ReviewTopics in current chemistry2011
Prion seeded conversion and amplification assays.
Review in Topics in current chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 23 citations in OpenAlex.
- Small protease sensitive oligomers of PrPSc in distinct human prions determine conversion rate of PrP(C).PLoS pathogens · 2012Trial
- Improving protocols for α-synuclein seed amplification assays: analysis of preanalytical and analytical variables and identification of candidate parameters for seed quantification.Clinical chemistry and laboratory medicine · 2024Article
- Role of prion protein glycosylation in replication of human prions by protein misfolding cyclic amplification.Laboratory investigation; a journal of technical methods and pathology · 2019Article
- Early and Pre-Clinical Detection of Prion Seeding Activity in Cerebrospinal Fluid of Goats using Real-Time Quaking-Induced Conversion Assay.Scientific reports · 2019Article
- Detection of Prions in Blood of Cervids at the Asymptomatic Stage of Chronic Wasting Disease.Scientific reports · 2017Article
- A Heparin Purification Process Removes Spiked Transmissible Spongiform Encephalopathy Agent.The AAPS journal · 2017Article
- Insights from Therapeutic Studies for PrP Prion Disease.Cold Spring Harbor perspectives in medicine · 2017Review
- Assessment of the PrPc Amino-Terminal Domain in Prion Species Barriers.Journal of virology · 2016Article
- Bank Vole Prion Protein As an Apparently Universal Substrate for RT-QuIC-Based Detection and Discrimination of Prion Strains.PLoS pathogens · 2015Article
- Article
- Molecular barriers to zoonotic transmission of prions.Emerging infectious diseases · 2014Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The conversion of the normal prion protein (PrP(C)) into its misfolded, aggregation-prone and infectious (prion) isoform is central to the progression of transmissible spongiform encephalopathies (TSEs) or prion diseases. Since the initial development of a cell free PrP conversion reaction, striking progress has been made in the development of much more continuous prion-induced conversion and amplification reactions. These studies have provided major insights into the molecular underpinnings of prion propagation and enabled the development of ultra-sensitive tests for prions and prion disease diagnosis. This chapter will provide an overview of such reactions and the practical and fundamental consequences of their development.
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.