Evidence map›Paper›PMID 8947553›Full record

ArticleThe Journal of cell biology1996

Bundling of actin filaments by elongation factor 1 alpha inhibits polymerization at filament ends.

J W Murray, B T Edmonds, G Liu, J Condeelis

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

39 citing papers in PubMed, 107 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

J W MurrayDepartment of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
B T Edmonds
G Liu
J Condeelis
Albert Einstein College of Medicine · US

Funding

INTERACTIONS OF ACTIN CYTOSKELETON WITH PLASMA MEMBRANER01GM025813 · NIGMS · YESHIVA UNIVERSITY · PI CONDEELIS, JOHN S · 1985 to 2003
$1.5M
CYTOSKELETAL ORGANIZATION AND MALIGNANT TRANSFORMATIONT32CA009475 · NCI · YESHIVA UNIVERSITY · PI SATIR, PETER · 1985 to 2002
$621k
NCI NIH HHS 5T32 CA09475-10NIGMS NIH HHS GM25813
6 · The paper itself

Abstract

Elongation factor 1 alpha (EF1 alpha) is an abundant protein that binds aminoacyl-tRNA and ribosomes in a GTP-dependent manner. EF1 alpha also interacts with the cytoskeleton by binding and bundling actin filaments and microtubules. In this report, the effect of purified EF1 alpha on actin polymerization and depolymerization is examined. At molar ratios present in the cytosol, EF1 alpha significantly blocks both polymerization and depolymerization of actin filaments and increases the final extent of actin polymer, while at high molar ratios to actin, EF1 alpha nucleates actin polymerization. Although EF1 alpha binds actin monomer, this monomer-binding activity does not explain the effects of EF1 alpha on actin polymerization at physiological molar ratios. The mechanism for the inhibition of polymerization is related to the actin-bundling activity of EF1 alpha. Both ends of the actin filament are inhibited for polymerization and both bundling and the inhibition of actin polymerization are affected by pH within the same physiological range; at high pH both bundling and the inhibition of actin polymerization are reduced. Additionally, it is seen that the binding of aminoacyl-tRNA to EF1 alpha releases EF1 alpha's inhibiting effect on actin polymerization. These data demonstrate that EF1 alpha can alter the assembly of F-actin, a filamentous scaffold on which non-membrane-associated protein translation may be occurring in vivo.

Indexed as

Actin CytoskeletonActinsGuanosine DiphosphateGuanosine TriphosphateHydrogen-Ion ConcentrationLightMathematicsMicroscopy, ElectronPeptide Elongation Factor 1Peptide Elongation FactorsPolymersRNA, Transfer, Amino AcylScattering, RadiationActinsGuanosine DiphosphateGuanosine TriphosphatePeptide Elongation Factor 1Peptide Elongation FactorsPolymersRNA, Transfer, Amino Acyl

Identifiers

PMID8947553
PMCPMC2121097
OpenAlexW2058028915

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.