, AMPK, lactate, microfluidic device |
|
Interaction of the chaperones alpha B-crystallin and CHIP with fibrillar alpha-synuclein: Effects on internalization by cells and identification of interacting interfaces |
Bendifallah |
2020 |
PD-MitoQUANT |
https://doi.org/10.1016/j.bbrc.2020.04.091 |
Molecular chaperones, Protein-protein interactions, Protein-protein interfaces, Cross linking, mass spectrometry |
|
Differential Membrane Binding and Seeding of Distinct α-Synuclein Fibrillar Polymorphs |
Shrivastava |
2020 |
PD-MitoQUANT |
https://pubmed.ncbi.nlm.nih.gov/32059758/ |
Basic research paper, protein aggregation, synucleinopathies, alpha-synuclein, Parkinson's disease |
|
The expression level of alpha-synuclein in different neuronal populations is the primary determinant of its prion-like seeding |
Courte |
2020 |
PD-MitoQUANT |
https://doi.org/10.1038/s41598-020-61757-x |
Mechanisms of disease, Parkinson's disease |
|
The differential solvent exposure of N-terminal residues provides ‘fingerprints’ of alpha-synuclein fibrillar polymorphs |
Landureau |
2021 |
PD-MitoQUANT |
https://doi.org/10.1016/j.jbc.2021.100737 |
alpha-synuclein,
protein misfolding,
strains,
limited proteolysis,
hydrogen-deuterium exchange,
mass spectrometry,
surface mapping,
neurodegenerative disease |
|
TP53INP1 exerts neuroprotection under ageing and Parkinson’s disease-related stress condition |
Dinh |
2021 |
PD-MitoQUANT |
https://doi.org/10.1038/s41419-021-03742-4 |
mice, neurons, gene, cell antibody, drosophila, rna, Parkinson
|
|
The PINK1 kinase-driven ubiquitin ligase Parkin promotes mitochondrial protein import through the presequence pathway in living cells |
Jacoupy |
2019 |
PD-MitoQUANT |
https://doi.org/10.1038/s41598-019-47352-9 |
|
|
Microglia jointly degrade fibrillar alpha-synuclein cargo by distribution through tunneling nanotubes |
Scheiblich |
2021 |
PD-MitoQUANT |
https://doi.org/10.1016/j.cell.2021.09.007 |
microglia,
alpha-synuclein,
tunneling nanotubes,
cell-to-cell transfer,
clearance,
LRRK2,
synucleinopathies,
degradation |
|
CEST-2.2 overexpression alters lipid metabolism and extends longevity of mitochondrial mutants |
Piazzesi |
2022 |
PD-MitoQUANT |
https://doi.org/10.15252/embr.202152606 |
Caenorhabditis elegans; carboxylesterase CEST-2.2; epigenetics; lipid metabolism; mitochondria. |
|
Sphingolipid changes in Parkinson L444P GBA mutation fibroblasts promote α-synuclein aggregation |
Galvagnion |
2022 |
PD-MitoQUANT |
https://doi.org/10.1093/brain/awab371 |
GBA; Parkinson’s disease; fibroblasts; lipidomics; α-synuclein. |
|
SGPL1 stimulates VPS39 recruitment to the mitochondria in MICU1 deficient cells |
Jackson |
2022 |
PD-MitoQUANT |
https://doi.org/10.1016/j.molmet.2022.101503 |
Autophagy; Caenorhabditis elegans; Longevity; MICU1; Mitochondria; Sphingosine signaling; VPS39. |
|
Modelling α-Synuclein Aggregation and Neurodegeneration with Fibril Seeds in Primary Cultures of Mouse Dopaminergic Neurons |
Tourville |
2022 |
PD-MitoQUANT |
https://doi.org/ 10.3390/cells11101640 |
α-Synuclein; cell culture model; dopamine neurons; fibril seeds; neurodegeneration;
Parkinson disease; protein aggregation |
|
AIFM1 beyond cell death: An overview of this OXPHOS-inducing factor in mitochondrial diseases |
Wischhof |
2022 |
PD-MitoQUANT |
https://doi.org/10.1016/j.ebiom.2022.104231 |
Aapoptosis-inducing factor (AIF),
CHCHD4,
Mitochondria,
Mitochondrial diseases,
Oxidative phosphorylation (OXPHOS) |
|