Associated Papers
A scalable approach to resolving variants of uncertain significance.
Tejura M et al.
Biorxiv : the Preprint Server for Biology, 2026
41727046 (PubMed )
Supplement: media-7.xlsx › VarChAMP_data_supp_mat_PP
Proteostasis plays an important role in demyelinating Charcot Marie Tooth disease.
Libberecht K et al.
Biochemical Pharmacology, 2023
Identification and clinical characterization of Charcot-Marie-Tooth disease type 1C patients with LITAF p.G112S mutation.
Park J et al.
Genes & Genomics, 2022
Charcot-Marie-Tooth disease type 1C: Clinical and electrophysiological findings for the c.334G>a (p.Gly112Ser) Litaf/Simple mutation.
Jerath NU et al.
Muscle & Nerve, 2017
The Charcot Marie Tooth disease protein LITAF is a zinc-binding monotopic membrane protein.
Qin W et al.
The Biochemical Journal, 2016
Tryptophan to Glycine mutation in the position 116 leads to protein aggregation and decreases the stability of the LITAF protein.
Kumar CV et al.
Journal of Biomolecular Structure & Dynamics, 2015
LITAF mutations associated with Charcot-Marie-Tooth disease 1C show mislocalization from the late endosome/lysosome to the mitochondria.
Lacerda AF et al.
Plos One, 2014
SIMPLE: A new regulator of endosomal trafficking and signaling in health and disease.
Chin LS et al.
Communicative & Integrative Biology, 2013
Charcot-Marie-Tooth disease-linked protein SIMPLE functions with the ESCRT machinery in endosomal trafficking.
Lee SM et al.
The Journal of Cell Biology, 2012
Mutations associated with Charcot-Marie-Tooth disease cause SIMPLE protein mislocalization and degradation by the proteasome and aggresome-autophagy pathways.
Lee SM et al.
Journal of Cell Science, 2011
SIMPLE mutation analysis in dominant demyelinating Charcot-Marie-Tooth disease: three novel mutations.
Latour P et al.
Journal of the Peripheral Nervous System : Jpns, 2006
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