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Emyr Lloyd-Evans

Researcher at Cardiff University

Publications -  63
Citations -  3632

Emyr Lloyd-Evans is an academic researcher from Cardiff University. The author has contributed to research in topics: Lysosomal storage disease & Biology. The author has an hindex of 22, co-authored 48 publications receiving 3159 citations. Previous affiliations of Emyr Lloyd-Evans include National Institutes of Health & University of Oxford.

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Niemann-Pick disease type C1 is a sphingosine storage disease that causes deregulation of lysosomal calcium

TL;DR: It is found that NPC1-mutant cells have a large reduction in the acidic compartment calcium store compared to wild-type cells, which represents a new target for therapeutic intervention, as elevation of cytosolic calcium with curcumin normalized NPC1 disease cellular phenotypes and prolonged survival of the NPC1 mouse.
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Molecular mechanisms of endolysosomal Ca2+ signalling in health and disease

TL;DR: The role of the Ca2+-mobilizing messenger NAADP (nicotinic acid adenine dinucleotide phosphate) as a major regulator of Ca2+, and the recent discovery of an endolysosomal channel family, the TPCs (two-pore channels), as its principal intracellular targets are discussed.
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Presenilin 1 Maintains Lysosomal Ca2+ Homeostasis via TRPML1 by Regulating vATPase-Mediated Lysosome Acidification

TL;DR: The results indicate that vATPase deficiency in PS1 loss-of-function states causes lysosomal/autophagy deficits and contributes to abnormal cellular Ca(2+) homeostasis, thus linking two AD-related pathogenic processes through a common molecular mechanism.
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Purified TPC Isoforms Form NAADP Receptors with Distinct Roles for Ca2+ Signaling and Endolysosomal Trafficking

TL;DR: This study shows that immunopurified endogenous TPC complexes possess the hallmark properties ascribed to NAADP receptors, including nanomolar ligand affinity, and proposes that NAadP regulates endolysosomal Ca2+ storage and release via TPCs and coordinates endoplasmic reticulum Ca2+.
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Accumulation of glycosphingolipids in niemann-pick C disease disrupts endosomal transport

TL;DR: It is suggested that accumulating GSL is part of a mislocalized membrane microdomain and is responsible for the deficit in endocytic trafficking found in Niemann-Pick type C disease.