Evidence map›Paper›PMID 25324850›Full record

ReviewFrontiers in plant science2014

Cell wall O-glycoproteins and N-glycoproteins: aspects of biosynthesis and function.

Eric Nguema-Ona, Maïté Vicré-Gibouin, Maxime Gotté, Barbara Plancot, Patrice Lerouge, Muriel Bardor, Azeddine Driouich

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in plant science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
20.1field-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

83 citing papers in PubMed, 163 citations in OpenAlex.

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  13. Intrinsic Mechanism of CaClInternational journal of molecular sciences · 2024
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23 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

7 authors at 2 institutions in 1 country.

Eric Nguema-OnaLaboratoire de Glycobiologie et Matrice Extracellulaire Végétale, UPRES EA 4358, Institut de Recherche et d'Innovation Biomédicale, Grand Réseau de Recherche-Végétal, Agronomie, Sol, Innovation, UFR des Sciences et Techniques, Normandie Université - Université de Rouen Mont-Saint-Aignan, France.
Maïté Vicré-GibouinLaboratoire de Glycobiologie et Matrice Extracellulaire Végétale, UPRES EA 4358, Institut de Recherche et d'Innovation Biomédicale, Grand Réseau de Recherche-Végétal, Agronomie, Sol, Innovation, UFR des Sciences et Techniques, Normandie Université - Université de Rouen Mont-Saint-Aignan, France.
Maxime GottéLaboratoire de Glycobiologie et Matrice Extracellulaire Végétale, UPRES EA 4358, Institut de Recherche et d'Innovation Biomédicale, Grand Réseau de Recherche-Végétal, Agronomie, Sol, Innovation, UFR des Sciences et Techniques, Normandie Université - Université de Rouen Mont-Saint-Aignan, France.
Barbara PlancotLaboratoire de Glycobiologie et Matrice Extracellulaire Végétale, UPRES EA 4358, Institut de Recherche et d'Innovation Biomédicale, Grand Réseau de Recherche-Végétal, Agronomie, Sol, Innovation, UFR des Sciences et Techniques, Normandie Université - Université de Rouen Mont-Saint-Aignan, France.
Patrice LerougeLaboratoire de Glycobiologie et Matrice Extracellulaire Végétale, UPRES EA 4358, Institut de Recherche et d'Innovation Biomédicale, Grand Réseau de Recherche-Végétal, Agronomie, Sol, Innovation, UFR des Sciences et Techniques, Normandie Université - Université de Rouen Mont-Saint-Aignan, France.
Muriel BardorLaboratoire de Glycobiologie et Matrice Extracellulaire Végétale, UPRES EA 4358, Institut de Recherche et d'Innovation Biomédicale, Grand Réseau de Recherche-Végétal, Agronomie, Sol, Innovation, UFR des Sciences et Techniques, Normandie Université - Université de Rouen Mont-Saint-Aignan, France ; Institut Universitaire de France Paris, France.
Azeddine DriouichLaboratoire de Glycobiologie et Matrice Extracellulaire Végétale, UPRES EA 4358, Institut de Recherche et d'Innovation Biomédicale, Grand Réseau de Recherche-Végétal, Agronomie, Sol, Innovation, UFR des Sciences et Techniques, Normandie Université - Université de Rouen Mont-Saint-Aignan, France ; Plate-Forme de Recherche en Imagerie Cellulaire de Haute-Normandie, Institut de Recherche et d'Innovation Biomédicale, Faculté des Sciences et Techniques, Normandie Université Mont-Saint-Aignan, France.
Normandie Université · FRInstitut Universitaire de France · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell wall O-glycoproteins and N-glycoproteins are two types of glycomolecules whose glycans are structurally complex. They are both assembled and modified within the endomembrane system, i.e., the endoplasmic reticulum (ER) and the Golgi apparatus, before their transport to their final locations within or outside the cell. In contrast to extensins (EXTs), the O-glycan chains of arabinogalactan proteins (AGPs) are highly heterogeneous consisting mostly of (i) a short oligo-arabinoside chain of three to four residues, and (ii) a larger β-1,3-linked galactan backbone with β-1,6-linked side chains containing galactose, arabinose and, often, fucose, rhamnose, or glucuronic acid. The fine structure of arabinogalactan chains varies between, and within plant species, and is important for the functional activities of the glycoproteins. With regards to N-glycans, ER-synthesizing events are highly conserved in all eukaryotes studied so far since they are essential for efficient protein folding. In contrast, evolutionary adaptation of N-glycan processing in the Golgi apparatus has given rise to a variety of organism-specific complex structures. Therefore, plant complex-type N-glycans contain specific glyco-epitopes such as core β,2-xylose, core α1,3-fucose residues, and Lewis(a) substitutions on the terminal position of the antenna. Like O-glycans, N-glycans of proteins are essential for their stability and function. Mutants affected in the glycan metabolic pathways have provided valuable information on the role of N-/O-glycoproteins in the control of growth, morphogenesis and adaptation to biotic and abiotic stresses. With regards to O-glycoproteins, only EXTs and AGPs are considered herein. The biosynthesis of these glycoproteins and functional aspects are presented and discussed in this review.

Indexed as

arabinogalactan proteincell wallendoplasmic reticulumextensinglycanglycosyltransferaseGolgi apparatusplants

Identifiers

PMID25324850
PMCPMC4183102
OpenAlexW2170400683

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.