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

Charged surface area of maurocalcine determines its interaction with the skeletal ryanodine receptor.

Biophysical journal - 1 Oct 2008

Lukács Balázs, Sztretye Mónika, Almássy János, Sárközi Sándor, Dienes Beatrix, Mabrouk Kamel, Simut Cecilia, Szabó László, Szentesi Péter, De Waard Michel, Ronjat Michel, Jóna István, Csernoch László

Abstract excerpt

The 33 amino acid scorpion toxin maurocalcine (MCa) has been shown to modify the gating of the skeletal-type ryanodine receptor (RyR1). Here we explored the effects of MCa and its mutants ([Ala(8)]MCa, [Ala(19)]MCa, [Ala(20)]MCa, [Ala(22)]MCa, [Ala(23)]MCa, and [Ala(24)]MCa) on RyR1 incorporated into artificial lipid bilayers and on elementary calcium release events (ECRE) in rat and frog skeletal muscle fibers....

Read the complete abstract on PubMed

Topics

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

Share to Calcium Channels
Share to Calcium-Transporting ATPases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytosol

Share to Muscle Fibers, Skeletal

Share to Permeability

Share to Ryanodine Receptor Calcium Release Channel

Share to Scorpion Venoms

Share to Surface Properties

Source

Open in PubMed Open full text

Identifiers

PMID: 18621823
DOI: 10.1529/biophysj.107.120840
PMCID: PMC2547443

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Charged surface area of maurocalcine determines its interaction with the skeletal ryanodine receptor.PMID 18621823Read ↗

An α-helical C-terminal tail segment of the skeletal L-type Ca2+ channel β1a subunit activates ryanodine receptor type 1 via a hydrophobic surface.Semantic proximity Read ↗

Activating the ryanodine receptor with dihydropyridine receptor II-III loop segments: size and charge do matter.Semantic proximity Read ↗

Mammalian skeletal muscle voltage-gated sodium channels are affected by scorpion depressant "insect-selective" toxins when preconditioned.Semantic proximity Read ↗

Structure-based mechanism of RyR channel operation by calcium and magnesium ionsSemantic proximity Read ↗

Different regions in skeletal and cardiac muscle ryanodine receptors are involved in transducing the functional effects of calmodulin.Semantic proximity Read ↗

Characterization of gating and peptide block of mSlo, a cloned calcium-dependent potassium channel.Semantic proximity Read ↗

The predicted TM10 transmembrane sequence of the cardiac Ca2+ release channel (ryanodine receptor) is crucial for channel activation and gating.Semantic proximity Read ↗

Maurotoxin versus Pi1/HsTx1 scorpion toxins. Toward new insights in the understanding of their distinct disulfide bridge patterns.Semantic proximity Read ↗

The N terminus of a schistosome beta subunit regulates inactivation and current density of a Cav2 channel.Semantic proximity Read ↗

Disulfide bridge reorganization induced by proline mutations in maurotoxin.Semantic proximity Read ↗

Molecular dynamic studies on the impact of mutations on the structure, stability, and N-terminal orientation of annexin A1: implications for membrane aggregation.Semantic proximity Read ↗

Removal of clustered positive charge from dihydropyridine receptor II-III loop peptide augments activation of ryanodine receptors.Semantic proximity Read ↗

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