Evidence map›Paper›PMID 11706187›Full record

ArticlePlant physiology2001

Rapid deposition of extensin during the elicitation of grapevine callus cultures is specifically catalyzed by a 40-kilodalton peroxidase.

P A Jackson, C I Galinha, C S Pereira, A Fortunato, N C Soares, S B Amâncio, C P Pinto Ricardo

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.8field-weighted citation impact, top 6% 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

29 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Article
  3. Class III Peroxidases PRX01, PRX44, and PRX73 Control Root Hair Growth inInternational journal of molecular sciences · 2022
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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

7 authors at 1 institution in 1 country.

P A JacksonInstituto de Tecnologia Química e Biológica, Apartado 127, 2781-901 Oeiras, Portugal.
C I Galinha
C S Pereira
A Fortunato
N C Soares
S B Amâncio
C P Pinto Ricardo
Instituto de Biologia Experimental e Tecnológica · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Elicitation or peroxide stimulation of grape (Vitis vinifera L. cv Touriga) vine callus cultures results in the rapid and selective in situ insolubilization of an abundant and ionically bound cell wall protein-denominated GvP1. Surface-enhanced laser desorption/ionization/time of flight-mass spectrometry analysis, the amino acid composition, and the N-terminal sequence of purified GvP1 identified it as an 89.9-kD extensin. Analysis of cell walls following the in situ insolubilization of GvP1 indicates large and specific increases in the major amino acids of GvP1 as compared with the amino acids present in salt-eluted cell walls. We calculate that following deposition, covalently bound GvP1 contributes up to 4% to 5% of the cell wall dry weight. The deposition of GvP1 in situ requires peroxide and endogenous peroxidase activity. Isoelectric focusing of saline eluates of callus revealed only a few basic peroxidases that were all isolated or purified to electrophoretic homogeneity. In vitro and in situ assays of extensin cross-linking activity using GvP1 and peroxidases showed that a 40-kD peroxidase cross-linked GvP1 within minutes, whereas other grapevine peroxidases had no significant activity with GvP1. Internal peptide sequences indicated this extensin peroxidase (EP) is a member of the class III peroxidases. We conclude that we have identified and purified an EP from grapevine callus that is responsible for the catalysis of GvP1 deposition in situ during elicitation. Our results suggest that GvP1 and this EP play an important combined role in grapevine cell wall defense.

Indexed as

Plant ProteinsAdaptation, PhysiologicalCatalysisCell WallCulture TechniquesGlycoproteinsImmunity, InnatePeroxidasePlant DiseasesVitisextensin protein, plantGlycoproteinsPeroxidasePlant Proteins

Identifiers

PMID11706187
PMCPMC129276
OpenAlexW1992058985

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.