Evidence map›Paper›PMID 18621823›Full record

ArticleBiophysical journal2008

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

Balázs Lukács, Mónika Sztretye, János Almássy, Sándor Sárközi, Beatrix Dienes, Kamel Mabrouk, Cecilia Simut, László Szabó, Péter Szentesi, Michel De Waard and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.6field-weighted citation impact, top 33% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 22 citations in OpenAlex.

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  9. In cellulo phosphorylation induces pharmacological reprogramming of maurocalcin, a cell-penetrating venom peptide.Proceedings of the National Academy of Sciences of the United States of America · 2016
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  14. Multiple actions of phi-LITX-Lw1a on ryanodine receptors reveal a functional link between scorpion DDH and ICK toxins.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 2 institutions in 3 countries.

Balázs LukácsDepartment of Physiology, Research Centre for Molecular Medicine, Medical and Health Science Centre, University of Debrecen, Debrecen, Hungary.
Mónika Sztretye
János Almássy
Sándor Sárközi
Beatrix Dienes
Kamel Mabrouk
Cecilia Simut
László Szabó
Péter Szentesi
Michel De Waard
Michel Ronjat
István Jóna
László Csernoch
University of Debrecen · HUUniversité Joseph Fourier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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. The peptides induced long-lasting subconductance states (LLSS) on RyR1 that lasted for several seconds. However, their average length and frequency were decreased if the mutation was placed farther away in the 3D structure from the critical (24)Arg residue. The effect was strongly dependent on the direction of the current through the channel. If the direction was similar to that followed by calcium during release, the peptides were 8- to 10-fold less effective. In fibers long-lasting calcium release events were observed after the addition of the peptides. The average length of these events correlated well with the duration of LLSS. These data suggest that the effect of the peptide is governed by the large charged surface formed by residues Lys(20), Lys(22), Arg(23), Arg(24), and Lys(8). Our observations also indicate that the results from bilayer experiments mimic the in situ effects of MCa on RyR1.

Indexed as

AnimalsCalciumCalcium ChannelsCalcium-Transporting ATPasesCytosolDose-Response Relationship, DrugIon Channel GatingMuscle Fibers, SkeletalMuscle, SkeletalMutationPermeabilityProtein BindingRana esculentaRatsRyanodine Receptor Calcium Release ChannelScorpion VenomsCalciumCalcium ChannelsCalcium-Transporting ATPasesmaurocalcineRyanodine Receptor Calcium Release ChannelScorpion Venoms

Identifiers

PMID18621823
PMCPMC2547443
OpenAlexW2041069228

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.