Evidence map›Paper›PMID 32250657›Full record

ArticleJournal of computational biology : a journal of computational molecular cell biology2020

Backbone Free Energy Estimator Applied to Viral Glycoproteins.

Robert C Penner

Abstract read
In one paragraph

Article in Journal of computational biology : a journal of computational molecular cell biology, 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
–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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. RecombinantVaccines · 2021
    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

1 author.

Robert C PennerInstitut des Hautes Études Scientifiques, Bures-sur-Yvette, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Earlier analysis of the Protein Data Bank derived the distribution of rotations from the plane of a protein hydrogen bond donor peptide group to the plane of its acceptor peptide group. The quasi Boltzmann formalism of Pohl-Finkelstein is employed to estimate free energies of protein elements with these hydrogen bonds, pinpointing residues with a high propensity for conformational change. This is applied to viral glycoproteins as well as capsids, where the 90th+ percentiles of free energies determine residues that correlate well with viral fusion peptides and other functional domains in known cases and thus provide a novel method for predicting these sites of importance as antiviral drug or vaccine targets in general. The method is implemented at https://bion-server.au.dk/hbonds/ from an uploaded Protein Data Bank file.

Indexed as

Computational BiologyDatabases, ProteinEncephalitis Viruses, Tick-BorneGlycoproteinsHemagglutinin Glycoproteins, Influenza VirusHumansHydrogen BondingInfluenza A virusMembrane GlycoproteinsModels, MolecularModels, StatisticalParamyxovirinaeProtein ConformationProtein StabilityThermodynamicsViral Envelope ProteinsGlycoproteinsG protein, vesicular stomatitis virusHemagglutinin Glycoproteins, Influenza VirusMembrane GlycoproteinsViral Envelope ProteinsViral Fusion ProteinsViral Proteinsantiviral drugsvaccine targetsviral glycoproteins

Identifiers

PMID32250657
PMCPMC7591380

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.