Evidence map›Paper›PMID 30392063›Full record

ReviewBiophysical reviews2018

Mechanisms of formin-mediated actin assembly and dynamics.

Naomi Courtemanche

Open access · bronzeAbstract readReview
In one paragraph

Review in Biophysical reviews, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

95 citing papers in PubMed, 162 citations in OpenAlex.

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  19. The Role of the Swollen State in Cell Proliferation.The Journal of membrane biology · 2025
    Review
  20. Article

35 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

1 author at 1 institution in 1 country.

Naomi CourtemancheDepartment of Genetics, Cell and Developmental Biology, University of Minnesota, 420 Washington Ave SE, 6-130 MCB, Minneapolis, MN, 55455, USA. ncourtem@umn.edu.ORCID http://orcid.org/0000-0003-4374-4782
University of Minnesota · US

Funding

Molecular mechanisms of bundled actin structure assembly by forminsR01GM122787 · NIGMS · UNIVERSITY OF MINNESOTA · PI Naomi Courtemanche · 2017 to 2026
$2.7M
National Institute of General Medical Sciences GM122787NIGMS NIH HHS R01 GM122787
6 · The paper itself

Abstract

Cellular viability requires tight regulation of actin cytoskeletal dynamics. Distinct families of nucleation-promoting factors enable the rapid assembly of filament nuclei that elongate and are incorporated into diverse and specialized actin-based structures. In addition to promoting filament nucleation, the formin family of proteins directs the elongation of unbranched actin filaments. Processive association of formins with growing filament ends is achieved through continuous barbed end binding of the highly conserved, dimeric formin homology (FH) 2 domain. In cooperation with the FH1 domain and C-terminal tail region, FH2 dimers mediate actin subunit addition at speeds that can dramatically exceed the rate of spontaneous assembly. Here, I review recent biophysical, structural, and computational studies that have provided insight into the mechanisms of formin-mediated actin assembly and dynamics.

Indexed as

ActinForminPolymerizationProfilin

Identifiers

PMID30392063
PMCPMC6297096
OpenAlexW2898961399

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.