Disease: Charcot-Marie-Tooth disease- Type 1C
- A dysfunctional endolysosomal pathway common to two sub-types of demyelinating Charcot-Marie-Tooth disease
- A novel LITAF/SIMPLE mutation within a family with a demyelinating form of Charcot-Marie-Tooth disease
- A novel LITAF/SIMPLE variant within a family with minimal demyelinating Charcot-Marie-Tooth disease
- A Rare Case of Charcot-Marie-Tooth Disease Type 1C With an Unusual Presentation
- Atypical presentation of Charcot-Marie-Tooth disease type 1C with a new mutation: a case report
- Charcot-Marie-Tooth disease type 1C: Clinical and electrophysiological findings for the c.334G>a (p.Gly112Ser) Litaf/Simple mutation
- Charcot-Marie-Tooth disease type 1C: Clinical and electrophysiological findings for the c.334G>a (p.Gly112Ser) Litaf/Simple mutation
- Demyelinating Peripheral Neuropathy Caused by the p.R160H Mutation in the <em>LITAF</em> Gene
- Dysregulated Inflammatory Signaling upon Charcot-Marie-Tooth Type 1C Mutation of SIMPLE Protein
- Endosomal recycling tubule scission and integrin recycling involve the membrane curvature-supporting protein LITAF
- Genotype-Phenotype Correlations in Charcot-Marie-Tooth Disease Due to <em>MTMR2</em> Mutations and Implications in Membrane Trafficking
- Identification and clinical characterization of Charcot-Marie-Tooth disease type 1C patients with LITAF p.G112S mutation
- LITAF mutations associated with Charcot-Marie-Tooth disease 1C show mislocalization from the late endosome/lysosome to the mitochondria
- Nerve ultrasound in patients with CMT1C: description of 3 cases
- Phenotypic spectrum of Charcot-Marie-Tooth disease due to LITAF/SIMPLE mutations: a study of 18 patients
- Screening for SH3TC2 variants in Charcot-Marie-Tooth disease in a cohort of Chinese patients
- The Charcot Marie Tooth disease protein LITAF is a zinc-binding monotopic membrane protein
- The topology, structure and PE interaction of LITAF underpin a Charcot-Marie-Tooth disease type 1C
- Tryptophan to Glycine mutation in the position 116 leads to protein aggregation and decreases the stability of the LITAF protein
- Variants of uncertain significance in the era of next-generation sequencing