Evidence map›Paper›PMID 20538977›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2 (WH2) domains of Spire and the implication for filament nucleation.

Anna M Ducka, Peteranne Joel, Grzegorz M Popowicz, Kathleen M Trybus, Michael Schleicher, Angelika A Noegel, Robert Huber, Tad A Holak, Tomasz Sitar

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. 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
2.8field-weighted citation impact, top 10% 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, 44 citations in OpenAlex.

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  14. In vitro studies of actin filament and network dynamics.Current opinion in cell biology · 2013
    Review
  15. Ablation of cyclase-associated protein 2 (CAP2) leads to cardiomyopathy.Cellular and molecular life sciences : CMLS · 2013
    Article
  16. Article
  17. Article
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  19. Article
  20. Molecular architecture of the Spire-actin nucleus and its implication for actin filament assembly.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
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 5 institutions in 3 countries.

Anna M DuckaMax-Planck-Institut für Biochemie, 82152 Martinsried, Germany.
Peteranne Joel
Grzegorz M Popowicz
Kathleen M Trybus
Michael Schleicher
Angelika A Noegel
Robert Huber
Tad A Holak
Tomasz Sitar
Max Planck Society · DEMax Planck Institute of Biochemistry · DEUniversity of Vermont · USLudwig-Maximilians-Universität München · DEUniversity of Cologne · DE

Funding

SMOOTH MUSCLE MYOSIN--CONFORMATION AND ACTIVITYR01HL038113 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 1993 to 2011
$3.9M
VASCULAR SMOOTH MUSCLE MYOSIN--CONFORMATION &ACTIVITYR29HL038113 · NHLBI · BRANDEIS UNIVERSITY · PI TRYBUS, KATHLEEN M · 1987 to 1991
–
NHLBI NIH HHS R01 HL038113
6 · The paper itself

Abstract

Three classes of proteins are known to nucleate new filaments: the Arp2/3 complex, formins, and the third group of proteins that contain ca. 25 amino acid long actin-binding Wiskott-Aldrich syndrome protein homology 2 domains, called the WH2 repeats. Crystal structures of the complexes between the actin-binding WH2 repeats of the Spire protein and actin were determined for the Spire single WH2 domain D, the double (SpirCD), triple (SpirBCD), quadruple (SpirABCD) domains, and an artificial Spire WH2 construct comprising three identical D repeats (SpirDDD). SpirCD represents the minimal functional core of Spire that can nucleate actin filaments. Packing in the crystals of the actin complexes with SpirCD, SpirBCD, SpirABCD, and SpirDDD shows the presence of two types of assemblies, "side-to-side" and "straight-longitudinal," which can serve as actin filament nuclei. The principal feature of these structures is their loose, open conformations, in which the sides of actins that normally constitute the inner interface core of a filament are flipped inside out. These Spire structures are distant from those seen in the filamentous nuclei of Arp2/3, formins, and in the F-actin filament.

Indexed as

ActinsAmino Acid SequenceAnimalsCrystallography, X-RayDrosophila ProteinsFemaleIn Vitro TechniquesMicrofilament ProteinsModels, MolecularMolecular Sequence DataMultiprotein ComplexesNuclear Magnetic Resonance, BiomolecularProtein Interaction Domains and MotifsProtein Structure, TertiaryRecombinant ProteinsSequence Homology, Amino AcidActinsDrosophila ProteinsMicrofilament ProteinsMultiprotein ComplexesRecombinant Proteinsspir protein, DrosophilaWiskott-Aldrich Syndrome Protein Family

Identifiers

PMID20538977
PMCPMC2900636
OpenAlexW2035793728

What OpenQuestion holds

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Registered trials

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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.