Varaico: Literature-Extracted Genetic Variants

Gene:TRIM32
Variant:p.R394H
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TRIM32

NM_012210.4:p.R394H

Associated Papers

Correction: Investigating genotype-phenotype correlation of limb-girdle muscular dystrophy R8: association of clinical severity, protein biological function and protein oligomerization.

Liang X et al.

Acta Neuropathologica Communications, 2025

Investigating genotype-phenotype correlation of limb-girdle muscular dystrophy R8: association of clinical severity, protein biological function and protein oligomerization.

Liang X et al.

Acta Neuropathologica Communications, 2025

Tripartite Motif-Containing Protein 32 (TRIM32): What Does It Do for Skeletal Muscle?

Jeong SY et al.

Cells, 2023

TRIM32 biallelic defects cause limb-girdle muscular dystrophy R8: identification of two novel mutations and investigation of genotype-phenotype correlation.

Guan Y et al.

Skeletal Muscle, 2023

Case report: A novel patient presenting TRIM32-related limb-girdle muscular dystrophy.

Rimoldi M et al.

Frontiers in Neurology, 2023

Tripartite motif-containing protein 32 regulates Ca2+ movement in skeletal muscle.

Choi JH et al.

American Journal of Physiology. Cell Physiology, 2022

TRIM32 and Malin in Neurological and Neuromuscular Rare Diseases.

Kumarasinghe L et al.

Cells, 2021

Exome Sequencing of 21 Bardet-Biedl Syndrome (BBS) Genes to Identify Obesity Variants in 6,851 American Indians.

Day SE et al.

Obesity (silver Spring, Md.), 2021

33616283 (PubMed )
Supplement: OBY-29-748-s001.xlsx › Table_S2

TRIM32: A Multifunctional Protein Involved in Muscle Homeostasis, Glucose Metabolism, and Tumorigenesis.

Bawa S et al.

Biomolecules, 2021

Costameric integrin and sarcoglycan protein levels are altered in a Drosophila model for Limb-girdle muscular dystrophy type 2H.

Bawa S et al.

Molecular Biology of the Cell, 2021

TRIM32, but not its muscular dystrophy-associated mutant, positively regulates and is targeted to autophagic degradation by p62/SQSTM1.

Overå KS et al.

Journal of Cell Science, 2019

A TRIM32-AMBRA1-ULK1 complex initiates the autophagy response in atrophic muscle cells.

Di Rienzo M et al.

Autophagy, 2019

Autophagy induction in atrophic muscle cells requires ULK1 activation by TRIM32 through unanchored K63-linked polyubiquitin chains.

Di Rienzo M et al.

Science Advances, 2019

Extending the clinical and mutational spectrum of TRIM32-related myopathies in a non-Hutterite population.

Johnson K et al.

Journal of Neurology, Neurosurgery, and Psychiatry, 2019

29921608 (PubMed )
Supplement: jnnp-2018-318288supp003.pdf

Capturing variation impact on molecular interactions in the IMEx Consortium mutations data set.

Del-Toro N et al.

Nature Communications, 2019

30602777 (PubMed )
Supplement: 41467_2018_7709_MOESM6_ESM.xlsx › Supplementary_data_3

A Comprehensive Atlas of E3 Ubiquitin Ligase Mutations in Neurological Disorders.

George AJ et al.

Frontiers in Genetics, 2018

29491882 (PubMed )
Supplement: Table2.xlsx › Sheet1

TRIM32 ubiquitin E3 ligase, one enzyme for several pathologies: From muscular dystrophy to tumours.

Lazzari E et al.

The International Journal of Biochemistry & Cell Biology, 2016

Detection of TRIM32 deletions in LGMD patients analyzed by a combined strategy of CGH array and massively parallel sequencing.

Nectoux J et al.

European Journal of Human Genetics : Ejhg, 2015

The E3 ubiquitin ligase TRIM32 regulates myoblast proliferation by controlling turnover of NDRG2.

Mokhonova EI et al.

Human Molecular Genetics, 2015

The common missense mutation D489N in TRIM32 causing limb girdle muscular dystrophy 2H leads to loss of the mutated protein in knock-in mice resulting in a Trim32-null phenotype.

Kudryashova E et al.

Human Molecular Genetics, 2011

TRIM32 protein sensitizes cells to tumor necrosis factor (TNFα)-induced apoptosis via its RING domain-dependent E3 ligase activity against X-linked inhibitor of apoptosis (XIAP).

Ryu YS et al.

The Journal of Biological Chemistry, 2011

Intragenic deletion of TRIM32 in compound heterozygotes with sarcotubular myopathy/LGMD2H.

Borg K et al.

Human Mutation, 2009

TRIM32 is an E3 ubiquitin ligase for dysbindin.

Locke M et al.

Human Molecular Genetics, 2009

Deficiency of the E3 ubiquitin ligase TRIM32 in mice leads to a myopathy with a neurogenic component.

Kudryashova E et al.

Human Molecular Genetics, 2009

Use of SNP array analysis to identify a novel TRIM32 mutation in limb-girdle muscular dystrophy type 2H.

Cossée M et al.

Neuromuscular Disorders : Nmd, 2009

Mutations that impair interaction properties of TRIM32 associated with limb-girdle muscular dystrophy 2H.

Saccone V et al.

Human Mutation, 2008

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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."