Evidence map›Paper›PMID 25177325›Full record

ReviewFrontiers in plant science2014

An update on post-translational modifications of hydroxyproline-rich glycoproteins: toward a model highlighting their contribution to plant cell wall architecture.

May Hijazi, Silvia M Velasquez, Elisabeth Jamet, José M Estevez, Cécile Albenne

Abstract 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 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
–field-weighted citation impact
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

66 citing papers in PubMed.

  1. Article
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  8. Article
  9. Differential prolyl hydroxylation by six Physcomitrella prolyl-4 hydroxylases.Computational and structural biotechnology journal · 2024
    Article
  10. Article
  11. Horticulture research · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Characterization of theInternational journal of molecular sciences · 2023
    Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article

6 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

5 authors.

May HijaziLaboratoire de Recherche en Sciences Végétales, Université de Toulouse, UPS, UMR 5546 Castanet-Tolosan, France ; CNRS, UMR 5546 Castanet-Tolosan, France.
Silvia M VelasquezFacultad de Ciencias Exactas y Naturales, Instituto de Fisiología, Biología Molecular y Neurociencias (IFIBYNE-CONICET), Universidad de Buenos Aires Buenos Aires, Argentina.
Elisabeth JametLaboratoire de Recherche en Sciences Végétales, Université de Toulouse, UPS, UMR 5546 Castanet-Tolosan, France ; CNRS, UMR 5546 Castanet-Tolosan, France.
José M EstevezFacultad de Ciencias Exactas y Naturales, Instituto de Fisiología, Biología Molecular y Neurociencias (IFIBYNE-CONICET), Universidad de Buenos Aires Buenos Aires, Argentina.
Cécile AlbenneLaboratoire de Recherche en Sciences Végétales, Université de Toulouse, UPS, UMR 5546 Castanet-Tolosan, France ; CNRS, UMR 5546 Castanet-Tolosan, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant cell walls are composite structures mainly composed of polysaccharides, also containing a large set of proteins involved in diverse functions such as growth, environmental sensing, signaling, and defense. Research on cell wall proteins (CWPs) is a challenging field since present knowledge of their role into the structure and function of cell walls is very incomplete. Among CWPs, hydroxyproline (Hyp)-rich O-glycoproteins (HRGPs) were classified into three categories: (i) moderately glycosylated extensins (EXTs) able to form covalent scaffolds; (ii) hyperglycosylated arabinogalactan proteins (AGPs); and (iii) Hyp/proline (Pro)-Rich proteins (H/PRPs) that may be non-, weakly- or highly-glycosylated. In this review, we provide a description of the main features of their post-translational modifications (PTMs), biosynthesis, structure, and function. We propose a new model integrating HRGPs and their partners in cell walls. Altogether, they could form a continuous glyco-network with non-cellulosic polysaccharides via covalent bonds or non-covalent interactions, thus strongly contributing to cell wall architecture.

Indexed as

arabinogalactan proteinextensinhydroxyprolineO-glycosylationproline-rich protein

Identifiers

PMID25177325
PMCPMC4132260

What OpenQuestion holds

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Registered trials

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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.