Evidence map›Paper›PMID 18544499›Full record

ReviewInternational review of cell and molecular biology2008

New insights into mechanism and regulation of actin capping protein.

John A Cooper, David Sept

Abstract readReview
In one paragraph

Review in International review of cell and molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 135 papers.

0numbers the graph read from it
0cells of the map it votes in
135citing papers in PubMed
–field-weighted citation impact
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

135 citing papers in PubMed.

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  15. We need to talk-how muscle stem cells communicate.Frontiers in cell and developmental biology · 2024
    Review
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75 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

2 authors.

John A CooperDepartment of Cell Biology, Washington University, St. Louis, MO 63110, USA.
David Sept

Funding

Molecular Mechanisms in Actin Assembly &Cell MotilityR01GM038542 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 1989 to 2013
$7.4M
NIGMS NIH HHS GM 38542NIGMS NIH HHS GM 67426NIGMS NIH HHS R01 GM038542
6 · The paper itself

Abstract

The heterodimeric actin capping protein, referred to here as "CP," is an essential element of the actin cytoskeleton, binding to the barbed ends of actin filaments and regulating their polymerization. In vitro, CP has a critical role in the dendritic nucleation process of actin assembly mediated by Arp2/3 complex, and in vivo, CP is important for actin assembly and actin-based process of morphogenesis and differentiation. Recent studies have provided new insight into the mechanism of CP binding the barbed end, which raises new possibilities for the dynamics of CP and actin in cells. In addition, a number of molecules that bind and regulate CP have been discovered, suggesting new ideas for how CP may integrate into diverse processes of cell physiology.

Indexed as

Actin Capping ProteinsActinsAdaptor Proteins, Signal TransducingAnimalsCarrier ProteinsCell MembraneCytoskeletal ProteinsDynactin ComplexIntercellular Signaling Peptides and ProteinsMicrofilament ProteinsMicrotubule-Associated ProteinsModels, MolecularPhylogenyProtein ConformationProtein IsoformsProtein SubunitsActin Capping ProteinsActinsAdaptor Proteins, Signal TransducingCarmil1 protein, mouseCarrier ProteinsCD2-associated proteinCytoskeletal ProteinsDynactin ComplexIntercellular Signaling Peptides and ProteinsMicrofilament ProteinsMicrotubule-Associated ProteinsmyotrophinProtein IsoformsProtein Subunits

Identifiers

PMID18544499
PMCPMC2583073

What OpenQuestion holds

Textmetadata
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.