Evidence map›Paper›PMID 11381081›Full record

ArticleThe Journal of cell biology2001

An atomic model of actin filaments cross-linked by fimbrin and its implications for bundle assembly and function.

N Volkmann, D DeRosier, P Matsudaira, D Hanein

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

79 citing papers in PubMed, 161 citations in OpenAlex.

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  13. Getting cells into shape by calcium-dependent actin cross-linking proteins.Frontiers in cell and developmental biology · 2023
    Review
  14. Structural mechanism for bidirectional actin cross-linking by T-plastin.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Article
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  18. Review
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19 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

4 authors at 3 institutions in 1 country.

N VolkmannThe Burnham Institute, 10901 North Torrey Pines Rd., La Jolla, California 92037, USA.
D DeRosier
P Matsudaira
D Hanein
Sanford Burnham Prebys Medical Discovery Institute · USBrandeis University · USMassachusetts Institute of Technology · US

Funding

STRUCTURAL STUDIES OF CELLULAR ASSEMBLIES OF ACTINR01GM026357 · NIGMS · BRANDEIS UNIVERSITY · PI DEROSIER, DAVID J · 1985 to 2002
$791k
NIGMS NIH HHS GM26357NIGMS NIH HHS R01 GM026357
6 · The paper itself

Abstract

Actin bundles have profound effects on cellular shape, division, adhesion, motility, and signaling. Fimbrin belongs to a large family of actin-bundling proteins and is involved in the formation of tightly ordered cross-linked bundles in the brush border microvilli and in the stereocilia of inner ear hair cells. Polymorphism in these three-dimensional (3D) bundles has prevented the detailed structural characterization required for in-depth understanding of their morphogenesis and function. Here, we describe the structural characterization of two-dimensional arrays of actin cross-linked with human T-fimbrin. Structural information obtained by electron microscopy, x-ray crystallography, and homology modeling allowed us to build the first molecular model for the complete actin-fimbrin cross-link. The restriction of the arrays to two dimensions allowed us to deduce the spatial relationship between the components, the mode of fimbrin cross-linking, and the flexibility within the cross-link. The atomic model of the fimbrin cross-link, the cross-linking rules deduced from the arrays, and the hexagonal packing of actin bundles in situ were all combined to generate an atomic model for 3D actin-fimbrin bundles. Furthermore, the assembly of the actin-fimbrin arrays suggests coupling between actin polymerization, fimbrin binding, and crossbridge formation, presumably achieved by a feedback between conformational changes and changes in affinity.

Indexed as

Microfilament ProteinsActin CytoskeletonActinsBiopolymersCalciumCrystallography, X-RayFourier AnalysisHumansMembrane GlycoproteinsMicroscopy, ElectronModels, BiologicalModels, MolecularPliabilityProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryActinsBiopolymersCalciumMembrane GlycoproteinsMicrofilament Proteinsplastin

Identifiers

PMID11381081
PMCPMC2174342
OpenAlexW2114178648

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.