Evidence map›Paper›PMID 25482604›Full record

ArticlePrion2014

Sensitive detection of aggregated prion protein via proximity ligation.

Maria Hammond, Lotta Wik, Jean-Philippe Deslys, Emmanuel Comoy, Tommy Linné, Ulf Landegren, Masood Kamali-Moghaddam

Abstract read
In one paragraph

Article in Prion, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Homogeneous and digital proximity ligation assays for the detection ofBiomolecular detection and quantification · 2016
    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

7 authors.

Maria Hammonda Department of Immunology, Genetics and Pathology; Science for Life Laboratory ; Uppsala University ; Uppsala , Sweden.
Lotta Wik
Jean-Philippe Deslys
Emmanuel Comoy
Tommy Linné
Ulf Landegren
Masood Kamali-Moghaddam

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The DNA assisted solid-phase proximity ligation assay (SP-PLA) provides a unique opportunity to specifically detect prion protein (PrP) aggregates by investigating the collocation of 3 or more copies of the specific protein. We have developed an SP-PLA that can detect PrP aggregates in brain homogenates from infected hamsters even after a 10(7)-fold dilution. In contrast, brain homogenate from uninfected animals did not generate a detectable signal at 100-fold higher concentration. Using either of the 2 monoclonal anti-PrP antibodies, 3F4 and 6H4, we successfully detected low concentrations of aggregated PrP. The presented results provide a proof of concept that this method might be an interesting tool in the development of diagnostic approaches of prion diseases.

Indexed as

AmyloidAnimalsAntibodies, ImmobilizedBrain ChemistryCricetinaeImmunoassayPrionsSensitivity and SpecificityAmyloidAntibodies, ImmobilizedPrions263KBSE, bovine spongiform encephalopathyCJD, Creutzfeldt-Jakob diseaseCSF, cerebrospinal fluiddiagnosisFIDA, fluorescence intensity distribution analysismonoclonal antibodyPLA, proximity ligation assayPMCA, protein misfolding cyclic amplificationprion proteinproximity ligation assayPrPC, cellular prion proteinPrP, prion proteinPrPSc, scrapie prion proteinqPCR, quantitative real-time PCRQuIC, quaking-induced conversionSP-PLA, solid phase proximity ligation assay

Identifiers

PMID25482604
PMCPMC4601298

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.