Evidence map›Paper›PMID 25433700›Full record

ArticleCell2014

The structure and regulation of human muscle α-actinin.

Euripedes de Almeida Ribeiro, Nikos Pinotsis, Andrea Ghisleni, Anita Salmazo, Petr V Konarev, Julius Kostan, Björn Sjöblom, Claudia Schreiner, Anton A Polyansky, Eirini A Gkougkoulia and 8 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed
8.7field-weighted citation impact, top 2% 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

126 citing papers in PubMed, 224 citations in OpenAlex.

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  16. Cryo-EM structure revealed a novel F-actin binding motif in abioRxiv : the preprint server for biology · 2025
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66 more citing papers are in PubMed but not listed here.

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

18 authors at 11 institutions in 7 countries.

Euripedes de Almeida RibeiroDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna, Austria.
Nikos PinotsisDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna, Austria.
Andrea GhisleniBritish Heart Foundation Centre of Research Excellence, Randall Division for Cell and Molecular Biophysics and Cardiovascular Division, King's College London, London SE1 1UL, UK.
Anita SalmazoDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna, Austria.
Petr V KonarevEuropean Molecular Biology Laboratory, Deutsches Elektronen-Synchrotron, Notkestrasse 85, 22603 Hamburg, Germany.
Julius KostanDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna, Austria.
Björn SjöblomDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna, Austria.
Claudia SchreinerDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna, Austria.
Anton A PolyanskyDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna, Austria; M.M. Shemyakin and Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.
Eirini A GkougkouliaDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna, Austria.
Mark R HoltBritish Heart Foundation Centre of Research Excellence, Randall Division for Cell and Molecular Biophysics and Cardiovascular Division, King's College London, London SE1 1UL, UK.
Finn L AachmannDepartment of Biotechnology, Norwegian University of Science and Technology, Sem Sælands vei 6/8, 7491 Trondheim, Norway.
Bojan ZagrovićDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna, Austria.
Enrica BordignonLaboratory of Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, 8093 Zurich, Switzerland; Fachbereich Physik, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany.
Katharina F PirkerDivision of Biochemistry, Department of Chemistry, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Dmitri I SvergunEuropean Molecular Biology Laboratory, Deutsches Elektronen-Synchrotron, Notkestrasse 85, 22603 Hamburg, Germany.
Mathias GautelBritish Heart Foundation Centre of Research Excellence, Randall Division for Cell and Molecular Biophysics and Cardiovascular Division, King's College London, London SE1 1UL, UK. Electronic address: mathias.gautel@kcl.ac.uk.
Kristina Djinović-CarugoDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna, Austria; Department of Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Aškerčeva 5, 1000 Ljubljana, Slovenia. Electronic address: kristina.djinovic@univie.ac.at.
Max Perutz Labs · ATUniversity of Vienna · ATVienna Biocenter · ATKing's College London · GBBOKU University · ATBritish Heart Foundation · GBDeutsches Elektronen-Synchrotron DESY · DEETH Zurich · CHEuropean Molecular Biology Laboratory · DENorwegian University of Science and Technology · NOUniversity of Ljubljana · SI

Funding

Austrian Science Fund FWF I 1593Austrian Science Fund FWF I 525British Heart Foundation CH/08/001European Research Council 279408Medical Research Council G0200496Medical Research Council G0600251Medical Research Council MR/J010456/1Medical Research Council MR/K015664/1
6 · The paper itself

Abstract

The spectrin superfamily of proteins plays key roles in assembling the actin cytoskeleton in various cell types, crosslinks actin filaments, and acts as scaffolds for the assembly of large protein complexes involved in structural integrity and mechanosensation, as well as cell signaling. α-actinins in particular are the major actin crosslinkers in muscle Z-disks, focal adhesions, and actin stress fibers. We report a complete high-resolution structure of the 200 kDa α-actinin-2 dimer from striated muscle and explore its functional implications on the biochemical and cellular level. The structure provides insight into the phosphoinositide-based mechanism controlling its interaction with sarcomeric proteins such as titin, lays a foundation for studying the impact of pathogenic mutations at molecular resolution, and is likely to be broadly relevant for the regulation of spectrin-like proteins.

Indexed as

ActininAmino Acid SequenceBinding SitesCrystallography, X-RayHumansLigandsModels, MolecularMolecular Sequence DataMuscle, SkeletalProtein Structure, TertiaryScattering, Small AngleSequence AlignmentX-Ray DiffractionActininACTN2 protein, humanLigands

Identifiers

PMID25433700
PMCPMC4259493
OpenAlexW2076143388

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.