ArticleJournal of the American Chemical Society2015
X-ray Crystallographic Structures of Oligomers of Peptides Derived from β2-Microglobulin.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 33 citations in OpenAlex.
- α-Alkylated α-amino acids reduce the aggregation of unfolded peptides.RSC advances · 2026Article
- An Improved Turn Structure for Inducing β-Hairpin Formation in Peptides.Angewandte Chemie (International ed. in English) · 2021Article
- Exploring amyloid oligomers with peptide model systems.Current opinion in chemical biology · 2021Review
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
- Synthesis and study of macrocyclic β-hairpin peptides for investigating amyloid oligomers.Methods in enzymology · 2021Article
- An explicitly designed paratope of amyloid-β prevents neuronal apoptosisChemical science · 2020Article
- The Early Phase of β2-Microglobulin Aggregation: Perspectives From Molecular Simulations.Frontiers in molecular biosciences · 2020Review
- X-ray Crystallographic Structure of a Teixobactin Derivative Reveals Amyloid-like Assembly.Journal of the American Chemical Society · 2018Article
- Controlling the Oligomerization State of Aβ-Derived Peptides with Light.Journal of the American Chemical Society · 2018Article
- Elucidating the Structures of Amyloid Oligomers with Macrocyclic β-Hairpin Peptides: Insights into Alzheimer's Disease and Other Amyloid Diseases.Accounts of chemical research · 2018Review
- The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides.Interface focus · 2017Review
- A Hexamer of a Peptide Derived from AβBiochemistry · 2017Article
- A Tetramer Derived from Islet Amyloid Polypeptide.The Journal of organic chemistry · 2017Article
- Small molecule probes of protein aggregation.Current opinion in chemical biology · 2017Review
- X-ray Crystallographic Structure of a Compact Dodecamer from a Peptide Derived from AβOrganic letters · 2017Article
- Stabilization, Assembly, and Toxicity of Trimers Derived from Aβ.Journal of the American Chemical Society · 2017Article
- Square channels formed by a peptide derived from transthyretin.Chemical science · 2016Article
- The omic approach to parasitic trematode research-a review of techniques and developments within the past 5 years.Parasitology research · 2016Review
- X-ray Crystallographic Structure of Oligomers Formed by a Toxic β-Hairpin Derived from α-Synuclein: Trimers and Higher-Order Oligomers.Journal of the American Chemical Society · 2016Article
- X-ray Crystallographic Structures of a Trimer, Dodecamer, and Annular Pore Formed by an Aβ17-36 β-Hairpin.Journal of the American Chemical Society · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Amyloid diseases such as Alzheimer's disease, Parkinson's disease, and type II diabetes share common features of toxic soluble protein oligomers. There are no structures at atomic resolution of oligomers formed by full-length amyloidogenic peptides and proteins, and only a few structures of oligomers formed by peptide fragments. The paucity of structural information provides a fundamental roadblock to understanding the pathology of amyloid diseases and developing preventions or therapies. Here, we present the X-ray crystallographic structures of three families of oligomers formed by macrocyclic peptides containing a heptapeptide sequence derived from the amyloidogenic E chain of β2-microglobulin (β2m). Each macrocyclic peptide contains the heptapeptide sequence β2m63-69 and a second heptapeptide sequence containing an N-methyl amino acid. These peptides form β-sheets that further associate into hexamers, octamers, and dodecamers: the hexamers are trimers of dimers; the octamers are tetramers of dimers; and the dodecamers contain two trimer subunits surrounded by three pairs of β-sheets. These structures illustrate a common theme in which dimer and trimer subunits further associate to form a hydrophobic core. The seven X-ray crystallographic structures not only illustrate a range of oligomers that a single amyloidogenic peptide sequence can form, but also how mutation can alter the size and topology of the oligomers. A cocrystallization experiment in which a dodecamer-forming peptide recruits a hexamer-forming peptide to form mixed dodecamers demonstrates that one species can dictate the oligomerization of another. These findings should also be relevant to the formation of oligomers of full-length peptides and proteins in amyloid diseases.
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.