Evidence map›Paper›PMID 35871440›Full record

ReviewGlycobiology2022

The SGNH hydrolase family: a template for carbohydrate diversity.

Alexander C Anderson, Stefen Stangherlin, Kyle N Pimentel, Joel T Weadge, Anthony J Clarke

Open access · hybridAbstract readReview
In one paragraph

Review in Glycobiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Frontiers in plant science · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Loss ofJBMR plus · 2025
    Article
  15. Article
  16. Plant Cell Wall PolysaccharidePlants (Basel, Switzerland) · 2024
    Review
  17. Loss ofbioRxiv : the preprint server for biology · 2024
    Article
  18. Article
  19. Article
  20. Evaluation of the Structure-Function Relationship of SGNH Lipase fromInternational journal of molecular sciences · 2024
    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

5 authors at 2 institutions in 1 country.

Alexander C AndersonDepartment of Molecular and Cellular Biology, University of Guelph, Guelph N1G2W1, Canada.ORCID 0000-0002-1870-2903
Stefen StangherlinDepartment of Chemistry & Biochemistry, Wilfrid Laurier University, Waterloo N2L3C5, Canada.ORCID 0000-0002-2953-4730
Kyle N PimentelDepartment of Molecular and Cellular Biology, University of Guelph, Guelph N1G2W1, Canada.ORCID 0000-0001-7459-1075
Joel T WeadgeDepartment of Biology, Wilfrid Laurier University, Waterloo N2L3C5, Canada.ORCID 0000-0002-8020-0015
Anthony J ClarkeDepartment of Molecular and Cellular Biology, University of Guelph, Guelph N1G2W1, Canada.ORCID 0000-0003-4076-0488
Wilfrid Laurier University · CAUniversity of Guelph · CA

Funding

CIHR PJT 156353
6 · The paper itself

Abstract

The substitution and de-substitution of carbohydrate materials are important steps in the biosynthesis and/or breakdown of a wide variety of biologically important polymers. The SGNH hydrolase superfamily is a group of related and well-studied proteins with a highly conserved catalytic fold and mechanism composed of 16 member families. SGNH hydrolases can be found in vertebrates, plants, fungi, bacteria, and archaea, and play a variety of important biological roles related to biomass conversion, pathogenesis, and cell signaling. The SGNH hydrolase superfamily is chiefly composed of a diverse range of carbohydrate-modifying enzymes, including but not limited to the carbohydrate esterase families 2, 3, 6, 12 and 17 under the carbohydrate-active enzyme classification system and database (CAZy.org). In this review, we summarize the structural and functional features that delineate these subfamilies of SGNH hydrolases, and which generate the wide variety of substrate preferences and enzymatic activities observed of these proteins to date.

Indexed as

CarbohydratesHydrolasesBiopolymersEsterasesProtein ConformationBiopolymersCarbohydratesEsterasesHydrolasescarbohydrate acetyltransferasecarbohydrate deacetylasecarbohydrate esteraseCAZyme structure–functionCE subfamilies

Identifiers

PMID35871440
PMCPMC9487903
OpenAlexW4286817335

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.