Evidence map›Paper›PMID 25383767›Full record

ArticlePloS one2014

KORRIGAN1 interacts specifically with integral components of the cellulose synthase machinery.

Nasim Mansoori, Jaap Timmers, Thierry Desprez, Claire L Alvim-Kamei, Claire L A Kamei, Dianka C T Dees, Jean-Paul Vincken, Richard G F Visser, Herman Höfte, Samantha Vernhettes and 1 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
8.9field-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

31 citing papers in PubMed, 54 citations in OpenAlex.

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  13. Interference of ArabidopsisFrontiers in plant science · 2022
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 2 countries.

Nasim MansooriPlant Breeding, Wageningen University and Research Centre, Wageningen, The Netherlands; Graduate School Experimental Plant Sciences, Wageningen University, The Netherlands.
Jaap TimmersPlant Breeding, Wageningen University and Research Centre, Wageningen, The Netherlands; Graduate School Experimental Plant Sciences, Wageningen University, The Netherlands; Carbohydrate Research Centre, Wageningen University and Research Centre, Wageningen, The Netherlands.
Thierry DesprezLaboratoire de Biologie Cellulaire, Institute Jean-Pierre Bourgin, Institut National de la Recherche Agronomique, Versailles, France.
Claire L Alvim-KameiPlant Breeding, Wageningen University and Research Centre, Wageningen, The Netherlands.
Claire L A Kamei
Dianka C T DeesPlant Breeding, Wageningen University and Research Centre, Wageningen, The Netherlands.
Jean-Paul VinckenPlant Breeding, Wageningen University and Research Centre, Wageningen, The Netherlands.
Richard G F VisserPlant Breeding, Wageningen University and Research Centre, Wageningen, The Netherlands.
Herman HöfteLaboratoire de Biologie Cellulaire, Institute Jean-Pierre Bourgin, Institut National de la Recherche Agronomique, Versailles, France.
Samantha VernhettesLaboratoire de Biologie Cellulaire, Institute Jean-Pierre Bourgin, Institut National de la Recherche Agronomique, Versailles, France.
Luisa M TrindadePlant Breeding, Wageningen University and Research Centre, Wageningen, The Netherlands.
Wageningen University & Research · NLInstitut National de la Recherche Agronomique · MAGraduate School Experimental Plant Sciences · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellulose is synthesized by the so called rosette protein complex and the catalytic subunits of this complex are the cellulose synthases (CESAs). It is thought that the rosette complexes in the primary and secondary cell walls each contains at least three different non-redundant cellulose synthases. In addition to the CESA proteins, cellulose biosynthesis almost certainly requires the action of other proteins, although few have been identified and little is known about the biochemical role of those that have been identified. One of these proteins is KORRIGAN (KOR1). Mutant analysis of this protein in Arabidopsis thaliana showed altered cellulose content in both the primary and secondary cell wall. KOR1 is thought to be required for cellulose synthesis acting as a cellulase at the plasma membrane-cell wall interface. KOR1 has recently been shown to interact with the primary cellulose synthase rosette complex however direct interaction with that of the secondary cell wall has never been demonstrated. Using various methods, both in vitro and in planta, it was shown that KOR1 interacts specifically with only two of the secondary CESA proteins. The KOR1 protein domain(s) involved in the interaction with the CESA proteins were also identified by analyzing the interaction of truncated forms of KOR1 with CESA proteins. The KOR1 transmembrane domain has shown to be required for the interaction between KOR1 and the different CESAs, as well as for higher oligomer formation of KOR1.

Indexed as

ArabidopsisArabidopsis ProteinsCell MembraneCellulaseCell WallGlucosyltransferasesMembrane ProteinsProtein BindingProtein MultimerizationProtein Structure, QuaternaryProtein Structure, TertiarySubstrate SpecificityArabidopsis ProteinsCellulasecellulose synthaseGlucosyltransferasesKOR1 protein, ArabidopsisMembrane Proteins

Identifiers

PMID25383767
PMCPMC4226561
OpenAlexW1990169724

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.