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

Two rings of negative charges in the cytosolic vestibule of type-1 ryanodine receptor modulate ion fluxes.

Biophysical journal - 15 Jan 2006

Xu Le, Wang Ying, Gillespie Dirk, Meissner Gerhard

Abstract excerpt

The tetrameric ryanodine receptor calcium release channels (RyRs) are cation-selective channels that have pore architecture similar to that of K+ channels. We recently identified, in close proximity to the selectivity filter motif GGGIG, a conserved lumenal DE motif that has a critical role in RyR ion permeation and selectivity. Here, we substituted three aspartate residues (D4938, D4945, D4953) with asparagine...

Read the complete abstract on PubMed

Topics

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

Share to Asparagine
Share to Biophysical Phenomena
Share to Biophysics

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cations

Share to Lipid Bilayers

Share to Neomycin

Share to Sarcoplasmic Reticulum

Source

Open in PubMed Open full text

Identifiers

PMID: 16239337
DOI: 10.1529/biophysj.105.072538
PMCID: PMC1367051

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Two rings of negative charges in the cytosolic vestibule of type-1 ryanodine receptor modulate ion fluxes.PMID 16239337Read ↗

Probing the role of negatively charged amino acid residues in ion permeation of skeletal muscle ryanodine receptor.Semantic proximity Read ↗

Changes in negative charge at the luminal mouth of the pore alter ion handling and gating in the cardiac ryanodine-receptor.Semantic proximity Read ↗

The Cardiac Ryanodine Receptor N-Terminal Region Contains an Anion Binding Site that Is Targeted by Disease MutationsSemantic proximity Read ↗

(De)constructing the ryanodine receptor: modeling ion permeation and selectivity of the calcium release channel.Semantic proximity Read ↗

Ryanodine receptors: structure and function.Semantic proximity Read ↗

The ryanodine receptor: a pivotal Ca2+ regulatory protein and potential therapeutic drug target.Semantic proximity Read ↗

The amino-terminal disease hotspot of ryanodine receptors forms a cytoplasmic vestibule.Semantic proximity Read ↗

A domain peptide of the cardiac ryanodine receptor regulates channel sensitivity to luminal Ca2+ via cytoplasmic Ca2+ sites.Semantic proximity Read ↗

An inner-pore mutation (F315D) promotes intracellular Mg2+ block and inward rectification of BK channels.Semantic proximity Read ↗

Three-dimensional perspective on ryanodine receptor mutations causing skeletal and cardiac muscle-related diseases.Semantic proximity Read ↗

Ryanodine receptor type 1 (RyR1) mutations C4958S and C4961S reveal excitation-coupled calcium entry (ECCE) is independent of sarcoplasmic reticulum store depletion.Semantic proximity Read ↗

Regulation of K+ flow by a ring of negative charges in the outer pore of BKCa channels. Part I: Aspartate 292 modulates K+ conduction by external surface charge effect.Semantic proximity Read ↗

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