Evidence map›Paper›PMID 9722612›Full record

ArticleThe Journal of cell biology1998

Mechanism of Cdc42-induced actin polymerization in neutrophil extracts.

S H Zigmond, M Joyce, C Yang, K Brown, M Huang, M Pring

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

26 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
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  6. Cell biology of embryonic migration.Birth defects research. Part C, Embryo today : reviews · 2008
    Review
  7. Physiologic properties and regulation of the actin cytoskeleton in vascular smooth muscle.Journal of cardiovascular pharmacology and therapeutics · 2008
    Review
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  9. Article
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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

6 authors at 1 institution in 1 country.

S H ZigmondDepartment of Biology, University of Pennsylvania. Philadelphia, Pennsylvania 19104-6018, USA. szigmond@sas.upenn.edu
M Joyce
C Yang
K Brown
M Huang
M Pring
University of Pennsylvania · US

Funding

CELL BIOLOGY OF LOCOMOTION AND CHEMOTAXIS OF LEUKOCYTESR37AI019883 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI ZIGMOND, SALLY H · 1994 to 2003
$1.6M
PINOCYTOSIS IN POLYMORPHONUCLEAR LEUKOCYTESR01AI019883 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI ZIGMOND, SALLY H · 1985 to 1992
–
NIAID NIH HHS AI-19883
6 · The paper itself

Abstract

Cdc42, activated with GTPgammaS, induces actin polymerization in supernatants of lysed neutrophils. This polymerization, like that induced by agonists, requires elongation at filament barbed ends. To determine if creation of free barbed ends was sufficient to induce actin polymerization, free barbed ends in the form of spectrin-actin seeds or sheared F-actin filaments were added to cell supernatants. Neither induced polymerization. Furthermore, the presence of spectrin-actin seeds did not increase the rate of Cdc42-induced polymerization, suggesting that the presence of Cdc42 did not facilitate polymerization from spectrin-actin seeds such as might have been the case if Cdc42 inhibited capping or released G-actin from a sequestered pool. Electron microscopy revealed that Cdc42-induced filaments elongated rapidly, achieving a mean length greater than 1 micron in 15 s. The mean length of filaments formed from spectrin-actin seeds was <0.4 micron. Had spectrin-actin seeds elongated at comparable rates before they were capped, they would have induced longer filaments. There was little change in mean length of Cdc42-induced filaments between 15 s and 5 min, suggesting that the increase in F-actin over this time was due to an increase in filament number. These data suggest that Cdc42 induction of actin polymerization requires both creation of free barbed ends and facilitated elongation at these ends.

Indexed as

Actin CytoskeletonActinsAnimalsAscitic Fluidcdc42 GTP-Binding ProteinCell Cycle ProteinsCell ExtractsGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Microscopy, ElectronNeutrophilsParticle SizeRabbitsRecombinant ProteinsSpectrinActinscdc42 GTP-Binding ProteinCell Cycle ProteinsCell ExtractsGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Recombinant ProteinsSpectrin

Identifiers

PMID9722612
PMCPMC2132886
OpenAlexW2069763343

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.