Evidence map›Paper›PMID 41065555›Full record

ArticleJournal of the American Chemical Society2025

Shaping the Glycan Landscape: Hidden Relationships between Linkage and Ring Distortions Induced by Carbohydrate-Active Enzymes.

Isabell Louise Grothaus, Paul Spellerberg, Carme Rovira, Lucio Colombi Ciacchi

Erratum issuedAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Crystal structure ofProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Isabell Louise GrothausHybrid Materials Interfaces Group, Bremen Center for Computational Materials Science and MAPEX Center for Materials and Processes, University of Bremen, 28359 Bremen, Germany.ORCID 0000-0002-0441-3860
Paul SpellerbergFaculty for Biology and Chemistry, University of Bremen, 28359 Bremen, Germany.
Carme RoviraDepartament de Química Inorgànica i Orgànica & IQTCUB, Universitat de Barcelona, Barcelona 08028, Spain.ORCID 0000-0003-1477-5010
Lucio Colombi CiacchiHybrid Materials Interfaces Group, Bremen Center for Computational Materials Science and MAPEX Center for Materials and Processes, University of Bremen, 28359 Bremen, Germany.ORCID 0000-0003-1444-9733

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbohydrate-active enzymes (CAZymes) catalyze glycan remodeling by forming and cleaving glycosidic bonds. An often-observed aspect of their catalytic mechanisms, particularly in glycosidases, is monosaccharide ring distortion that brings the substrate from a stable solution conformation to a reactive state. To what extent this distortion is promoted by steric constraints in the enzyme's binding pocket or by more elusive dynamical effects associated with the glycan conformational flexibility is still a matter of debate. In our work, we quantify the conformational phase-space changes experienced by glycans upon CAZyme binding by means of enhanced-sampling molecular dynamics simulations. Our results reveal a novel correlation between torsional degrees of freedom along the glycosidic bonds and the pucker degrees of freedom within the mannose ring at the -1 subsite of glycan M5G0 upon binding to the Golgi α-mannosidase II enzyme. Key factors driving this torsional phase-space reshaping and the associated transition from solution

Indexed as

PolysaccharidesCarbohydrate ConformationMolecular Dynamics SimulationPolysaccharides

Identifiers

PMID41065555
PMCPMC12550843

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.