Associated Papers
Differential ion selectivity and disease-associated dysfunction of TRPML channels revealed by patient and engineered mutants.
Rue BE et al.
The Journal of Biological Chemistry, 2026
A novel Bi-Allelic pathogenic MCOLN1 variant underlying mucolipidosis type IV in an Iranian family: clinical, genetic, and molecular dynamics-based structural analysis.
Mohsenipour M et al.
Bmc Medical Genomics, 2025
Exploring the impact of variations in the mucolipin1 protein that result in mucolipidosis type 4 using the technique of molecular docking and dynamics simulation.
K P et al.
Journal of Biomolecular Structure & Dynamics, 2024
Neurodegenerative Lysosomal Storage Disorders: TPC2 Comes to the Rescue!
Prat Castro S et al.
Cells, 2022
ConVarT: a search engine for matching human genetic variants with variants from non-human species.
Pir MS et al.
Nucleic Acids Research, 2022
Long-term observation of a Japanese mucolipidosis IV patient with a novel homozygous p.F313del variant of MCOLN1.
Hayashi T et al.
American Journal of Medical Genetics. Part A, 2020
Cryo-EM structures of the mammalian endo-lysosomal TRPML1 channel elucidate the combined regulation mechanism.
Zhang S et al.
Protein & Cell, 2017
BK channel agonist represents a potential therapeutic approach for lysosomal storage diseases.
Zhong XZ et al.
Scientific Reports, 2016
A small molecule restores function to TRPML1 mutant isoforms responsible for mucolipidosis type IV.
Chen CC et al.
Nature Communications, 2014
TRPML1: an ion channel in the lysosome.
Wang W et al.
Handbook of Experimental Pharmacology, 2014
Mucolipidosis type IV: an update.
Wakabayashi K et al.
Molecular Genetics and Metabolism, 2011
Functional multimerization of mucolipin channel proteins.
Curcio-Morelli C et al.
Journal of Cellular Physiology, 2010
The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel.
Dong XP et al.
Nature, 2008
Isolated ocular disease is associated with decreased mucolipin-1 channel conductance.
Goldin E et al.
Investigative Ophthalmology & Visual Science, 2008
Mucolipin-1 is a lysosomal membrane protein required for intracellular lactosylceramide traffic.
Pryor PR et al.
Traffic (copenhagen, Denmark), 2006
Cation channel activity of mucolipin-1: the effect of calcium.
Cantiello HF et al.
Pflugers Archiv : European Journal of Physiology, 2005
Overexpression of wild-type and mutant mucolipin proteins in mammalian cells: effects on the late endocytic compartment organization.
Manzoni M et al.
Febs Letters, 2004
Molecular pathophysiology of mucolipidosis type IV: pH dysregulation of the mucolipin-1 cation channel.
Raychowdhury MK et al.
Human Molecular Genetics, 2004
Mucolipidosis type IV is caused by mutations in a gene encoding a novel transient receptor potential channel.
Sun M et al.
Human Molecular Genetics, 2000