ArticleAnalytical biochemistry2018
Disulfide bond mapping of Pfs25, a recombinant malaria transmission blocking vaccine candidate.
Article in Analytical biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Global diversity of the gene encoding the Pfs25 protein-a Plasmodium falciparum transmission-blocking vaccine candidate.Parasites & vectors · 2021Article
- Particle-based, Pfs230 and Pfs25 immunization is effective, but not improved by duplexing at fixed total antigen dose.Malaria journal · 2020Article
- A C-terminal Pfs48/45 malaria transmission-blocking vaccine candidate produced in the baculovirus expression system.Scientific reports · 2020Article
- Fusion to Tetrahymena thermophila granule lattice protein 1 confers solubility to sexual stage malaria antigens in Escherichia coli.Protein expression and purification · 2019Article
- A malaria vaccine adjuvant based on recombinant antigen binding to liposomes.Nature nanotechnology · 2018Article
- Peptide data on the disulfide bond analysis of baculovirus produced Pfs25 by LC-MSMS.Data in brief · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A liquid chromatography tandem-mass spectrometry method was developed to map the eleven disulfide bonds in Pfs25, a malaria transmission-blocking vaccine candidate. The compact and complex nature of Pfs25 has led to difficulties in prior peptide mapping efforts. Here, we report confirmation of proper disulfide pairing of a recombinant Pfs25, by optimizing denaturation and digestion with trypsin/Lys-C. The digested peptides were separated by reversed phase HPLC to obtain the peptide map and elucidate the disulfide linkages. MS
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Registered trials
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