Evidence map›Paper›PMID 8587980›Full record

ArticlePlant physiology1996

Characterization of an endo-beta-1,4-glucanase gene induced by auxin in elongating pea epicotyls.

S C Wu, J M Blumer, A G Darvill, P Albersheim

Open access · greenAbstract readComparative Study
In one paragraph

Article in Plant physiology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
15.0field-weighted citation impact, top 1% 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

17 citing papers in PubMed, 61 citations in OpenAlex.

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  17. A membrane-anchored E-type endo-1,4-beta-glucanase is localized on Golgi and plasma membranes of higher plants.Proceedings of the National Academy of Sciences of the United States of America · 1997
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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.

S C WuDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens 30602-4712, USA.
J M Blumer
A G Darvill
P Albersheim
University of Georgia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A gene (EGL1) encoding an endo-beta-1,4-D-glucanase (EGase, EC 3.2.1.4) of pea (Pisum sativum) has been cloned and characterized. EGL1 encodes a 486-amino acid polypeptide, including a 24-mer putative signal peptide. The mature protein has a calculated molecular mass of 51.3 kD and an isoelectric point of 9.1. This pea EGase shares significant similarity with EGases from other plant species, but it appears to be distinct from the EGases associated with abscission and fruit ripening. Although EGL1 transcripts are detected in all parts of pea plants, they are relatively abundant in flowers and young pods undergoing rapid growth and most abundant in elongating epicotyls of etiolated seedlings. When epicotyl segments (6 mm long, 4 mm from the apical hook) are incubated in a 5 microM solution of the synthetic auxin analog 2,4-dichlorophenoxyacetic acid, the concentration of EGL1 mRNA increases about 10-fold when the segments elongate most rapidly.

Indexed as

Gene Expression Regulation, PlantGenes, Plant2,4-Dichlorophenoxyacetic AcidAmino Acid SequenceBase SequenceCellulaseCloning, MolecularDNA, ComplementaryIndoleacetic AcidsMolecular Sequence DataPisum sativumPlant ProteinsPlant ShootsRNA, MessengerRNA, PlantSequence Analysis, DNA2,4-Dichlorophenoxyacetic AcidCellulaseDNA, Complementaryendoglucanase EGL1Indoleacetic AcidsPlant ProteinsRNA, MessengerRNA, Plant

Identifiers

PMID8587980
PMCPMC157705
OpenAlexW2096746739

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.