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TRIM72 gene

Known as: tripartite motif containing 72, MITSUGUMIN, 53-KD, mitsugumin 53 
National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2017
2017
Inhibition of Macrophage Complement Receptor CRIg by TRIM72 Polarizes Innate Immunity of the Lung
Abstract The complement system plays a critical role in immune responses against pathogens. However, its identity and regulation… 
2016
2016
Lack of MG53 in human heart precludes utility as a biomarker of myocardial injury or endogenous cardioprotective factor.
AIMS Mitsugumin-53 (MG53/TRIM72) is an E3-ubiquitin ligase that rapidly accumulates at sites of membrane injury and plays an… 
Review
2016
Review
2016
Dual function of MG53 in membrane repair and insulin signaling
MG53 is a member of the TRIM-family protein that acts as a key component of the cell membrane repair machinery. MG53 is also an… 
2016
2016
Mitsugumin 53 regulates extracellular Ca2+ entry and intracellular Ca2+ release via Orai1 and RyR1 in skeletal muscle
Mitsugumin 53 (MG53) participates in the membrane repair of various cells, and skeletal muscle is the major tissue that expresses… 
Highly Cited
2015
Highly Cited
2015
Modulation of Wound Healing and Scar Formation by MG53 Protein-mediated Cell Membrane Repair*
Background: MG53 is a membrane repair gene whose role in wound healing has not been studied. Results: Topical administration of… 
2015
2015
Effect of Metabolic Syndrome on Mitsugumin 53 Expression and Function
Mitsugumin 53 (MG53) is a protein essential in cellular membrane repair. It facilitates the nucleation of intracellular vesicles… 
2015
2015
Upregulation of MG53 Induces Diabetic Cardiomyopathy Through Transcriptional Activation of Peroxisome Proliferation-Activated Receptor α
Background—Diabetic cardiomyopathy, which contributes to >50% diabetic death, is featured by myocardial lipid accumulation… 
2012
2012
The C2A domain in dysferlin is important for association with MG53 (TRIM72)
In skeletal muscle, Mitsugumin 53 (MG53), also known as muscle-specific tripartite motif 72, reportedly interacts with dysferlin… 
Highly Cited
2011
Highly Cited
2011
MG53 participates in ischaemic postconditioning through the RISK signalling pathway.
AIMS Recent studies show that ischaemic postconditioning (PostC), similar to the well-established ischaemic preconditioning (IPC… 
Highly Cited
2011
Highly Cited
2011
Dysferlin, Annexin A1, and Mitsugumin 53 Are Upregulated in Muscular Dystrophy and Localize to Longitudinal Tubules of the T-System With Stretch
Mutations in dysferlin cause an inherited muscular dystrophy because of defective membrane repair. Three interacting partners of… 
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