ArticleBiophysical journal2009
Two distinct conformations of Abeta aggregates on the surface of living PC12 cells.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed.
- Glucose directs amyloid-beta into membrane-active oligomers.Physical chemistry chemical physics : PCCP · 2017Article
- Beyond attachment: Roles of DC-SIGN in dengue virus infection.Traffic (Copenhagen, Denmark) · 2017Article
- Effects of Low Amyloid-β (Aβ) Concentration on Aβ1-42 Oligomers Binding and GluN2B Membrane Expression.Journal of Alzheimer's disease : JAD · 2015Article
- Article
- Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs).Chemical reviews · 2014Review
- Aggregation distributions on cells determined by photobleaching image correlation spectroscopy.Biophysical journal · 2013Article
- Thermodynamically stable amyloid-β monomers have much lower membrane affinity than the small oligomers.Frontiers in physiology · 2013Article
- Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease.Cold Spring Harbor perspectives in medicine · 2012Review
- Article
- Cell surface binding and internalization of aβ modulated by degree of aggregation.International journal of Alzheimer's disease · 2011Article
- Formation of Toxic Amyloid Fibrils by Amyloid β-Protein on Ganglioside Clusters.International journal of Alzheimer's disease · 2011Article
- Direct observation of single amyloid-β(1-40) oligomers on live cells: binding and growth at physiological concentrations.PloS one · 2011Article
- Measurement of the attachment and assembly of small amyloid-β oligomers on live cell membranes at physiological concentrations using single-molecule tools.Biophysical journal · 2010Article
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Abeta42 has been found to associate rapidly to neuronal cells and is the primary constituent of senile plaques. In this study we monitored the aggregation of Abeta42 with living PC12 cells. Using photobleaching Förster resonance energy transfer, we observed one set of aggregates that displayed colocalization and another that displayed energy transfer. Cell surface aggregates were found to become resistant to potassium iodide (KI)-induced quenching. Exposed Abeta42 regions were probed with three monoclonal antibodies directed against the N-terminus, an internal sequence, and the C-terminus of Abeta42. Two populations of aggregates were revealed: one that bound all three antibodies, and one that bound all but the C-terminus antibody. Of interest, using fluorescent recovery after photobleaching, we observed no Abeta42 exchange within either type of aggregate. These findings offer what we believe is new insight into the conformations of Abeta42 that accumulate on the surface of living cells. One conformation is incapable of energy transfer, is sensitive to KI, and binds C-terminus-specific antibodies. The other conformation increases in number over time, is capable of energy transfer, is quencher-resistant, and has a sequestered C-terminus. With further studies to characterize Abeta aggregation on live cells, the underlying mechanisms leading to Alzheimer's disease may be revealed.
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.