Evidence map›Paper›PMID 18056414›Full record

ArticleThe Journal of cell biology2007

Structural basis of filamin A functions.

Fumihiko Nakamura, Teresia M Osborn, Christopher A Hartemink, John H Hartwig, Thomas P Stossel

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 166 papers.

0numbers the graph read from it
0cells of the map it votes in
166citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

166 citing papers in PubMed, 279 citations in OpenAlex.

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  17. PACSIN2 regulates platelet integrin β1 hemostatic function.Journal of thrombosis and haemostasis : JTH · 2023
    Article
  18. [Molecular dynamics simulation of force-regulated interaction between glycoprotein IbSheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi · 2023
    Article
  19. Article
  20. Article

106 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

5 authors at 3 institutions in 2 countries.

Fumihiko NakamuraTranslational Medicine Division, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA. fnakamura@rics.bwh.harvard.edu
Teresia M Osborn
Christopher A Hartemink
John H Hartwig
Thomas P Stossel
Brigham and Women's Hospital · USHarvard University · USUniversity of Gothenburg · SE

Funding

PHAGOCYTOSIS--PULMONARY ALVEOLAR MACROPHAGESR01HL019429 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI STOSSEL, THOMAS PETER · 1985 to 2015
$10.1M
REGULATION OF PLATELET SHAPE CHANGESR01HL056252 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI HARTWIG, JOHN H · 1996 to 2008
$3.3M
PHAGOCYTOSIS: PULMONARY ALVEOLAR MACROPHAGESR37HL019429 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI STOSSEL, THOMAS PETER · 1989 to 1998
–
NHLBI NIH HHS HL19429NHLBI NIH HHS HL56252NHLBI NIH HHS R01 HL019429NHLBI NIH HHS R01 HL056252
6 · The paper itself

Abstract

Filamin A (FLNa) can effect orthogonal branching of F-actin and bind many cellular constituents. FLNa dimeric subunits have N-terminal spectrin family F-actin binding domains (ABDs) and an elongated flexible segment of 24 immunoglobulin (Ig) repeats. We generated a library of FLNa fragments to examine their F-actin binding to define the structural properties of FLNa that enable its various functions. We find that Ig repeats 9-15 contain an F-actin-binding domain necessary for high avidity F-actin binding. Ig repeats 16-24, where most FLNa-binding partners interact, do not bind F-actin, and thus F-actin does not compete with Ig repeat 23 ligand, FilGAP. Ig repeats 16-24 have a compact structure that suggests their unfolding may accommodate pre-stress-mediated stiffening of F-actin networks, partner binding, mechanosensing, and mechanoprotection properties of FLNa. Our results also establish the orientation of FLNa dimers in F-actin branching. Dimerization, mediated by FLNa Ig repeat 24, accounts for rigid high-angle FLNa/F-actin branching resistant to bending by thermal forces, and high avidity F-actin binding and cross-linking.

Indexed as

Actin CytoskeletonActinsBinding SitesCell Line, TumorContractile ProteinsCross-Linking ReagentsCytoskeletonDimerizationFilaminsGTPase-Activating ProteinsHumansMicrofilament ProteinsMutant ProteinsPeptide FragmentsProtein BindingProtein Structure, TertiaryActinsARHGAP24 protein, humanContractile ProteinsCross-Linking ReagentsFilaminsGTPase-Activating ProteinsMicrofilament ProteinsMutant ProteinsPeptide FragmentsProtein SubunitsRecombinant Proteins

Identifiers

PMID18056414
PMCPMC2099194
OpenAlexW2064818197

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.