Evidence map›Paper›PMID 31294851›Full record

ArticleProteins2020

An NMR and MD study of complexes of bacteriophage lambda lysozyme with tetra- and hexa-N-acetylchitohexaose.

Aysegul Turupcu, Alice M Bowen, Alexandre Di Paolo, André Matagne, Chris Oostenbrink, Christina Redfield, Lorna J Smith

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proteins, 2020. 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
0.3field-weighted citation impact, top 44% 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, 3 citations in OpenAlex.

  1. Article
  2. Three-Dimensional Structures of Carbohydrates and Where to Find Them.International journal of molecular sciences · 2020
    Review
  3. Review
  4. 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

7 authors at 3 institutions in 3 countries.

Aysegul TurupcuInstitute of Molecular Modeling and Simulation, University of Natural Resources and Life Sciences Vienna, Vienna, Austria.
Alice M BowenDepartment of Chemistry, University of Oxford, Oxford, UK.
Alexandre Di PaoloLaboratoire d'Enzymologie et Repliement des Protéines, Centre d'Ingénierie des Protéines, Institut de Chimie, Université de Liège, Liège, Belgium.
André MatagneLaboratoire d'Enzymologie et Repliement des Protéines, Centre d'Ingénierie des Protéines, Institut de Chimie, Université de Liège, Liège, Belgium.
Chris OostenbrinkInstitute of Molecular Modeling and Simulation, University of Natural Resources and Life Sciences Vienna, Vienna, Austria.
Christina RedfieldDepartment of Biochemistry, University of Oxford, Oxford, UK.
Lorna J SmithDepartment of Chemistry, University of Oxford, Oxford, UK.ORCID 0000-0001-5040-9267
University of Oxford · GBBOKU University · ATUniversity of Liège · BE

Funding

Austrian Science Fund FWF BioToP grant number W1224Austrian Science Fund FWF W 1224Wellcome Trust Grant No. 079440
6 · The paper itself

Abstract

The X-ray structure of lysozyme from bacteriophage lambda (λ lysozyme) in complex with the inhibitor hexa-N-acetylchitohexaose (NAG6) (PDB: 3D3D) has been reported previously showing sugar units from two molecules of NAG6 bound in the active site. One NAG6 is bound with four sugar units in the ABCD sites and the other with two sugar units in the E'F' sites potentially representing the cleavage reaction products; each NAG6 cross links two neighboring λ lysozyme molecules. Here we use NMR and MD simulations to study the interaction of λ lysozyme with the inhibitors NAG4 and NAG6 in solution. This allows us to study the interactions within the complex prior to cleavage of the polysaccharide.

Indexed as

Bacteriophage lambdaCatalytic DomainEnzyme InhibitorsMolecular Docking SimulationMolecular Dynamics SimulationMuramidaseNuclear Magnetic Resonance, BiomolecularOligosaccharidesProtein BindingProtein ConformationEnzyme InhibitorsMuramidaseN-acetylchitohexaoseOligosaccharidesligand bindinglysozymesmolecular dynamicsNMR spectroscopyoligosaccharides

Identifiers

PMID31294851
PMCPMC6916166
OpenAlexW2960525629

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.