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We report a novel LRSAM1 mutation c.2021-2024del (p.E674VfsX11) in 4 members of a Chinese autosomal dominant Charcot-Marie-Tooth disease type 2 family
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The article systematically represents the molecular functions, nature and detailed characterization of LRSAM1 E3 ubiquitin ligase, which are linked to molecular mechanisms of neurodegeneration. (Review)
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Our study shows the potential function of mir-939 through regulating LRSAM1 in Hirschsprung's disease
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We identified a novel LRSAM1 missense mutation (c.2120C > T, p.Pro707Leu) mapping to the RING domain. The identified missense mutation, as well as of another recently reported pathogenic missense mutation (c.2081G > A, p.Cys694Tyr), revealed that in vitro ubiquitylation activity was largely abrogated.
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findings suggest that the mutant LRSAM1 may aberrantly affect the formation of transcription machinery.
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findings demonstrate that the isolated genetic entity Charcot-Marie-Tooth type 2G is caused by a missense mutation in LRSAM1.
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LRSAM1 exhibited self-association in vitro and in vivo. The study found the self-association of LRSAM1 promotes intermolecular ubiquitination and proved a potential N-terminal ubiquitination.
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Plant homeodomain finger protein 23 negatively regulates cell autophagy by promoting ubiquitination and degradation of E3 ligase LRSAM1
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disruption of the C-terminal RING domain confers dominant negative properties to LRSAM1
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Our data further confirms that LRSAM1 mutations are associated with CMT2 of AD inheritance.
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Authors identify LRSAM1 as the E3 ligase responsible for anti-Salmonella autophagy-associated ubiquitination.
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homozygous mutation in LRSAM1 was proposed as a strong candidate for the disease in a family with recessive axonal polyneuropathy
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LRSAM1 as a component of the antibacterial autophagic response.
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LRSAM1 is a strong candidate for the causal gene for the Charcot-Marie-Tooth disease.
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Results suggest that RIFLE represents a novel signaling protein that mediates components of the Wnt/wingless signaling pathway and cell adhesion in PC12 cells [RIFLE protein].
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Tal regulates a Tsg101-associated complex responsible for the sorting of cargo into cytoplasm-containing vesicles that bud at the multivesicular body and at the plasma membrane
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Tal polyubiquitinates lysine residues in the C-terminus of uncomplexed Tsg101, resulting in proteasomal degradation.