Evidence map›Paper›PMID 9334343›Full record

ArticleThe Journal of cell biology1997

Evidence for a conformational change in actin induced by fimbrin (N375) binding.

D Hanein, P Matsudaira, D J DeRosier

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

34 citing papers in PubMed, 105 citations in OpenAlex.

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  17. High-resolution cryo-EM structure of the F-actin-fimbrin/plastin ABD2 complex.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  18. Article
  19. The yeast actin cytoskeleton: from cellular function to biochemical mechanism.Microbiology and molecular biology reviews : MMBR · 2006
    Review
  20. Review
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

3 authors at 2 institutions in 1 country.

D HaneinThe W.M. Keck Institute for Cellular Visualization and The Rosenstiel Basic Medical Sciences Research Center, Department of Biology, Brandeis University, Waltham, Massachusetts 02254, USA.
P Matsudaira
D J DeRosier
Massachusetts Institute of Technology · USWhitehead Institute for Biomedical Research · US

Funding

STRUCTURAL STUDIES OF CELLULAR ASSEMBLIES OF ACTINR01GM026357 · NIGMS · BRANDEIS UNIVERSITY · PI DEROSIER, DAVID J · 1985 to 2002
$791k
IN VIVO NMR SPECTROSCOPY OF TUMOR RESPONSEP01CA044703 · NCI · JOHNS HOPKINS UNIVERSITY · PI GLICKSON, JERRY D · 1987 to 1989
–
NCI NIH HHS CA44703NIGMS NIH HHS GM26357NIGMS NIH HHS R01 GM026357
6 · The paper itself

Abstract

Fimbrin belongs to a superfamily of actin cross-linking proteins that share a conserved 27-kD actin-binding domain. This domain contains a tandem duplication of a sequence that is homologous to calponin. Calponin homology (CH) domains not only cross-link actin filaments into bundles and networks, but they also bind intermediate filaments and some signal transduction proteins to the actin cytoskeleton. This fundamental role of CH domains as a widely used actin-binding domain underlines the necessity to understand their structural interaction with actin. Using electron cryomicroscopy, we have determined the three-dimensional structure of F-actin and F-actin decorated with the NH2-terminal CH domains of fimbrin (N375). In a difference map between actin filaments and N375-decorated actin, one end of N375 is bound to a concave surface formed between actin subdomains 1 and 2 on two neighboring actin monomers. In addition, a fit of the atomic model for the actin filament to the maps reveals the actin residues that line, the binding surface. The binding of N375 changes actin, which we interpret as a movement of subdomain 1 away from the bound N375. This change in actin structure may affect its affinity for other actin-binding proteins and may be part of the regulation of the cytoskeleton itself. Difference maps between actin and actin decorated with other proteins provides a way to look for novel structural changes in actin.

Indexed as

Protein ConformationActinsAmino Acid SequenceAnimalsBinding SitesCalcium-Binding ProteinsCalponinsCloning, MolecularComputer SimulationConserved SequenceHumansMembrane GlycoproteinsMicrofilament ProteinsMicroscopy, ElectronModels, MolecularModels, StructuralActinsCalcium-Binding ProteinsCalponinsMembrane GlycoproteinsMicrofilament ProteinsplastinRecombinant Proteins

Identifiers

PMID9334343
PMCPMC2139807
OpenAlexW1967471059

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.