Evidence map›Paper›PMID 9557880›Full record

ArticleGlycoconjugate journal1998

Studies on the conformational behaviour of GlcNAc-Man3-GlcNAc2 oligosaccharides using molecular dynamics simulations.

T Kozar, I Tvaroska, J P Carver

Abstract read
PubMed Publisher
In one paragraph

Article in Glycoconjugate journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

3 authors.

T KozarGlycoDesign Inc., Toronto, Ontario, Canada. tibor@glycodesign.com
I Tvaroska
J P Carver

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Three-dimensional structures of the natural substrate unit for the enzyme N-acetylglucosamine-transferase II, GIcNAc-Man3-GlcNAc2, were investigated by molecular modelling methods. Molecular dynamics (MD) and molecular mechanics calculations on two hexasaccharides, namely GlcNAc-Man3-GlcNAc2-Asn and GlcNAc-Man3-GlcNAc2-OMe were performed by the Biosym/MSI software using the CVFF and CFF95 force fields in vacuum. The MD simulations were calculated for 3 ns at different simulation temperatures and for two values of dielectric constant, epsilon=1 and epsilon=4. From each 3 ns trajectory, 3050 structures have been optimized. The local minima obtained have been clustered into families exhibiting similar values of glycosidic torsional angles phi, psi, and omega. The influence of the simulation conditions and force fields used on the conformational behaviour and structure of the title oligosaccharides is discussed.

Indexed as

AcetylglucosamineCarbohydrate ConformationCarbohydrate SequenceComputer SimulationModels, MolecularMolecular Sequence DataN-AcetylglucosaminyltransferasesOligosaccharidesAcetylglucosamineN-AcetylglucosaminyltransferasesOligosaccharides

Identifiers

What OpenQuestion holds

Textmetadata
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.