Evidence map›Paper›PMID 36808948›Full record

ArticleBiochemistry2023

Conformational Control of Fast Asparagine Deamidation in a Norovirus Capsid Protein.

Robert Creutznacher, Eric Schulze-Niemand, Patrick König, Vesna Stanojlovic, Alvaro Mallagaray, Thomas Peters, Matthias Stein, Mario Schubert

Open access · hybridAbstract read
In one paragraph

Article in Biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Virus-Glycan Interactions Studied by Solute NMR.Methods in molecular biology (Clifton, N.J.) · 2025
    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

8 authors at 3 institutions in 2 countries.

Robert CreutznacherInstitute of Chemistry and Metabolomics, University of Lübeck, Ratzeburger Allee 160, 23562 Lübeck, Germany.
Eric Schulze-NiemandMolecular Simulations and Design Group, Max Planck Institute for Dynamics of Complex Technical Systems, Sandtorstrasse 1, 39106 Magdeburg, Germany.
Patrick KönigInstitute of Chemistry and Metabolomics, University of Lübeck, Ratzeburger Allee 160, 23562 Lübeck, Germany.
Vesna StanojlovicDepartment of Biosciences and Medical Biology, University of Salzburg, Hellbrunnerstrasse 34, 5020 Salzburg, Austria.
Alvaro MallagarayInstitute of Chemistry and Metabolomics, University of Lübeck, Ratzeburger Allee 160, 23562 Lübeck, Germany.
Thomas PetersInstitute of Chemistry and Metabolomics, University of Lübeck, Ratzeburger Allee 160, 23562 Lübeck, Germany.ORCID 0000-0002-7570-8260
Matthias SteinMolecular Simulations and Design Group, Max Planck Institute for Dynamics of Complex Technical Systems, Sandtorstrasse 1, 39106 Magdeburg, Germany.ORCID 0000-0001-7793-0052
Mario SchubertDepartment of Biosciences and Medical Biology, University of Salzburg, Hellbrunnerstrasse 34, 5020 Salzburg, Austria.ORCID 0000-0003-0278-4091
University of Lübeck · DEMax Planck Institute for Dynamics of Complex Technical Systems · DEUniversity of Salzburg · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Accelerated spontaneous deamidation of asparagine 373 and subsequent conversion into an isoaspartate has been shown to attenuate the binding of histo blood group antigens (HBGAs) to the protruding domain (P-domain) of the capsid protein of a prevalent norovirus strain (GII.4). Here, we link an unusual backbone conformation of asparagine 373 to its fast site-specific deamidation. NMR spectroscopy and ion exchange chromatography have been used to monitor the deamidation reaction of P-domains of two closely related GII.4 norovirus strains, specific point mutants, and control peptides. MD simulations over several microseconds have been instrumental to rationalize the experimental findings. While conventional descriptors such as available surface area, root-mean-square fluctuations, or nucleophilic attack distance fail as explanations, the population of a rare

Indexed as

Capsid ProteinsNorovirusAsparagineBinding SitesProtein BindingProtein DomainsAsparagineCapsid Proteins

Identifiers

PMID36808948
PMCPMC9996831
OpenAlexW4321437579

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.