Evidence map›Paper›PMID 17374510›Full record

ArticleComputational biology and chemistry2007

Computational characterization and design of SARS coronavirus receptor recognition and antibody neutralization.

Yuan Zhang, Nan Zheng, Yang Zhong

Abstract read
In one paragraph

Article in Computational biology and chemistry, 2007. 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. Viral quasispecies evolution.Microbiology and molecular biology reviews : MMBR · 2012
    Review
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.

Yuan ZhangSchool of Life Sciences, Fudan University, Shanghai 200433, China. yuanzhang5@fudan.edu.cn
Nan Zheng
Yang Zhong

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The sequential determination of crystal structures of the SARS coronavirus spike receptor-binding domain (RBD) in complex with its cellular receptor or neutralizing antibody opened a door for the design and development of antiviral competitive inhibitors. Based on those complex structures, we conduct computational characterization and design of RBD-mediated receptor recognition and antibody neutralization. The comparisons between computational predictions and experimental evidences validate our structural bioinformatics protocols. And the calculations predict a number of single substitutions on RBD, receptor or antibody that could remarkably elevate the binding affinities of those complexes. It is reasonable to anticipate our structure-based computation-derived hypotheses could be informative to the future biochemical and immunological tests.

Indexed as

Computational BiologyMembrane GlycoproteinsSevere acute respiratory syndrome-related coronavirusViral Envelope ProteinsAntibodies, MonoclonalAntibodies, ViralBinding Sites, AntibodyCrystallography, X-RayDrug DesignNeutralization TestsReceptors, VirusSpike Glycoprotein, CoronavirusAntibodies, MonoclonalAntibodies, ViralMembrane GlycoproteinsReceptors, VirusSpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVViral Envelope Proteins

Identifiers

PMID17374510
PMCPMC7106420

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.