Evidence map›Paper›PMID 32877175›Full record

ArticleJournal of the American Chemical Society2020

Glycoside Hydrolases Restrict the Side Chain Conformation of Their Substrates To Gain Additional Transition State Stabilization.

Jonathan C K Quirke, David Crich

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Unnatural C6-Substituted d-Galactosides as Attenuated Substrates of Glycosyl Hydrolases.Chembiochem : a European journal of chemical biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Influence of Side Chain Conformation on the Activity of Glycosidase Inhibitors.Angewandte Chemie (International ed. in English) · 2023
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. 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

2 authors at 1 institution in 1 country.

Jonathan C K QuirkeDepartment of Pharmaceutical and Biomedical Sciences, University of Georgia, 250 West Green Street, Athens, Georgia 30602, United States.ORCID 0000-0002-5877-2770
David CrichDepartment of Pharmaceutical and Biomedical Sciences, University of Georgia, 250 West Green Street, Athens, Georgia 30602, United States.ORCID 0000-0003-2400-0083
University of Georgia · US

Funding

Methods and Mechanisms in Carbohydrate ChemistryR01GM062160 · NIGMS · WAYNE STATE UNIVERSITY · PI CRICH, DAVID · 2001 to 2024
$7.1M
NIGMS NIH HHS R01 GM062160
6 · The paper itself

Abstract

Carbohydrate side chain conformation confers a significant influence on reactivity during glycosylation and anomeric bond hydrolysis due to stabilization of the oxocarbenium-like transition state. By analysis of 513 pyranoside-bound glycoside hydrolase (GH) crystal structures, we determine that most glucosidases and β-mannosidases preferentially bind their substrates in the most reactive

Indexed as

1-DeoxynojirimycinCarbohydrate ConformationCarbohydratesCrystallography, X-RayEnzyme InhibitorsGlycoside HydrolasesGlycosylationHydrolysisIndolizidinesIndolizinesLigandsModels, MolecularNeuraminic AcidsPhase TransitionProtein BindingProtein Stability1-DeoxynojirimycinCarbohydratescastanospermineEnzyme InhibitorsGlycoside HydrolasesIndolizidinesIndolizinesLigandsNeuraminic Acids

Identifiers

PMID32877175
PMCPMC7544649
OpenAlexW3081961888

What OpenQuestion holds

Textmetadata
LicenceTDM
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.