Evidence map›Paper›PMID 15591063›Full record

ArticleThe Journal of biological chemistry2005

Maurocalcine and domain A of the II-III loop of the dihydropyridine receptor Cav 1.1 subunit share common binding sites on the skeletal ryanodine receptor.

Xavier Altafaj, Weijun Cheng, Eric Estève, Julie Urbani, Didier Grunwald, Jean-Marc Sabatier, Roberto Coronado, Michel De Waard, Michel Ronjat

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
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  4. 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
    Article
  5. Scorpion venom components that affect ion-channels function.Toxicon : official journal of the International Society on Toxinology · 2013
    Review
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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

9 authors at 4 institutions in 2 countries.

Xavier AltafajINSERM U607/DRDC, CEA, 17 rue des Martyrs, 38054 Grenoble Cedex 09, France.
Weijun Cheng
Eric Estève
Julie Urbani
Didier Grunwald
Jean-Marc Sabatier
Roberto Coronado
Michel De Waard
Michel Ronjat
Commissariat à l'Énergie Atomique et aux Énergies Alternatives · FRInserm · FRUniversity of Wisconsin–Madison · USCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Maurocalcine is a scorpion venom toxin of 33 residues that bears a striking resemblance to the domain A of the dihydropyridine voltage-dependent calcium channel type 1.1 (Cav1.1) subunit. This domain belongs to the II-III loop of Cav1.1, which is implicated in excitation-contraction coupling. Besides the structural homology, maurocalcine also modulates RyR1 channel activity in a manner akin to a synthetic peptide of domain A. Because of these similarities, we hypothesized that maurocalcine and domain A may bind onto an identical region(s) of RyR1. Using a set of RyR1 fragments, we demonstrate that peptide A and maurocalcine bind onto two discrete RyR1 regions: fragments 3 and 7 encompassing residues 1021-1631 and 3201-3661, respectively. The binding onto fragment 7 is of greater importance and was thus further investigated. We found that the amino acid region 3351-3507 of RyR1 (fragment 7.2) is sufficient for these interactions. Proof that peptide A and maurocalcine bind onto the same site is provided by competition experiments in which binding of fragment 7.2 to peptide A is inhibited by preincubation with maurocalcine. Moreover, when expressed in COS-7 cells, RyR1 carrying a deletion of fragment 7 shows a loss of interaction with both peptide A and maurocalcine. At the functional level, this deletion abolishes the maurocalcine induced stimulation of [3H]ryanodine binding onto microsomes of transfected COS-7 cells without affecting the caffeine and ATP responses.

Indexed as

Adenosine TriphosphateAnimalsBinding, CompetitiveBinding SitesCalcium Channels, L-TypeCaveolin 1CaveolinsChromatographyCloning, MolecularCOS CellsCryoelectron MicroscopyMicroscopy, FluorescenceMuscle, SkeletalPeptidesPlasmidsProtein BindingAdenosine TriphosphateCalcium Channels, L-TypeCaveolin 1CaveolinsmaurocalcinePeptidesRecombinant Fusion ProteinsRyanodineRyanodine Receptor Calcium Release ChannelScorpion Venoms

Identifiers

PMID15591063
PMCPMC2712624
OpenAlexW1982294722

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.