ArticlePrion
Using small molecule reagents to selectively modify epitopes based on their conformation.
Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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.
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.
Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Detecting Differences in Prion Protein Conformation by Quantifying Methionine Oxidation.ACS omega · 2022Article
- Structure of prion β-oligomers as determined by short-distance crosslinking constraint-guided discrete molecular dynamics simulations.Proteomics · 2021Article
- Quantifying the Role of Lysine in Prion Replication by Nano-LC Mass Spectrometry and Bioassay.Frontiers in bioengineering and biotechnology · 2020Article
- N(ε)-Carboxymethyl Modification of Lysine Residues in Pathogenic Prion Isoforms.Molecular neurobiology · 2016Article
- Conformation-dependent epitopes recognized by prion protein antibodies probed using mutational scanning and deep sequencing.Journal of molecular biology · 2015Article
- Prion protein-specific antibodies that detect multiple TSE agents with high sensitivity.PloS one · 2014Article
- Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PrP(Sc) is an infectious protein. The only experimentally verified difference between PrP(Sc) and its normal cellular isoform (PrP(C)) is conformational. This work describes an approach to determining the presence of surface exposed or sequestered amino acids present in the PrP(Sc) isoform. The N-hydroxysuccinimide esters of acetic acid and 4-trimethylammoniumbutyric acid were synthesized and reacted with detergent-solubilized brain extracts from Me7-infected mice, uninfected mice, 263K-infected hamsters or uninfected hamsters. These reaction mixtures were analyzed by western blots probed with the antibodies 3F4, 6D11, 7D9, AG4, AH6, GE8 or MAB5424. The 3F4, 6D11, AH6, and GE8 antibodies recognize an epitope that is encrypted in the PrP(Sc) isoform, but exposed in the PrP(C) isoform. These reagents permit the detection of prion infected brain extracts without the need for proteinase K digestion. In addition they can be used, with an appropriate antibody, to determine which amino acids of PrP(Sc) are exposed on the surface and which are encrypted, thus providing useful structural information. This approach was used to distinguish between the 263K and drowsy strains of hamster-adapted scrapie without the use of proteinase K.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.