ArticleThe Journal of biological chemistry2007
Production and characterization of RNA aptamers specific for amyloid fibril epitopes.
Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 40 citations in OpenAlex.
- Aptamers targeting amyloidogenic proteins and their emerging role in neurodegenerative diseases.The Journal of biological chemistry · 2022Review
- Detection of Amyloid β Oligomers with RNA Aptamers in AppACS omega · 2020Article
- Glycated albumin precipitation using aptamer conjugated magnetic nanoparticles.Scientific reports · 2020Article
- Riboswitch identification using Ligase-Assisted Selection for the Enrichment of Responsive Ribozymes (LigASERR).Synthetic biology (Oxford, England) · 2019Article
- Aptamers Selected for Recognizing Amyloid β-Protein-A Case for Cautious Optimism.International journal of molecular sciences · 2018Review
- Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation.Biophysical reviews · 2017Review
- Unraveling Prion Protein Interactions with Aptamers and Other PrP-Binding Nucleic Acids.International journal of molecular sciences · 2017Review
- Nucleic Acid-Based Theranostics for Tackling Alzheimer's Disease.Theranostics · 2017Review
- Distinguishing closely related amyloid precursors using an RNA aptamer.The Journal of biological chemistry · 2014Article
- Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly.Molecular cell · 2014Article
- Aptamers as both drugs and drug-carriers.BioMed research international · 2014Review
- Toggled RNA aptamers against aminoglycosides allowing facile detection of antibiotics using gold nanoparticle assays.Analytical chemistry · 2012Article
- Generation of neutralizing aptamers against herpes simplex virus type 2: potential components of multivalent microbicides.The Journal of general virology · 2011Article
- The emerging field of RNA nanotechnology.Nature nanotechnology · 2010Review
- Selection of aptamers for amyloid beta-protein, the causative agent of Alzheimer's disease.Journal of visualized experiments : JoVE · 2010Article
- RNA aptamers generated against oligomeric Abeta40 recognize common amyloid aptatopes with low specificity but high sensitivity.PloS one · 2009Article
- Characterization of RNA aptamers that disrupt the RUNX1-CBFbeta/DNA complex.Nucleic acids research · 2009Article
- Therapeutic applications of DNA and RNA aptamers.Oligonucleotides · 2009Review
- 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
6 authors at 3 institutions in 1 country.
Funding
Abstract
One of the most fascinating features of amyloid fibrils is their generic cross-beta architecture that can be formed from many different and completely unrelated proteins. Nonetheless, amyloid fibrils with diverse structural and phenotypic properties can form, both in vivo and in vitro, from the same protein sequence. Here, we have exploited the power of RNA selection techniques to isolate small, structured, single-stranded RNA molecules known as aptamers that were targeted specifically to amyloid-like fibrils formed in vitro from beta(2)-microglobulin (beta(2)m), the amyloid fibril protein associated with dialysis-related amyloidosis. The aptamers bind with high affinity (apparent K(D) approximately nm) to beta(2)m fibrils with diverse morphologies generated under different conditions in vitro, as well as to amyloid fibrils isolated from tissues of dialysis-related amyloidosis patients, demonstrating that they can detect conserved epitopes between different fibrillar species of beta(2)m. Interestingly, the aptamers also recognize some other, but not all, amyloid fibrils generated in vitro or isolated from ex vivo sources. Based on these observations, we have shown that although amyloid fibrils share many common structural properties, they also have features that are unique to individual fibril types.
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.