Evidence map›Paper›PMID 23846692›Full record

ArticleThe Journal of biological chemistry2013

Engineering the pattern of protein glycosylation modulates the thermostability of a GH11 xylanase.

Raquel Fonseca-Maldonado, Davi Serradella Vieira, Juliana Sanchez Alponti, Eric Bonneil, Pierre Thibault, Richard John Ward

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 80 citations in OpenAlex.

  1. Computational Study of COACS omega · 2026
    Article
  2. Review
  3. Review
  4. A thermostable and highly active fungal GH3 β-glucosidase generated by random and saturation mutagenesis.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2025
    Article
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  19. UniqueJournal of biological engineering · 2019
    Article
  20. Article
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

6 authors at 4 institutions in 2 countries.

Raquel Fonseca-MaldonadoFrom the Departamento de Bioquímica e Imunologia, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, São Paulo CEP 14049-900, Brazil.
Davi Serradella Vieirathe Departamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, São Paulo CEP 14049-901, Brazil.
Juliana Sanchez Alpontithe Departamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, São Paulo CEP 14049-901, Brazil.
Eric Bonneilthe Institute for Research in Immunology and Cancer, Université de Montréal, Montreal, Quebec, Canada, and.
Pierre Thibaultthe Institute for Research in Immunology and Cancer, Université de Montréal, Montreal, Quebec, Canada, and.
Richard John Wardthe Departamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, São Paulo CEP 14049-901, Brazil,; the Laboratório Nacional de Ciência e Tecnologia do Bioetanol/Centro Nacional de Pesquisa em Energia e Materiais, Campinas, São Paulo CEP 13083-970, Brazil. Electronic address: rjward@ffclrp.usp.br.
Institute for Research in Immunology and Cancer · CAUniversidade de São Paulo · BRUniversidade Estadual de Campinas (UNICAMP) · BRUniversité de Montréal · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein glycosylation is a common post-translational modification, the effect of which on protein conformational and stability is incompletely understood. Here we have investigated the effects of glycosylation on the thermostability of Bacillus subtilis xylanase A (XynA) expressed in Pichia pastoris. Intact mass analysis of the heterologous wild-type XynA revealed two, three, or four Hex(8-16)GlcNAc2 modifications involving asparagine residues at positions 20, 25, 141, and 181. Molecular dynamics (MD) simulations of the XynA modified with various combinations of branched Hex9GlcNAc2 at these positions indicated a significant contribution from protein-glycan interactions to the overall energy of the glycoproteins. The effect of glycan content and glycosylation position on protein stability was evaluated by combinatorial mutagenesis of all six potential N-glycosylation sites. The majority of glycosylated enzymes expressed in P. pastoris presented increased thermostability in comparison with their unglycosylated counterparts expressed in Escherichia coli. Steric effects of multiple glycosylation events were apparent, and glycosylation position rather than the number of glycosylation events determined increases in thermostability. The MD simulations also indicated that clustered glycan chains tended to favor less stabilizing glycan-glycan interactions, whereas more dispersed glycosylation patterns favored stabilizing protein-glycan interactions.

Indexed as

Protein EngineeringBacillus subtilisBacterial ProteinsEndo-1,4-beta XylanasesEnzyme StabilityEscherichia coliGlycosylationHot TemperatureMutagenesisPichiaRecombinant ProteinsBacterial ProteinsEndo-1,4-beta XylanasesRecombinant ProteinsGlycoside HydrolasesGlycosylationMass Spectrometry (MS)Molecular Dynamics SimulationProtein DesignProtein EngineeringProtein Thermostability

Identifiers

PMID23846692
PMCPMC3757213
OpenAlexW2057984012

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.