Evidence map›Paper›PMID 15161961›Full record

ArticleThe Plant cell2004

Silencing of hydroxycinnamoyl-coenzyme A shikimate/quinate hydroxycinnamoyltransferase affects phenylpropanoid biosynthesis.

Laurent Hoffmann, Sébastien Besseau, Pierrette Geoffroy, Christophe Ritzenthaler, Denise Meyer, Catherine Lapierre, Brigitte Pollet, Michel Legrand

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 238 papers.

0numbers the graph read from it
0cells of the map it votes in
238citing papers in PubMed
4.3field-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

238 citing papers in PubMed, 590 citations in OpenAlex.

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  18. Understanding genetic architecture overcomes tradeoffs between seed quality and insect resistance.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025
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178 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

8 authors at 2 institutions in 1 country.

Laurent HoffmannInstitut de Biologie Moléculaire des Plantes, Unité Propre de Recherche, 2357 du Centre National de la Recherche Scientifique, Université Louis Pasteur, 67000 Strasbourg, France.
Sébastien Besseau
Pierrette Geoffroy
Christophe Ritzenthaler
Denise Meyer
Catherine Lapierre
Brigitte Pollet
Michel Legrand
Institut de Biologie Moléculaire des Plantes · FRLaboratoire de Chimie · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The hydroxyl group in the 3-position of the phenylpropanoid compounds is introduced at the level of coumarate shikimate/quinate esters, whose synthesis implicates an acyltransferase activity. Specific antibodies raised against the recombinant tobacco (Nicotiana tabacum) acyltransferase revealed the accumulation of the enzyme in stem vascular tissues of tobacco, in accordance with a putative role in lignification. For functional analysis, the acyltransferase gene was silenced in Arabidopsis thaliana and N. benthamiana by RNA-mediated posttranscriptional gene silencing. In Arabidopsis, gene silencing resulted in a dwarf phenotype and changes in lignin composition as indicated by histochemical staining. An in-depth study of silenced N. benthamiana plants by immunological, histochemical, and chemical methods revealed the impact of acyltransferase silencing on soluble phenylpropanoids and lignin content and composition. In particular, a decrease in syringyl units and an increase in p-hydroxyphenyl units were recorded. Enzyme immunolocalization by confocal microscopy showed a correlation between enzyme accumulation levels and lignin composition in vascular cells. These results demonstrate the function of the acyltransferase in phenylpropanoid biosynthesis.

Indexed as

RNA InterferenceAcyltransferasesArabidopsisCellulaseCell WallChromatography, High Pressure LiquidGene Expression Regulation, PlantImmune SeraImmunohistochemistryIsomerismLigninMolecular Sequence DataNicotianaPlant RootsPlant StemsQuinic AcidAcyltransferasescaffeoylquinic acidCellulasehydroxycinnamoyl-CoA-quinate transferaseImmune SeraLigninQuinic Acid

Identifiers

PMID15161961
PMCPMC490038
OpenAlexW2165405896

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.