Evidence map›Paper›PMID 19252850›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2009

Preparation of recombinant viral glycoproteins for novel and therapeutic antibody discovery.

Yee-Peng Chan, Lianying Yan, Yan-Ru Feng, Christopher C Broder

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Structure and design of Langya virus glycoprotein antigens.bioRxiv : the preprint server for biology · 2023
    Article
  6. Article
  7. Recombinant Soluble Henipavirus Glycoprotein Preparation.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  8. Therapeutic Antibodies: An Overview.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

4 authors.

Yee-Peng ChanUniformed Services, University of the Health Sciences, Bethesda, MD, USA.
Lianying Yan
Yan-Ru Feng
Christopher C Broder

Funding

Vaccine strategy for broad spectrum protection agains non-typhoidal salmonellU54AI057168 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI LEVINE, MYRON MAX · 2003 to 2013
$91.5M
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
NIAID NIH HHS AI054715NIAID NIH HHS AI057168NIAID NIH HHS R01 AI054715NIAID NIH HHS U54 AI057168
6 · The paper itself

Abstract

Neutralizing antibodies are a critical component in the protection or recovery from viral infections. In the absence of available vaccines or antiviral drugs for many important human viral pathogens, the identification and characterization of new human monoclonal antibodies (hmAbs) that are able to neutralize viruses offers the possibility for effective pre- and/or post-exposure therapeutic modalities. Such hmAbs may also help in our understanding of the virus entry process, the mechanisms of virus neutralization, and in the eventual development of specific entry inhibitors, vaccines, and research tools. The majority of the more recently developed antiviral hmAbs have come from the use of antibody phage-display technologies using both naïve and immune libraries. Many of these agents are also enveloped viruses possessing important neutralizing determinants within their membrane-anchored envelope glycoproteins, and the use of recombinant, soluble versions of these viral glycoproteins is often critical in the isolation and development of antiviral hmAbs. This chapter will detail several methods that have been successfully employed to produce, purify, and characterize soluble and secreted versions of several viral envelope glycoproteins which have been successfully used as antigens to capture and isolate human phage-displayed monoclonal antibodies.

Indexed as

AnimalsAntibodiesCell LineChromatography, GelElectrophoresis, Polyacrylamide GelGlycoproteinsHumansMolecular BiologyMolecular WeightRecombinant ProteinsSolubilityUltracentrifugationVaccinia virusViral ProteinsAntibodiesGlycoproteinsRecombinant ProteinsViral Proteins

Identifiers

PMID19252850
PMCPMC3277858

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.