Evidence map›Paper›PMID 8061523›Full record

ArticleThe Plant cell1994

A calmodulin-sensitive interaction between microtubules and a higher plant homolog of elongation factor-1 alpha.

N A Durso, R J Cyr

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
5.5field-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

52 citing papers in PubMed, 179 citations in OpenAlex.

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  15. eEF1A: thinking outside the ribosome.The Journal of biological chemistry · 2010
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Microtubule-associated proteins in higher plants.Journal of plant research · 2007
    Review
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 at 1 institution in 1 country.

N A DursoDepartment of Biology, Pennsylvania State University, University Park 16802.
R J Cyr
Pennsylvania State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The microtubules (MTs) of higher plant cells are organized into arrays with essential functions in plant cell growth and differentiation; however, molecular mechanisms underlying the organization and regulation of these arrays remain largely unknown. We have approached this problem using tubulin affinity chromatography to isolate carrot proteins that interact with MTs. From these proteins, a 50-kD polypeptide was selectively purified by exploiting its Ca(2+)-dependent binding to calmodulin (CaM). This polypeptide was identified as a homolog of elongation factor-1 alpha (EF-1 alpha)--a highly conserved and ubiquitous protein translation factor. The carrot EF-1 alpha homolog bundles MTs in vitro, and moreover, this bundling is modulated by the addition of Ca2+ and CaM together (Ca2+/CaM). A direct binding between the EF-1 alpha homolog and MTs was demonstrated, providing novel evidence for such an interaction. Based on these findings, and others discussed herein, we propose that an EF-1 alpha homolog mediates the lateral association of MTs in plant cells by a Ca2+/CaM-sensitive mechanism.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCalciumCalmodulinCattleChromatography, AffinityElectrophoresis, Polyacrylamide GelGene Expression RegulationHumansMicrotubulesMolecular Sequence DataMultigene FamilyPeptide Elongation Factor 1Peptide Elongation FactorsPlant DevelopmentCalciumCalmodulinPeptide Elongation Factor 1Peptide Elongation FactorsPlant Proteins, DietaryTubulin

Identifiers

PMID8061523
PMCPMC160487
OpenAlexW2045606678

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.