Evidence map›Paper›PMID 37610572›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Recombinant Soluble Henipavirus Glycoprotein Preparation.

Lianying Yan, Spencer L Sterling, Deborah L Fusco, Yee-Peng Chan, Kai Xu, Eric D Laing, Christopher C Broder

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
19.4field-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

12 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
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  9. Structure and design of Langya virus glycoprotein antigens.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Article
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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 2 institutions in 1 country.

Lianying YanDepartment of Microbiology and Immunology, Uniformed Services University, Bethesda, MD, USA.
Spencer L SterlingDepartment of Microbiology and Immunology, Uniformed Services University, Bethesda, MD, USA.
Deborah L FuscoDepartment of Microbiology and Immunology, Uniformed Services University, Bethesda, MD, USA.
Yee-Peng ChanDepartment of Microbiology and Immunology, Uniformed Services University, Bethesda, MD, USA.
Kai XuDepartment of Veterinary Biosciences, College of Veterinary Medicine, The Ohio State University, Columbus, OH, USA.
Eric D LaingDepartment of Microbiology and Immunology, Uniformed Services University, Bethesda, MD, USA.
Christopher C BroderDepartment of Microbiology and Immunology, Uniformed Services University, Bethesda, MD, USA. christopher.broder@usuhs.edu.
Uniformed Services University of the Health Sciences · USThe Ohio State University · US

Funding

Project 3 - USUHSU19AI142764 · NIAID · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI BRODER, CHRISTOPHER C · 2019 to 2023
$24.6M
Vaccines and Therapeutics for Nipah and Hendra virusU01AI077995 · NIAID · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI BRODER, CHRISTOPHER C · 2008 to 2012
$5.5M
Nipah Virus and Hendra Virus Entry and Virion AssemblyR01AI054715 · NIAID · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI BRODER, CHRISTOPHER C · 2006 to 2016
$3.1M
Structure, function, and antigenicity of emerging henipavirus surface glycoproteinsU01AI173348 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI Kai Xu · 2023 to 2026
$2.4M
NIAID NIH HHS R01 AI054715NIAID NIH HHS U01 AI077995NIAID NIH HHS U01 AI173348NIAID NIH HHS U19 AI142764
6 · The paper itself

Abstract

Henipaviruses possess two envelope glycoproteins, the attachment (G) and the fusion (F) proteins that mediate cellular entry and are the major targets of virus-neutralizing antibody responses. Recombinant expression technologies have been used to produce soluble G and F proteins (sG and sF) that retain native-like oligomeric conformations and epitopes, which are advantageous for the development and characterization of vaccines and antiviral antibody therapeutics. In addition to Hendra virus and Nipah virus tetrameric sG and trimeric sF production, we also describe the expression and purification of Cedar virus tetrameric sG and Ghana virus trimeric sF glycoproteins. These henipavirus glycoproteins were also used as immunizing antigens to generate monoclonal antibodies, and binding was demonstrated with a pan-henipavirus multiplex microsphere immunoassay.

Indexed as

HenipavirusAntibodies, BlockingAntibodies, MonoclonalAntibodies, BlockingAntibodies, MonoclonalCedar virusCross-linkingExpressionF glycoproteinG glycoproteinGhana virusHendra virusHenipavirusesMòjiāng virusMultiplex microsphere immunoassayNipah virusPurification

Identifiers

PMID37610572
OpenAlexW4386084396

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.