Evidence map›Paper›PMID 38285951›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2024

Helical sulfonyl-γ-AApeptides modulating Aβ oligomerization and cytotoxicity by recognizing Aβ helix.

Heng Liu, Yunpeng Cui, Xue Zhao, Lulu Wei, Xudong Wang, Ning Shen, Timothy Odom, Xuming Li, William Lawless, Kanchana Karunarathne and 5 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
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

15 authors at 1 institution in 1 country.

Heng LiuDepartment of Chemistry, University of South Florida, Tampa, FL 33620.ORCID 0000-0002-0456-4626
Yunpeng CuiDepartment of Chemistry, University of South Florida, Tampa, FL 33620.ORCID 0009-0006-4865-0493
Xue ZhaoDepartment of Chemistry, University of South Florida, Tampa, FL 33620.ORCID 0009-0000-4872-1577
Lulu WeiDepartment of Chemistry, University of South Florida, Tampa, FL 33620.ORCID 0000-0003-4657-9479
Xudong WangDepartment of Molecular Biosciences, University of South Florida, Tampa, FL 33620.
Ning ShenDepartment of Chemistry, University of South Florida, Tampa, FL 33620.
Timothy OdomDepartment of Chemistry, University of South Florida, Tampa, FL 33620.
Xuming LiDepartment of Chemistry, University of South Florida, Tampa, FL 33620.
William LawlessDepartment of Chemistry, University of South Florida, Tampa, FL 33620.
Kanchana KarunarathneDepartment of Physics, University of South Florida, Tampa, FL 33620.ORCID 0009-0008-8271-255X
Martin MuscholDepartment of Physics, University of South Florida, Tampa, FL 33620.
Wayne GuidaDepartment of Chemistry, University of South Florida, Tampa, FL 33620.ORCID 0000-0003-3353-4853
Chuanhai CaoTaneja College of Pharmacy, University of South Florida, Tampa, FL 33612.
Libin YeDepartment of Molecular Biosciences, University of South Florida, Tampa, FL 33620.ORCID 0000-0003-0818-2972
Jianfeng CaiDepartment of Chemistry, University of South Florida, Tampa, FL 33620.ORCID 0000-0003-3106-3306
University of South Florida · US

Funding

Recognition of Abeta monomeric helixR01AG056569 · NIA · UNIVERSITY OF SOUTH FLORIDA · PI CHUANHAI CAO, Jianfeng Cai · 2017 to 2026
$4.1M
Targeting Wnt signaling pathwayR01GM150196 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI Jianfeng Cai · 2023 to 2026
$1.7M
The Role of Intermediate Conformations in G Protein-coupled Receptor SignalingR01GM149659 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI Libin Ye · 2023 to 2026
$1.4M
NIA NIH HHS R01 AG056569NIGMS NIH HHS R01 GM149659NIGMS NIH HHS R01 GM150196
6 · The paper itself

Abstract

In contrast to prevalent strategies which make use of β-sheet mimetics to block Aβ fibrillar growth, in this study, we designed a series of sulfonyl-γ-AApeptide helices that targeted the crucial α-helix domain of Aβ13-26 and stabilized Aβ conformation to avoid forming the neurotoxic Aβ oligomeric β-sheets. Biophysical assays such as amyloid kinetics and TEM demonstrated that the Aβ oligomerization and fibrillation could be greatly prevented and even reversed in the presence of sulfonyl-γ-AApeptides in a sequence-specific and dose-dependent manner. The studies based on circular dichroism, Two-dimensional nuclear magnetic resonance spectroscopy (2D-NMR) spectra unambiguously suggested that the sulfonyl-γ-AApeptide Ab-6 could bind to the central region of Aβ

Indexed as

AmidesAmyloidAmyloid beta-PeptidesMolecular ConformationPeptide FragmentsProtein Conformation, alpha-HelicalAmidesAmyloidAmyloid beta-Peptidesgamma-AApeptidePeptide FragmentsAlzheimer’s diseaseAβ aggregationfoldamerhelix stabilizationsulfonyl-γ-AApeptides

Identifiers

PMID38285951
PMCPMC10861862
OpenAlexW4391304218

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.