Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Activating mutations of the TRPML1 channel revealed by proline-scanning mutagenesis.

The Journal of biological chemistry - 13 Nov 2009

Dong Xian-ping, Wang Xiang, Shen Dongbiao, Chen Su, Liu Meiling, Wang Yanbin, Mills Eric, Cheng Xiping, Delling Markus, Xu Haoxing

Abstract excerpt

The mucolipin TRP (TRPML) proteins are a family of endolysosomal cation channels with genetically established importance in humans and rodent. Mutations of human TRPML1 cause type IV mucolipidosis, a devastating pediatric neurodegenerative disease. Our recent electrophysiological studies revealed...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Electrophysiology
Share to Exocytosis
Share to Kidney

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lysosomes

Share to Manganese

Share to Proline

Share to Transient Receptor Potential Channels

Share to TRPM Cation Channels

Source

Open in PubMed Open full text

Identifiers

PMID: 19638346
DOI: 10.1074/jbc.M109.037184
PMCID: PMC2797275

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19638346-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Activating mutations of the TRPML1 channel revealed by proline-scanning mutagenesis.PMID 19638346Read ↗

Differential ion selectivity and disease-associated dysfunction of TRPML channels revealed by patient and engineered mutants.Semantic proximity Read ↗

TRPML1: an ion channel in the lysosome.Semantic proximity Read ↗

TRPML1 gating modulation by allosteric mutations and lipids.Semantic proximity Read ↗

TRPpathies.Semantic proximity Read ↗

Role of TRPML and two-pore channels in endolysosomal cation homeostasis.Semantic proximity Read ↗

The cation channel mucolipin-1 is a bifunctional protein that facilitates membrane remodeling via its serine lipase domain.Semantic proximity Read ↗

TRPML3.Semantic proximity Read ↗

Regulation of TRPML1 function.Semantic proximity Read ↗

Activating mutation in a mucolipin transient receptor potential channel leads to melanocyte loss in varitint-waddler mice.Semantic proximity Read ↗

The TRPML3 channel: from gene to function.Semantic proximity Read ↗

Identification of a gain-of-function mutation in a Golgi P-type ATPase that enhances Mn2+ efflux and protects against toxicity.Semantic proximity Read ↗

Functional multimerization of mucolipin channel proteins.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.