Varaico: Literature-Extracted Genetic Variants

Gene:SDS
Variant:p.A53T
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SDS

NM_006843.3:p.A53T

Associated Papers

The C. elegans gba-3 gene encodes a glucocerebrosidase that exacerbates α-synuclein-mediated impairments in deletion mutants.

Liu N et al.

Translational Neurodegeneration, 2025

39940047 (PubMed )
Supplement: 40035_2024_463_MOESM1_ESM.docx

The hexosamine biosynthetic pathway rescues lysosomal dysfunction in Parkinson's disease patient iPSC derived midbrain neurons.

Wani WY et al.

Nature Communications, 2024

38897986 (PubMed )
Supplement: 41467_2024_49256_MOESM1_ESM.pdf

Parkinson's disease-associated mutations in α-synuclein alters its lipid-bound state.

Maltseva S et al.

Biophysical Journal, 2024

Neuronal identity defines α-synuclein and tau toxicity.

Praschberger R et al.

Neuron, 2023

36948206 (PubMed )
Supplement: mmc5.pdf

Interaction Between the Glymphatic System and α-Synuclein in Parkinson's Disease.

Zhang Y et al.

Molecular Neurobiology, 2023

Pharmacological PINK1 activation ameliorates Pathology in Parkinson's Disease models.

Chin RM et al.

Biorxiv : the Preprint Server for Biology, 2023

Succinate dehydrogenase variants in paraganglioma: why are B subunit variants 'bad'?

Gruber LM et al.

Endocrine Oncology (bristol, England), 2023

37434649 (PubMed )
Supplement: supplementary_table_1.xlsx › Missense_Variants

Anionic lipid vesicles have differential effects on the aggregation of early onset-associated α-synuclein missense mutants.

Watt KJC et al.

The Journal of Biological Chemistry, 2022

The E46K mutation modulates α-synuclein prion replication in transgenic mice.

Holec SAM et al.

Plos Pathogens, 2022

DOPAnization of tyrosine in α-synuclein by tyrosine hydroxylase leads to the formation of oligomers.

Jin M et al.

Nature Communications, 2022

36371400 (PubMed )
Supplement: 41467_2022_34555_MOESM1_ESM.pdf

Distinct profiles of LRRK2 activation and Rab GTPase phosphorylation in clinical samples from different PD cohorts.

Petropoulou-Vathi L et al.

Npj Parkinson's Disease, 2022

Mechanisms of enhanced aggregation and fibril formation of Parkinson's disease-related variants of α-synuclein.

Ohgita T et al.

Scientific Reports, 2022

Cytosolic aggregation of mitochondrial proteins disrupts cellular homeostasis by stimulating the aggregation of other proteins.

Nowicka U et al.

Elife, 2021

Reduced oligodendrocyte exosome secretion in multiple system atrophy involves SNARE dysfunction.

Yu Z et al.

Brain : a Journal of Neurology, 2020

32428221 (PubMed )
Supplement: awaa110_supplementary_data.zip › awaa110-suppl_data › Yu_et_al_MSA_exosomes_Suppl_material_2020-4-7_rev_AU_.docx

Stress-Induced Cellular Clearance Is Mediated by the SNARE Protein ykt6 and Disrupted by α-Synuclein.

Cuddy LK et al.

Neuron, 2019

Replication of multiple system atrophy prions in primary astrocyte cultures from transgenic mice expressing human α-synuclein.

Krejciova Z et al.

Acta Neuropathologica Communications, 2019

Role of Parkinson's Disease-Linked Mutations and N-Terminal Acetylation on the Oligomerization of α-Synuclein Induced by 3,4-Dihydroxyphenylacetaldehyde.

Lima VA et al.

Acs Chemical Neuroscience, 2019

A sensitive assay reveals structural requirements for α-synuclein fibril growth.

Dhavale DD et al.

The Journal of Biological Chemistry, 2017

Extracellular α-synuclein induces sphingosine 1-phosphate receptor subtype 1 uncoupled from inhibitory G-protein leaving β-arrestin signal intact.

Zhang L et al.

Scientific Reports, 2017

The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction.

Sot B et al.

Scientific Reports, 2017

28102321 (PubMed )
Supplement: srep40859-s1.pdf

Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation.

Yu H et al.

The Journal of Chemical Physics, 2015

Familial Parkinson disease-associated mutations alter the site-specific microenvironment and dynamics of α-synuclein.

Sahay S et al.

The Journal of Biological Chemistry, 2015

Germline FH mutations presenting with pheochromocytoma.

Clark GR et al.

The Journal of Clinical Endocrinology and Metabolism, 2014

Familial Parkinson disease mutations influence α-synuclein assembly.

Ono K et al.

Neurobiology of Disease, 2011

Defects in very long chain fatty acid synthesis enhance alpha-synuclein toxicity in a yeast model of Parkinson's disease.

Lee YJ et al.

Plos One, 2011

Novel suppressors of alpha-synuclein toxicity identified using yeast.

Liang J et al.

Human Molecular Genetics, 2008

Tissue transglutaminase modulates alpha-synuclein oligomerization.

Segers-Nolten IM et al.

Protein Science : a Publication of the Protein Society, 2008

Sequence determinants regulating fibrillation of human alpha-synuclein.

Koo HJ et al.

Biochemical and Biophysical Research Communications, 2008

alpha-Synucleinopathy models and human neuropathology: similarities and differences.

Kahle PJ

Acta Neuropathologica, 2008

YGR198w (YPP1) targets A30P alpha-synuclein to the vacuole for degradation.

Flower TR et al.

The Journal of Cell Biology, 2007

Alpha-synuclein inhibits aromatic amino acid decarboxylase activity in dopaminergic cells.

Tehranian R et al.

Journal of Neurochemistry, 2006

Alpha-synuclein overexpression increases cytosolic catecholamine concentration.

Mosharov EV et al.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience, 2006

Alpha-synuclein targets the plasma membrane via the secretory pathway and induces toxicity in yeast.

Dixon C et al.

Genetics, 2005

Stabilization of alpha-synuclein protein with aging and familial parkinson's disease-linked A53T mutation.

Li W et al.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience, 2004

alpha-Synuclein-synaptosomal membrane interactions: implications for fibrillogenesis.

Jo E et al.

European Journal of Biochemistry, 2004

Effects of Parkinson's disease-linked mutations on the structure of lipid-associated alpha-synuclein.

Bussell R et al.

Biochemistry, 2004

15096050 (PubMed )
Supplement: bi0361352Bsi20040217_073011.pdf
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Regarding the variants extracted from papers and shown text snippets from research papers, the following holds: "Some rights reserved. This work permits non-commercial use, distribution and reproduction in any medium, provided the original author and source are credited."