Evidence map›Paper›PMID 26516868›Full record

ReviewMarine drugs2015

Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to Phenotypes.

Pascal Viens, Marie-Ève Lacombe-Harvey, Ryszard Brzezinski

Open access · goldAbstract readReview
In one paragraph

Review in Marine drugs, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 77 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Targeting Non-ACS omega · 2025
    Article
  5. Improved Enzymatic Properties of Chitosanase CsnMY002 fromInternational journal of molecular sciences · 2025
    Article
  6. Article
  7. Article
  8. Characterization of 5'-nucleotidases secreted from Streptomyces.Applied microbiology and biotechnology · 2023
    Article
  9. Insights into promiscuous chitosanases: the known and the unknown.Applied microbiology and biotechnology · 2022
    Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

3 authors at 1 institution in 1 country.

Pascal ViensBiologie, Faculté des Sciences, Université de Sherbrooke, 2500, boul. de l'Université, Sherbrooke, QC J1K 2R1, Canada. Pascal.Viens@USherbrooke.ca.
Marie-Ève Lacombe-HarveyBiologie, Faculté des Sciences, Université de Sherbrooke, 2500, boul. de l'Université, Sherbrooke, QC J1K 2R1, Canada. marie-eve.lacombe@videotron.ca.
Ryszard BrzezinskiBiologie, Faculté des Sciences, Université de Sherbrooke, 2500, boul. de l'Université, Sherbrooke, QC J1K 2R1, Canada. Ryszard.Brzezinski@USherbrooke.ca.
Université de Sherbrooke · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chitosanases, enzymes that catalyze the endo-hydrolysis of glycolytic links in chitosan, are the subject of numerous studies as biotechnological tools to generate low molecular weight chitosan (LMWC) or chitosan oligosaccharides (CHOS) from native, high molecular weight chitosan. Glycoside hydrolases belonging to family GH46 are among the best-studied chitosanases, with four crystallography-derived structures available and more than forty enzymes studied at the biochemical level. They were also subjected to numerous site-directed mutagenesis studies, unraveling the molecular mechanisms of hydrolysis. This review is focused on the taxonomic distribution of GH46 proteins, their multi-modular character, the structure-function relationships and their biological functions in the host organisms.

Indexed as

AnimalsChitosanCrystallographyGlycoside HydrolasesHumansHydrolysisMolecular WeightMutagenesis, Site-DirectedOligosaccharidesPhenotypeChitosanchitosanaseGlycoside HydrolasesOligosaccharidesBacilluschitosanchitosanasechlorovirusglycoside hydrolasehydrolysisMicrobacteriumpolysaccharideStreptomyces

Identifiers

PMID26516868
PMCPMC4663542
OpenAlexW1855901990

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.