Varaico: Literature-Extracted Genetic Variants

Gene:PRKN
Variant:p.C289G
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PRKN

NM_004562.3:p.C289G

Associated Papers

Cis or trans: a puzzle of Parkin activation mechanism.

Sherawat M et al.

Essays in Biochemistry, 2026

Canonical and alternate mechanisms that regulate ubiquitylation by the E3 ligase parkin.

Basilone NT et al.

Biochemical Society Transactions, 2025

Computational association in parkinson's disease SNPs with brain structural and functional alterations.

Subramaniyan S et al.

Neurogenetics, 2025

Structural-functional relevance of DNAJBs in protein aggregation and associated neurodegenerative diseases.

Fatima S et al.

Biochimica Et Biophysica Acta. Proteins and Proteomics, 2025

Therapeutic potential of Parkin and its regulation in Parkinson's disease.

Safreena N et al.

Biochemical Pharmacology, 2024

PRKN-linked familial Parkinson's disease: cellular and molecular mechanisms of disease-linked variants.

Clausen L et al.

Cellular and Molecular Life Sciences : Cmls, 2024

Genotype-phenotype correlation in PRKN-associated Parkinson's disease.

Menon PJ et al.

Npj Parkinson's Disease, 2024

38553467 (PubMed )
Supplement: 41531_2024_677_MOESM1_ESM.pdf

DNAJB6 mutants display toxic gain of function through unregulated interaction with Hsp70 chaperones.

Abayev-Avraham M et al.

Nature Communications, 2023

Comparative analysis of web-based programs for single amino acid substitutions in proteins.

Choudhury A et al.

Plos One, 2022

35507592 (PubMed )
Supplement: pone.0267084.s001.xlsx › PARK2

Assessing the relationship between monoallelic PRKN mutations and Parkinson's risk.

Lubbe SJ et al.

Human Molecular Genetics, 2021

33448283 (PubMed )
Supplement: 2020_12_09_monoallelic_v31_hmg_suppl_data_accepted_ddaa273.docx

J-domain proteins interaction with neurodegenerative disease-related proteins.

Ayala Mariscal SM et al.

Experimental Cell Research, 2021

Characterization of Recessive Parkinson Disease in a Large Multicenter Study.

Lesage S et al.

Annals of Neurology, 2020

Chaperones and Proteostasis: Role in Parkinson's Disease.

Joshi N et al.

Diseases (basel, Switzerland), 2020

Functional diversity between HSP70 paralogs caused by variable interactions with specific co-chaperones.

Serlidaki D et al.

The Journal of Biological Chemistry, 2020

Neuromuscular Diseases Due to Chaperone Mutations: A Review and Some New Results.

Sarparanta J et al.

International Journal of Molecular Sciences, 2020

The PARK2 Mutation Associated with Parkinson's Disease Enhances the Vulnerability of Peripheral Blood Lymphocytes to Paraquat.

Ming F et al.

Biomed Research International, 2020

The landscape of Parkin variants reveals pathogenic mechanisms and therapeutic targets in Parkinson's disease.

Yi W et al.

Human Molecular Genetics, 2019

Neuronal microtubules and proteins linked to Parkinson's disease: a relevant interaction?

Calogero AM et al.

Biological Chemistry, 2019

Association of Subthalamic Deep Brain Stimulation With Motor, Functional, and Pharmacologic Outcomes in Patients With Monogenic Parkinson Disease: A Systematic Review and Meta-analysis.

Artusi CA et al.

Jama Network Open, 2019

Bioenergetics and Autophagic Imbalance in Patients-Derived Cell Models of Parkinson Disease Supports Systemic Dysfunction in Neurodegeneration.

González-Casacuberta I et al.

Frontiers in Neuroscience, 2019

Pla2g6 Deficiency in Zebrafish Leads to Dopaminergic Cell Death, Axonal Degeneration, Increased β-Synuclein Expression, and Defects in Brain Functions and Pathways.

Sánchez E et al.

Molecular Neurobiology, 2018

Alterations in the E3 ligases Parkin and CHIP result in unique metabolic signaling defects and mitochondrial quality control issues.

Lizama BN et al.

Neurochemistry International, 2018

Impact of altered phosphorylation on loss of function of juvenile Parkinsonism-associated genetic variants of the E3 ligase parkin.

Aguirre JD et al.

The Journal of Biological Chemistry, 2018

The M458L missense mutation disrupts the catalytic properties of Parkin.

Do YJ et al.

Febs Letters, 2018

Spinocerebellar Ataxia Type 2.

Scoles DR et al.

Advances in Experimental Medicine and Biology, 2018

Cellular and Molecular Basis of Neurodegeneration in Parkinson Disease.

Zeng XS et al.

Frontiers in Aging Neuroscience, 2018

Versatile members of the DNAJ family show Hsp70 dependent anti-aggregation activity on RING1 mutant parkin C289G.

Kakkar V et al.

Scientific Reports, 2016

Dual Function of Phosphoubiquitin in E3 Activation of Parkin.

Walinda E et al.

The Journal of Biological Chemistry, 2016

In Silico Analysis of SNPs in PARK2 and PINK1 Genes That Potentially Cause Autosomal Recessive Parkinson Disease.

Bakhit YH et al.

Advances in Bioinformatics, 2016

Parkin maintains mitochondrial levels of the protective Parkinson's disease-related enzyme 17-β hydroxysteroid dehydrogenase type 10.

Bertolin G et al.

Cell Death and Differentiation, 2015

Structural studies of parkin and sacsin: Mitochondrial dynamics in neurodegenerative diseases.

Li X et al.

Movement Disorders : Official Journal of the Movement Disorder Society, 2015

Parkin structure and function.

Seirafi M et al.

The Febs Journal, 2015

HSPA1A-independent suppression of PARK2 C289G protein aggregation by human small heat shock proteins.

Minoia M et al.

Molecular and Cellular Biology, 2014

The Copper Metabolism MURR1 domain protein 1 (COMMD1) modulates the aggregation of misfolded protein species in a client-specific manner.

Vonk WI et al.

Plos One, 2014

Genetic insights into sporadic Parkinson's disease pathogenesis.

Chai C et al.

Current Genomics, 2013

The TOMM machinery is a molecular switch in PINK1 and PARK2/PARKIN-dependent mitochondrial clearance.

Bertolin G et al.

Autophagy, 2013

Structure of the human Parkin ligase domain in an autoinhibited state.

Wauer T et al.

The Embo Journal, 2013

PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding.

Lazarou M et al.

The Journal of Cell Biology, 2013

Mitochondrial dynamics and Parkinson's disease: focus on parkin.

Lim KL et al.

Antioxidants & Redox Signaling, 2012

A simple cell based assay to measure Parkin activity.

Morrison E et al.

Journal of Neurochemistry, 2011

Molecular chaperone-mediated rescue of mitophagy by a Parkin RING1 domain mutant.

Rose JM et al.

Human Molecular Genetics, 2011

Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation update.

Nuytemans K et al.

Human Mutation, 2010

20506312 (PubMed )
Supplement: humu0031-0763-SD1.pdf

Parkin overexpression selects against a deleterious mtDNA mutation in heteroplasmic cybrid cells.

Suen DF et al.

Proceedings of the National Academy of Sciences of the United States of America, 2010

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1.

Geisler S et al.

Nature Cell Biology, 2010

Somatic mutations of the Parkinson's disease-associated gene PARK2 in glioblastoma and other human malignancies.

Veeriah S et al.

Nature Genetics, 2010

SH3 domains from a subset of BAR proteins define a Ubl-binding domain and implicate parkin in synaptic ubiquitination.

Trempe JF et al.

Molecular Cell, 2009

Identification of a novel Zn2+-binding domain in the autosomal recessive juvenile Parkinson-related E3 ligase parkin.

Hristova VA et al.

The Journal of Biological Chemistry, 2009

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