Evidence map›Paper›PMID 31695027›Full record

ArticleNature communications2019

Molecular basis for chirality-regulated Aβ self-assembly and receptor recognition revealed by ion mobility-mass spectrometry.

Gongyu Li, Kellen DeLaney, Lingjun Li

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

20 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Single ion mobility monitoring (SIMAnalytical and bioanalytical chemistry · 2024
    Article
  7. Article
  8. Article
  9. Review
  10. Article
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  14. Review
  15. Article
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  18. Advancing d-amino acid-containing peptide discovery in the metazoan.Biochimica et biophysica acta. Proteins and proteomics · 2021
    Review
  19. Article
  20. Article
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

3 authors at 1 institution in 1 country.

Gongyu LiSchool of Pharmacy, University of Wisconsin-Madison, Madison, WI, 53705, USA.ORCID http://orcid.org/0000-0002-2367-4433
Kellen DeLaneyDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Lingjun LiSchool of Pharmacy, University of Wisconsin-Madison, Madison, WI, 53705, USA. lingjun.li@wisc.edu.ORCID http://orcid.org/0000-0003-0056-3869
University of Wisconsin–Madison · US

Funding

Mass Spectrometric Studies of Neuropeptides in FeedingR01DK071801 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI LINGJUN LI · 2006 to 2026
$6.7M
Di-Leu-enabled multiplexed quantitation for biomarker discovery and validation in Alzheimer's diseaseRF1AG052324 · NIA · UNIVERSITY OF WISCONSIN-MADISON · PI LI, LINGJUN · 2018 to 2018
$2.4M
Mass Spectrometric Studies of Neuropeptides in FeedingR56DK071801 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI LI, LINGJUN · 2011 to 2011
$216k
Mass spectrometry profiling of secreted neuropeptides in the stomatogastric nervous system in response to feedingF31GM126870 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DELANEY, KELLEN L. · 2018 to 2019
$66k
NIA NIH HHS RF1 AG052324NIDDK NIH HHS R01 DK071801NIDDK NIH HHS R56 DK071801NIGMS NIH HHS F31 GM126870
6 · The paper itself

Abstract

Despite extensive efforts on probing the mechanism of Alzheimer's disease (AD) and enormous investments into AD drug development, the lack of effective disease-modifying therapeutics and the complexity of the AD pathogenesis process suggest a great need for further insights into alternative AD drug targets. Herein, we focus on the chiral effects of truncated amyloid beta (Aβ) and offer further structural and molecular evidence for epitope region-specific, chirality-regulated Aβ fragment self-assembly and its potential impact on receptor-recognition. A multidimensional ion mobility-mass spectrometry (IM-MS) analytical platform and in-solution kinetics analysis reveal the comprehensive structural and molecular basis for differential Aβ fragment chiral chemistry, including the differential and cooperative roles of chiral Aβ N-terminal and C-terminal fragments in receptor recognition. Our method is applicable to many other systems and the results may shed light on the potential development of novel AD therapeutic strategies based on targeting the D-isomerized Aβ, rather than natural L-Aβ.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesDrug DiscoveryEpitopesHumansKineticsMass SpectrometryPeptide FragmentsRecognition, PsychologyAmyloid beta-PeptidesEpitopesPeptide Fragments

Identifiers

PMID31695027
PMCPMC6834639
OpenAlexW2986840503

What OpenQuestion holds

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LicenceCC BY
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.