Evidence map›Paper›PMID 23089868›Full record

ArticleNature chemistry2012

Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity.

Pin-Nan Cheng, Cong Liu, Minglei Zhao, David Eisenberg, James S Nowick

Open access · greenAbstract read
In one paragraph

Article in Nature chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed, 1 pooled it
9.9field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

103 citing papers in PubMed, 1 synthesis or guideline pooled it, 239 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Backbone double-mutant cycle analysis quantifies hydrogen-bond energies in proteins.Protein science : a publication of the Protein Society · 2026
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  20. Chemical science · 2024
    Article

43 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Pin-Nan ChengDepartment of Chemistry, University of California, Irvine, California 92697-2025, USA.
Cong Liu
Minglei Zhao
David Eisenberg
James S Nowick
University of California, Irvine · USUniversity of California, Los Angeles · USHoward Hughes Medical Institute · US

Funding

Structural Biology of Amyloid DiseaseR01AG029430 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI EISENBERG, DAVID · 2007 to 2016
$3.9M
Purchase of an Microwave Peptide SynthesizerR01GM097562 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI NOWICK, JAMES S · 2012 to 2019
$2.5M
CHEMICAL MODELS OF PROTEIN BETA SHEET INTERACTIONSR01GM049076 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI NOWICK, JAMES S · 1999 to 2009
$1.7M
Howard Hughes Medical InstituteNIA NIH HHS 1R01 AG029430NIA NIH HHS R01 AG029430NIGMS NIH HHS 1R01 GM097562NIGMS NIH HHS 5R01 GM049076NIGMS NIH HHS R01 GM049076NIGMS NIH HHS R01 GM097562
6 · The paper itself

Abstract

The amyloid protein aggregation associated with diseases such as Alzheimer's, Parkinson's and type II diabetes (among many others) features a bewildering variety of β-sheet-rich structures in transition from native proteins to ordered oligomers and fibres. The variation in the amino-acid sequences of the β-structures presents a challenge to developing a model system of β-sheets for the study of various amyloid aggregates. Here, we introduce a family of robust β-sheet macrocycles that can serve as a platform to display a variety of heptapeptide sequences from different amyloid proteins. We have tailored these amyloid β-sheet mimics (ABSMs) to antagonize the aggregation of various amyloid proteins, thereby reducing the toxicity of amyloid aggregates. We describe the structures and inhibitory properties of ABSMs containing amyloidogenic peptides from the amyloid-β peptide associated with Alzheimer's disease, β(2)-microglobulin associated with dialysis-related amyloidosis, α-synuclein associated with Parkinson's disease, islet amyloid polypeptide associated with type II diabetes, human and yeast prion proteins, and Tau, which forms neurofibrillary tangles.

Indexed as

Amyloid beta-PeptidesAnimalsCell SurvivalDrug DesignHumansMacrocyclic CompoundsModels, MolecularPC12 CellsPeptidomimeticsProtein MultimerizationProtein Structure, SecondaryRatsAmyloid beta-PeptidesMacrocyclic CompoundsPeptidomimetics

Identifiers

PMID23089868
PMCPMC3481199
OpenAlexW2118331478

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.