ArticleBiophysical journal2009
Structural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/deuterium exchange.
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 26 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
26 citing papers in PubMed, 61 citations in OpenAlex.
- Multifaceted Effects of a Multiple Nitric Oxide Photoreleaser and its Photoproducts on Amyloid-β Aggregation.Chembiochem : a European journal of chemical biology · 2026Article
- Inducers and modulators of protein aggregation in Alzheimer's disease - Critical tools for understanding the foundations of aggregate structures.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025Review
- Chiral Interface of Amyloid Beta (Aβ): Relevance to Protein Aging, Aggregation and Neurodegeneration.Symmetry · 2020Article
- Ubiquitin binds the amyloid β peptide and interferes with its clearance pathways.Chemical science · 2019Article
- Newfound effect of N-acetylaspartate in preventing and reversing aggregation of amyloid-beta in vitro.Neurobiology of disease · 2018Article
- Side-chain moieties from the N-terminal region of Aβ are Involved in an oligomer-stabilizing network of interactions.PloS one · 2018Article
- What amyloid ligands can tell us about molecular polymorphism and disease.Neurobiology of aging · 2016Review
- Nanoscale Structure and Spectroscopic Probing of Aβ1-40 Fibril Bundle Formation.Frontiers in chemistry · 2016Article
- Two distinct β-sheet structures in Italian-mutant amyloid-beta fibrils: a potential link to different clinical phenotypes.Cellular and molecular life sciences : CMLS · 2015Article
- A synchrotron-based hydroxyl radical footprinting analysis of amyloid fibrils and prefibrillar intermediates with residue-specific resolution.Biochemistry · 2014Article
- 2D IR cross peaks reveal hydrogen-deuterium exchange with single residue specificity.The journal of physical chemistry. B · 2013Article
- Aβ monomers transiently sample oligomer and fibril-like configurations: ensemble characterization using a combined MD/NMR approach.Journal of molecular biology · 2013Article
- Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease.Cold Spring Harbor perspectives in medicine · 2012Review
- Structure-based design of conformation- and sequence-specific antibodies against amyloid β.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- A safe, blood-brain barrier permeable triphenylmethane dye inhibits amyloid-β neurotoxicity by generating nontoxic aggregates.ACS chemical neuroscience · 2011Article
- Insight into amyloid structure using chemical probes.Chemical biology & drug design · 2011Review
- A new approach to explore the impact of freeze-thaw cycling on protein structure: hydrogen/deuterium exchange mass spectrometry (HX-MS).Pharmaceutical research · 2011Article
- Aromatic small molecules remodel toxic soluble oligomers of amyloid beta through three independent pathways.The Journal of biological chemistry · 2011Article
- Polymorphic structures of Alzheimer's β-amyloid globulomers.PloS one · 2011Article
- Structurally distinct toxicity inhibitors bind at common loci on β-amyloid fibril.Protein science : a publication of the Protein Society · 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
4 authors at 2 institutions in 1 country.
Funding
Abstract
The aggregation of amyloid-beta protein (Abeta) in vivo is a critical pathological event in Alzheimer's disease. Although more and more evidence shows that the intermediate oligomers are the primary neurotoxic species in Alzheimer's disease, the particular structural features responsible for the toxicity of these intermediates are poorly understood. We measured the peptide level solvent accessibility of multiple Abeta(1-40) aggregated states using hydrogen exchange detected by mass spectrometry. A gradual reduction in solvent accessibility, spreading from the C-terminal region to the N-terminal region was observed with ever more aggregated states of Abeta peptide. The observed hydrogen exchange protection begins with reporter peptides 20-34 and 35-40 in low molecular weight oligomers found in fresh samples and culminates with increasing solvent protection of reporter peptide 1-16 in long time aged fibrillar species. The more solvent exposed structure of intermediate oligomers in the N-termini relative to well-developed fibrils provides a novel explanation for the structure-dependent neurotoxicity of soluble oligomers reported previously.
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.