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References from Cellular and systemic modifiers of alpha-synuclein proteostasis. Local targets link to admitted publications; unresolved targets remain external evidence.
α-synuclein pathology in synucleinopathies: mechanisms, biomarkers, and therapeutic challenges
10.3390/ijms26115405 · 2025 · External reference
Alpha-synuclein in Parkinson's disease and other synucleinopathies: from overt neurodegeneration back to early synaptic dysfunction
10.1038/s41419-023-05672-9 · 2023 · External reference
Characterization of a novel protein regulated during the critical period for song learning in the zebra finch
10.1016/0896-6273(95)90040-3 · 1995 · External reference
Stabilization of α-synuclein secondary structure upon binding to synthetic membranes
10.1074/jbc.273.16.9443 · 1998 · External reference
A short motif in the N-terminal region of α-synuclein is critical for both aggregation and function
10.1038/s41594-020-0384-x · 2020 · External reference
A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly
10.1074/jbc.m008919200 · 2001 · External reference
Characterization of hydrophobic residue requirements for α-synuclein fibrillization
10.1021/bi900539p · 2009 · External reference
C-terminal calcium binding of α-synuclein modulates synaptic vesicle interaction
10.1038/s41467-018-03111-4 · 2018 · External reference
VAMP2 regulates phase separation of α-synuclein
10.1038/s41556-024-01451-6 · 2024 · External reference
Structural and functional implications of C-terminal regions of α-synuclein
10.1021/bi026284c · 2002 · External reference
α-synuclein occurs physiologically as a helically folded tetramer that resists aggregation
10.1038/nature10324 · 2011 · External reference
A soluble α-synuclein construct forms a dynamic tetramer
10.1073/pnas.1113260108 · 2011 · External reference
Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal
10.1523/jneurosci.08-08-02804.1988 · 1988 · External reference
The precursor protein of non-Aβ component of alzheimer's disease amyloid is a presynaptic protein of the central nervous system
10.1016/0896-6273(95)90302-x · 1995 · External reference
Red blood cells are the major source of alpha-synuclein in blood
10.1159/000112832 · 2008 · External reference
Cell biology and pathophysiology of α-synuclein
10.1101/cshperspect.a024091 · 2018 · External reference
Functional and pathological effects of α-synuclein on synaptic SNARE complexes
10.1016/j.jmb.2022.167714 · 2023 · External reference
The new mutation, E46K, of α-synuclein causes Parkinson and Lewy body dementia
10.1002/ana.10795 · 2004 · External reference
Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease
10.1038/ng0298-106 · 1998 · External reference
Mutation in the α-synuclein gene identified in families with Parkinson's disease
10.1126/science.276.5321.2045 · 1997 · External reference
α-synuclein locus duplication as a cause of familial Parkinson's disease
10.1016/s0140-6736(04)17103-1 · 2004 · External reference
Causal relation between α-synuclein locus duplication as a cause of familial Parkinson's disease
10.1016/s0140-6736(04)17104-3 · 2004 · External reference
α-synuclein locus triplication causes Parkinson's disease
10.1126/science.1090278 · 2003 · External reference
Posttranslational modifications of α-synuclein, their therapeutic potential, and crosstalk in health and neurodegenerative diseases
10.1124/pharmrev.123.001111 · 2024 · External reference
Post-translational modifications of soluble α-synuclein regulate the amplification of pathological α-synuclein
10.1038/s41593-022-01239-7 · 2023 · External reference
Alpha-synuclein post-translational modifications: implications for pathogenesis of Lewy body disorders
10.3389/fnagi.2021.690293 · 2021 · External reference
α-synuclein phase separation and amyloid aggregation are modulated by C-terminal truncations
10.1002/1873-3468.14361 · 2022 · External reference
C-terminal truncation modulates α-synuclein's cytotoxicity and aggregation by promoting the interactions with membrane and chaperone
10.1038/s42003-022-03768-0 · 2022 · External reference
Do post-translational modifications influence protein aggregation in neurodegenerative diseases: a systematic review
10.3390/brainsci10040232 · 2020 · External reference
Differential role of C-terminal truncations on alpha-synuclein pathology and Lewy body formation
10.1038/s41531-025-01084-y · 2025 · External reference
Alpha-synuclein structure, functions, and interactions
10.4103/1735-1995.181989 · 2016 · External reference
The function of α-synuclein
10.1016/j.neuron.2013.09.004 · 2013 · External reference
α-synuclein in synaptic function and dysfunction
10.1016/j.tins.2022.11.007 · 2023 · External reference
Alpha-synuclein and Parkinson's disease
10.1007/pl00000671 · 2000 · External reference
Dysregulated lipid metabolism and its role in α-synucleinopathy in Parkinson's disease
10.3389/fnins.2019.00328 · 2019 · External reference
Lipids at the crossroad of α-synuclein function and dysfunction: biological and pathological implications
10.3389/fncel.2019.00175 · 2019 · External reference
Lipids: key players that modulate α-synuclein toxicity and neurodegeneration in Parkinson's disease
10.3390/ijms21093301 · 2020 · External reference
Parkinson's disease: proteinopathy or lipidopathy?
10.1038/s41531-019-0103-7 · 2020 · External reference
The role of lipids interacting with α-synuclein in the pathogenesis of Parkinson's disease
10.3233/jpd-171103 · 2017 · External reference
α-synuclein occurs in lipid-rich high molecular weight complexes, binds fatty acids, and shows homology to the fatty acid-binding proteins
10.1073/pnas.171300598 · 2001 · External reference
Alpha-synuclein physiology and pathology: a perspective on cellular structures and organelles
10.3389/fnins.2019.01399 · 2020 · External reference
Monomeric alpha-synuclein exerts a physiological role on brain ATP synthase
10.1523/jneurosci.1659-16.2016 · 2016 · External reference
Alpha-synuclein interacts with regulators of ATP homeostasis in mitochondria
10.1038/s41467-025-62895-4 · 2025 · External reference
Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading
10.1073/pnas.1524128113 · 2016 · External reference
An analytical solution to the kinetics of breakable filament assembly
10.1126/science.1178250 · 2009 · External reference
Direct observation of the interconversion of normal and toxic forms of α-synuclein
10.1016/j.cell.2012.03.037 · 2012 · External reference
Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
10.1038/s41467-018-05971-2 · 2018 · External reference
α-synuclein-based animal models of Parkinson's disease: challenges and opportunities in a new era
10.1016/j.tins.2016.09.003 · 2016 · External reference
C. elegans model identifies genetic modifiers of α-synuclein inclusion formation during aging
10.1371/journal.pgen.1000027 · 2008 · External reference
Aggregates assembled from overexpression of wild-type α-synuclein are not toxic to human neuronal cells
10.1097/nen.0b013e31818c3618 · 2008 · External reference
A broken α-helix in folded α-synuclein
10.1074/jbc.m213128200 · 2003 · External reference
α-synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation
10.1073/pnas.1416598111 · 2014 · External reference
Neuropathology, biochemistry, and biophysics of α-synuclein aggregation
10.1111/j.1471-4159.2007.04764.x · 2007 · External reference
Unresolved reference
2023 · External reference
Parkinson's disease
10.1016/s0140-6736(14)61393-3 · 2015 · External reference
The amyloid state and its association with protein misfolding diseases
10.1038/nrm3810 · 2014 · External reference
Liquid–liquid phase separation in disease
10.1146/annurev-genet-112618-043527 · 2019 · External reference
Liquid–liquid phase separation and its mechanistic role in pathological protein aggregation
10.1016/j.jmb.2020.03.004 · 2020 · External reference
α-Synuclein aggregation nucleates through liquid–liquid phase separation
10.1038/s41557-020-0465-9 · 2020 · External reference
Biomolecular condensates undergo a generic shear-mediated liquid-to-solid transition
10.1038/s41565-020-0731-4 · 2020 · External reference
Liquid phase condensation in cell physiology and disease
10.1126/science.aaf4382 · 2017 · External reference
Sequence determinants of the aggregation of proteins within condensates generated by liquid-liquid phase separation
10.1016/j.jmb.2021.167201 · 2022 · External reference
Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing
10.1038/s41580-020-00326-6 · 2021 · External reference
Observation of an α-synuclein liquid droplet state and its maturation into Lewy body-like assemblies
2021 · External reference
Toxic prefibrillar α-synuclein amyloid oligomers adopt a distinctive antiparallel β-sheet structure
10.1042/bj20111924 · 2012 · External reference
Liquid–liquid phase separation of alpha-synuclein increases the structural variability of fibrils formed during amyloid aggregation
10.1111/febs.17244 · 2024 · External reference
Liquid-liquid phase separation of α-synuclein: a new mechanistic insight for α-synuclein aggregation associated with Parkinson's disease pathogenesis
10.1016/j.jmb.2022.167713 · 2023 · External reference
Protein G-quadruplex interactions and their effects on phase transitions and protein aggregation
10.1093/nar/gkae229 · 2024 · External reference
Modulating α-synuclein liquid–liquid phase separation
10.1021/acs.biochem.1c00434 · 2021 · External reference
Protein aggregation and neurodegenerative disease
10.1038/nm1066 · 2004 · External reference
Distinct effects of familial Parkinson's disease-associated mutations on α-synuclein phase separation and amyloid aggregation
10.3390/biom13050726 · 2023 · External reference
Ubiquilin-2 liquid droplets catalyze α-synuclein fibril formation
10.1038/s44318-025-00591-1 · 2025 · External reference
Synapsin condensates recruit alpha-synuclein
10.1016/j.jmb.2021.166961 · 2021 · External reference
A liquid phase of synapsin and lipid vesicles
10.1126/science.aat5671 · 2018 · External reference
Vesicle clustering in a living synapse depends on a synapsin region that mediates phase separation
10.1016/j.celrep.2020.01.092 · 2020 · External reference
Calcium promotes α-synuclein liquid-liquid phase separation to accelerate amyloid aggregation
10.1016/j.bbrc.2022.02.097 · 2022 · External reference
Manganese promotes α-synuclein amyloid aggregation through the induction of protein phase transition
10.1016/j.jbc.2021.101469 · 2022 · External reference
The Lewy body in Parkinson's disease and related neurodegenerative disorders
10.1007/s12035-012-8280-y · 2013 · External reference
The Lewy body in Parkinson's disease: molecules implicated in the formation and degradation of α-synuclein aggregates
10.1111/j.1440-1789.2007.00803.x · 2007 · External reference
Morphogenesis of Lewy bodies: dissimilar incorporation of α-synuclein, ubiquitin, and p62
10.1093/jnen/62.12.1241 · 2003 · External reference
Proteomic identification of novel proteins associated with Lewy bodies
10.2741/2973 · 2008 · External reference
Lewy pathology in Parkinson's disease consists of crowded organelles and lipid membranes
10.1038/s41593-019-0423-2 · 2019 · External reference
Rapid iPSC inclusionopathy models shed light on formation, consequence, and molecular subtype of α-synuclein inclusions
10.1016/j.neuron.2024.06.002 · 2024 · External reference
Defining a Lewy body: running up the hill of shifting definitions and evolving concepts
10.3233/jpd-230183 · 2024 · External reference
Ca2+ is a key factor in α-synuclein-induced neurotoxicity
10.1242/jcs.180737 · 2016 · External reference
Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation
2015 · External reference
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
10.1038/s41467-019-09477-3 · 2019 · External reference
Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers
10.1126/science.aan6160 · 2017 · External reference
Shape matters: the complex relationship between aggregation and toxicity in protein-misfolding diseases
10.1042/ebc20160008 · 2016 · External reference
Defining the limits: protein aggregation and toxicity in vivo
10.3109/10409238.2014.914151 · 2014 · External reference
Seeking a mechanism for the toxicity of oligomeric α-synuclein
10.3390/biom5020282 · 2015 · External reference
The amyloid-cell membrane system
10.1016/j.bpc.2013.06.003 · 2013 · External reference
Alpha-synuclein oligomers interact with metal ions to induce oxidative stress and neuronal death in Parkinson's disease
10.1089/ars.2015.6343 · 2016 · External reference
Small soluble α-synuclein aggregates are the toxic species in Parkinson's disease
10.1038/s41467-022-33252-6 · 2022 · External reference
In vivo demonstration that α-synuclein oligomers are toxic
10.1073/pnas.1100976108 · 2011 · External reference
The role of alpha-synuclein oligomerization and aggregation in cellular and animal models of Parkinson's disease
10.1371/journal.pone.0038545 · 2012 · External reference
Exogenous α-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death
10.1016/j.neuron.2011.08.033 · 2011 · External reference
Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells
10.1073/pnas.0908005106 · 2009 · External reference
Prying into the prion hypothesis for Parkinson's disease
10.1523/jneurosci.1788-16.2017 · 2017 · External reference
Prion-like mechanisms in the pathogenesis of tauopathies and synucleinopathies
10.1007/s11910-014-0495-z · 2014 · External reference
The prion-like spreading of α-synuclein: from in vitro to in vivo models of Parkinson's disease
10.1016/j.arr.2019.01.012 · 2019 · External reference
Biogenesis, secretion, and intercellular interactions of exosomes and other extracellular vesicles
10.1146/annurev-cellbio-101512-122326 · 2014 · External reference
Cell-produced α-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival
10.1523/jneurosci.5699-09.2010 · 2010 · External reference
Release and uptake of pathologic alpha-synuclein
10.1007/s00441-017-2775-9 · 2018 · External reference
The proteostasis network and its decline in ageing
10.1038/s41580-019-0101-y · 2019 · External reference
Proteostasis impairment in protein-misfolding and -aggregation diseases
10.1016/j.tcb.2014.05.003 · 2014 · External reference
Pathways of cellular proteostasis in aging and disease
10.1083/jcb.201709072 · 2018 · External reference
Interplay of proteostasis capacity and protein aggregation: implications for cellular function and disease
10.1016/j.jmb.2024.168615 · 2024 · External reference
Translation initiator EIF4G1 mutations in familial Parkinson disease
10.1016/j.ajhg.2011.08.009 · 2011 · External reference
Sequence variants in eukaryotic translation initiation factor 4-gamma (eIF4G1) are associated with Lewy body dementia
10.1007/s00401-012-1059-4 · 2013 · External reference
Whole exome sequencing of rare variants in EIF4G1 and VPS35 in Parkinson disease
10.1212/wnl.0b013e31828727d4 · 2013 · External reference
Eukaryotic translation initiation factors and regulators
10.1016/s0959-440x(03)00009-5 · 2003 · External reference
Parkinson's disease genes VPS35 and EIF4G1 interact genetically and converge on α-synuclein
10.1016/j.neuron.2014.11.027 · 2015 · External reference
Linking the VPS35 and EIF4G1 pathways in Parkinson's disease
10.1016/j.neuron.2014.12.045 · 2015 · External reference
Defects in mRNA translation in LRRK2-mutant hiPSC-derived dopaminergic neurons lead to dysregulated calcium homeostasis
10.1016/j.stem.2020.08.002 · 2020 · External reference
Protein translation in the pathogenesis of Parkinson's disease
10.3390/ijms25042393 · 2024 · External reference
Protein synthesis is suppressed in sporadic and familial Parkinson's disease by LRRK2
10.1096/fj.202001046r · 2020 · External reference
Dysregulated mRNA translation in the G2019S LRRK2 and LRRK2 knock-out mouse brains
10.1523/eneuro.0310-21.2021 · 2021 · External reference
Regulators of proteostasis are translationally repressed in fibroblasts from patients with sporadic and LRRK2-G2019S Parkinson's disease
10.1038/s41531-023-00460-w · 2023 · External reference
Ribosomal protein s15 phosphorylation mediates LRRK2 neurodegeneration in Parkinson's disease
10.1016/j.cell.2014.01.064 · 2014 · External reference
Differential protein–protein interactions of LRRK1 and LRRK2 indicate roles in distinct cellular signaling pathways
10.1111/jnc.12798 · 2014 · External reference
The Parkinson's disease protein alpha-synuclein is a modulator of processing bodies and mRNA stability
10.1016/j.cell.2022.05.008 · 2022 · External reference
P-bodies and stress granules: possible roles in the control of translation and mRNA degradation
10.1101/cshperspect.a012286 · 2012 · External reference
P-bodies: composition, properties, and functions
10.1021/acs.biochem.7b01162 · 2018 · External reference
The unfolded protein response: an overview
10.3390/biology10050384 · 2021 · External reference
Mechanisms, regulation and functions of the unfolded protein response
10.1038/s41580-020-0250-z · 2020 · External reference
Canary in a coal mine: collided ribosomes as sensors of cellular conditions
10.1016/j.tibs.2021.09.001 · 2022 · External reference
mTOR signaling in Parkinson's disease
10.1007/s12017-016-8417-7 · 2017 · External reference
Enhanced mTORC1 signaling and protein synthesis in pathologic α-synuclein cellular and animal models of Parkinson's disease
10.1126/scitranslmed.add0499 · 2023 · External reference
Molecular chaperones in protein folding and proteostasis
10.1038/nature10317 · 2011 · External reference
Regulation of α-synuclein by chaperones in mammalian cells
10.1038/s41586-019-1808-9 · 2020 · External reference
Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/α-synuclein complex by Hip
10.1038/emboj.2009.298 · 2009 · External reference
Human Hsp70 disaggregase reverses Parkinson's-linked α-synuclein amyloid fibrils
10.1016/j.molcel.2015.07.012 · 2015 · External reference
Hsc70 Protein interaction with soluble and fibrillar α-synuclein
10.1074/jbc.m111.261321 · 2011 · External reference
Potential application of heat shock proteins as therapeutic targets in Parkinson's disease
10.1016/j.neuint.2022.105453 · 2023 · External reference
A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease
10.1016/j.celrep.2014.09.042 · 2014 · External reference
Targeting heat shock proteins to modulate α-synuclein toxicity
10.1177/1756285613493469 · 2014 · External reference
Hsp70 Reduces α-synuclein aggregation and toxicity
10.1074/jbc.m400255200 · 2004 · External reference
Small heat shock proteins protect against α-synuclein-induced toxicity and aggregation
10.1016/j.bbrc.2006.10.085 · 2006 · External reference
Chaperone suppression of α-synuclein toxicity in a Drosophila model for Parkinson's disease
10.1126/science.1067389 · 2002 · External reference
Hsp110 mitigates α-synuclein pathology in vivo
10.1073/pnas.1903268116 · 2019 · External reference
The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
10.1038/s41598-017-08324-z · 2017 · External reference
Single-cell transcriptomic and proteomic analysis of Parkinson's disease brains
10.1126/scitranslmed.abo1997 · 2024 · External reference
The cellular modifier MOAG-4/SERF drives amyloid formation through charge complementation
10.15252/embj.2020107568 · 2021 · External reference
Identification of MOAG-4/SERF as a regulator of age-related proteotoxicity
10.1016/j.cell.2010.07.020 · 2010 · External reference
MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions
10.1074/jbc.m116.764886 · 2017 · External reference
The disordered protein SERF promotes α-synuclein aggregation through liquid–liquid phase separation
10.1016/j.jbc.2024.105667 · 2024 · External reference
Molecular insights into the interaction between a disordered protein and a folded RNA
10.1073/pnas.2409139121 · 2024 · External reference
SERF, a family of tiny highly conserved, highly charged proteins with enigmatic functions
10.1111/febs.16555 · 2023 · External reference
The ubiquitin-proteasome system and autophagy: coordinated and independent activities
10.1016/j.biocel.2016.07.019 · 2016 · External reference
Autophagy in synucleinopathy: the overwhelmed and defective machinery
10.3390/cells8060565 · 2019 · External reference
Early-onset impairment of the ubiquitin-proteasome system in dopaminergic neurons caused by α-synuclein
10.1186/s40478-020-0894-0 · 2020 · External reference
Inhibition of 26Sproteasome activity by α-synuclein is mediated by the proteasomal chaperone Rpn14/PAAF1
10.1111/acel.14128 · 2024 · External reference
Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to alpha-synuclein inclusions
10.1016/j.nbd.2009.05.023 · 2009 · External reference
Gene expression profiling of parkinsonian substantia nigra pars compacta; alterations in ubiquitin-proteasome, heat shock protein, iron and oxidative stress regulated proteins, cell adhesion/cellular matrix and vesicle trafficking genes
10.1007/s00702-004-0212-1 · 2004 · External reference
Selective loss of 20S proteasome α-subunits in the substantia nigra pars compacta in Parkinson's disease
10.1016/s0304-3940(02)00296-3 · 2002 · External reference
Proteasomal inhibition by α-synuclein filaments and oligomers
10.1074/jbc.m306390200 · 2004 · External reference
α-synuclein protofibrils inhibit 26 S proteasome-mediated protein degradation
10.1074/jbc.m710560200 · 2008 · External reference
Dopamine-modified α-synuclein blocks chaperone-mediated autophagy
2008 · External reference
The complex ultrastructure of the endolysosomal system
10.1101/cshperspect.a016857 · 2014 · External reference
Common genetic risk for Parkinson's disease and dysfunction of the endo-lysosomal system
10.1098/rstb.2022.0517 · 2024 · External reference
Mutations in GBA are associated with familial Parkinson disease susceptibility and age at onset
10.1212/01.wnl.0000327823.81237.d1 · 2009 · External reference
Identification of p.Gln858* in ATP13A2 in two EOPD patients and presentation of their clinical features
10.1016/j.neulet.2014.06.023 · 2014 · External reference
ATP13A2 Regulates cellular alpha-synuclein multimerization, membrane association, and externalization
10.3390/ijms22052689 · 2021 · External reference
A genome-wide RNA interference screening reveals protectiveness of SNX5 knockdown in a Parkinson's disease cell model
10.1186/s40035-025-00486-5 · 2025 · External reference
Extracellular aggregated alpha synuclein primarily triggers lysosomal dysfunction in neural cells prevented by trehalose
10.1038/s41598-018-35811-8 · 2019 · External reference
Alpha-synuclein and the endolysosomal system in Parkinson's disease: guilty by association
10.3390/biom11091333 · 2021 · External reference
Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration
10.1073/pnas.1112368109 · 2012 · External reference
Proteomic profiling of exosomes: current perspectives
10.1002/pmic.200800109 · 2008 · External reference
Lysosomal dysfunction increases exosome-mediated alpha-synuclein release and transmission
10.1016/j.nbd.2011.01.029 · 2011 · External reference
Autophagy inhibition promotes SNCA/alpha-synuclein release and transfer via extracellular vesicles with a hybrid autophagosome-exosome-like phenotype
10.1080/15548627.2017.1395992 · 2018 · External reference
Lysosomal exocytosis releases pathogenic α-synuclein species from neurons in synucleinopathy models
10.1038/s41467-022-32625-1 · 2022 · External reference
Lysosomal dysfunction in α-synuclein pathology: molecular mechanisms and therapeutic strategies
10.1007/s00018-024-05419-5 · 2024 · External reference
TFEB-mediated autophagy rescues midbrain dopamine neurons from alpha-synuclein toxicity
10.1073/pnas.1305623110 · 2013 · External reference
Lysosome activation clears aggregates and enhances quiescent neural stem cell activation during aging
10.1126/science.aag3048 · 2018 · External reference
Targeting of lysosomal pathway genes for Parkinson's disease modification: insights from cellular and animal models
10.3389/fneur.2021.681369 · 2021 · External reference
Reciprocal effects of alpha-synuclein aggregation and lysosomal homeostasis in synucleinopathy models
10.1186/s40035-023-00363-z · 2023 · External reference
Genetics of Parkinson's disease
10.1101/cshperspect.a008888 · 2012 · External reference
Energetic basis of brain activity: implications for neuroimaging
10.1016/j.tins.2004.06.005 · 2004 · External reference
Interplay of mitochondrial calcium signalling and reactive oxygen species production in the brain
10.1042/bst20240261 · 2024 · External reference
Mitochondrial permeability transition, cell death and neurodegeneration
10.3390/cells13070648 · 2024 · External reference
A cellular perspective on brain energy metabolism and functional imaging
10.1016/j.neuron.2015.03.035 · 2015 · External reference
α-synuclein pathology and mitochondrial dysfunction: toxic partners in Parkinson's disease
10.1016/j.nbd.2025.106889 · 2025 · External reference
Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
10.1038/nature05292 · 2006 · External reference
Alpha-synuclein: pathology, mitochondrial dysfunction and neuroinflammation in Parkinson's disease
10.1016/j.nbd.2017.04.004 · 2018 · External reference
Calcium control of neurotransmitter release
10.1101/cshperspect.a011353 · 2012 · External reference
α-synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulum-mitochondria interactions
10.1074/jbc.m111.302794 · 2012 · External reference
α-synuclein is localized to mitochondria-associated ER membranes
10.1523/jneurosci.2507-13.2014 · 2014 · External reference
α-synuclein binds to the ER–mitochondria tethering protein VAPB to disrupt Ca2+ homeostasis and mitochondrial ATP production
10.1007/s00401-017-1704-z · 2017 · External reference
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson's disease
10.1038/s41467-018-04422-2 · 2018 · External reference
Mitochondrial alpha-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo
10.1016/j.neulet.2010.09.061 · 2010 · External reference
Mitochondrial import and accumulation of α-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain
10.1074/jbc.m710012200 · 2008 · External reference
Direct membrane association drives mitochondrial fission by the Parkinson disease-associated protein α-synuclein
10.1074/jbc.m110.213538 · 2011 · External reference
Mitochondrial calcium as a key regulator of mitochondrial ATP production in mammalian cells
10.1016/j.bbabio.2009.01.019 · 2009 · External reference
Spatial transcriptomics reveals molecular dysfunction associated with cortical Lewy pathology
10.1038/s41467-024-47027-8 · 2024 · External reference
α-synuclein pathology disrupts mitochondrial function in dopaminergic and cholinergic neurons at-risk in Parkinson's disease
10.1186/s13024-024-00756-2 · 2024 · External reference
Pathological structural conversion of α-synuclein at the mitochondria induces neuronal toxicity
10.1038/s41593-022-01140-3 · 2022 · External reference
Unbiased screens for modifiers of alpha-synuclein toxicity
10.1007/s11910-019-0925-z · 2019 · External reference
Delaying aging and the aging-associated decline in protein homeostasis by inhibition of tryptophan degradation
10.1073/pnas.1203083109 · 2012 · External reference
Tryptophan metabolism as a common therapeutic target in cancer, neurodegeneration and beyond
10.1038/s41573-019-0016-5 · 2019 · External reference
Kynurenines in the mammalian brain: when physiology meets pathology
10.1038/nrn3257 · 2012 · External reference
Kynurenic acid as an antagonist of α7 nicotinic acetylcholine receptors in the brain: facts and challenges
10.1016/j.bcp.2012.12.014 · 2013 · External reference
Metabolomics: potential non-protein biomarker candidates of Parkinson's disease
10.1016/j.neubiorev.2025.106310 · 2025 · External reference
Parkinson's disease is characterized by vitamin B6-dependent inflammatory kynurenine pathway dysfunction
10.1038/s41531-025-00964-7 · 2025 · External reference
Age- and disease-specific changes of the kynurenine pathway in Parkinson's and alzheimer's disease
10.1111/jnc.14843 · 2019 · External reference
Tryptophan metabolites are associated with symptoms and nigral pathology in Parkinson's disease
10.1002/mds.28202 · 2020 · External reference
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