Evidence map›Paper›PMID 23903833›Full record

ArticleJournal of virology2013

Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus.

Yaoqing Chen, Kanagalaghatta R Rajashankar, Yang Yang, Sudhakar S Agnihothram, Chang Liu, Yi-Lun Lin, Ralph S Baric, Fang Li

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed, 1 pooled it
8.7field-weighted citation impact, top 1% 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

101 citing papers in PubMed, 1 synthesis or guideline pooled it, 133 citations in OpenAlex.

  1. Pooled it
  2. Article
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  4. Review
  5. Article
  6. Article
  7. Article
  8. Designed miniproteins potently inhibit and protect against MERS-CoV.bioRxiv : the preprint server for biology · 2024
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
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  15. Advances in mRNA and other vaccines against MERS-CoV.Translational research : the journal of laboratory and clinical medicine · 2022
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

41 more citing papers are in PubMed but not listed here.

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 4 institutions in 1 country.

Yaoqing ChenDepartment of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota, USA.
Kanagalaghatta R Rajashankar
Yang Yang
Sudhakar S Agnihothram
Chang Liu
Yi-Lun Lin
Ralph S Baric
Fang Li
University of Minnesota Medical Center · USUniversity of North Carolina at Chapel Hill · USCornell University · USUniversity of Minnesota · US

Funding

Unlocking Zika Virus Immune Control and Pathogenesis with the Collaborative CrossU19AI100625 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI HEISE, MARK T · 2012 to 2021
$36.6M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Broad Spectrum Neutralizing Human Abs to SARS and Related CoronavirusesR01AI085524 · NIAID · DANA-FARBER CANCER INST · PI MARASCO, WAYNE A. · 2010 to 2014
$5.4M
Receptor recognition mechanisms of coronavirusesR01AI089728 · NIAID · UNIVERSITY OF MINNESOTA · PI Fang Li, Timothy Patrick Sheahan · 2010 to 2026
$4.7M
NIAID NIH HHS 1U19AI100625NIAID NIH HHS R01 AI085524NIAID NIH HHS R01AI085524NIAID NIH HHS R01 AI089728NIAID NIH HHS R01AI089728NIAID NIH HHS U19 AI100625NIGMS NIH HHS 8P41GM103403-10NIGMS NIH HHS P41 GM103403
6 · The paper itself

Abstract

The newly emerged Middle East respiratory syndrome coronavirus (MERS-CoV) has infected at least 77 people, with a fatality rate of more than 50%. Alarmingly, the virus demonstrates the capability of human-to-human transmission, raising the possibility of global spread and endangering world health and economy. Here we have identified the receptor-binding domain (RBD) from the MERS-CoV spike protein and determined its crystal structure. This study also presents a structural comparison of MERS-CoV RBD with other coronavirus RBDs, successfully positioning MERS-CoV on the landscape of coronavirus evolution and providing insights into receptor binding by MERS-CoV. Furthermore, we found that MERS-CoV RBD functions as an effective entry inhibitor of MERS-CoV. The identified MERS-CoV RBD may also serve as a potential candidate for MERS-CoV subunit vaccines. Overall, this study enhances our understanding of the evolution of coronavirus RBDs, provides insights into receptor recognition by MERS-CoV, and may help control the transmission of MERS-CoV in humans.

Indexed as

Amino Acid SequenceCoronavirusCrystallography, X-RayDipeptidyl Peptidase 4Host-Pathogen InteractionsHumansLeukemia Virus, MurineMiddle EastMolecular Sequence DataProtein ConformationSequence Homology, Amino AcidSyndromeViral ProteinsDipeptidyl Peptidase 4DPP4 protein, humanViral Proteins

Identifiers

PMID23903833
PMCPMC3807420
OpenAlexW2132056320

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.