Evidence map›Paper›PMID 37124297›Full record

ArticleJACS Au2023

Decoding the Roles of Amyloid-β (1-42)'s Key Oligomerization Domains toward Designing Epitope-Specific Aggregation Inhibitors.

Dongjoon Im, Soohyeong Kim, Gyusub Yoon, Da Gyeong Hyun, Yu-Gon Eom, Ye Eun Lee, Chang Ho Sohn, Jeong-Mo Choi, Hugh I Kim

Abstract read
In one paragraph

Article in JACS Au, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Multivalent Neuroprotective Activity ofPharmaceuticals (Basel, Switzerland) · 2024
    Article
  8. Article
  9. Article
  10. Neuroprotection byInternational journal of molecular sciences · 2024
    Article
  11. Review
  12. Article
  13. Antioxidants (Basel, Switzerland) · 2023
    Article
  14. 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

9 authors.

Dongjoon ImDepartment of Chemistry, Korea University, Seoul 02841, Republic of Korea.ORCID https://orcid.org/0000-0002-6206-657X
Soohyeong KimDepartment of Chemistry, Korea University, Seoul 02841, Republic of Korea.
Gyusub YoonDepartment of Chemistry, Korea University, Seoul 02841, Republic of Korea.
Da Gyeong HyunDepartment of Chemistry, Korea University, Seoul 02841, Republic of Korea.
Yu-Gon EomDepartment of Chemistry, Pusan National University, Busan 46241, Republic of Korea.
Ye Eun LeeDepartment of Chemistry, Korea University, Seoul 02841, Republic of Korea.ORCID https://orcid.org/0000-0001-7151-1009
Chang Ho SohnCenter for Nanomedicine, Institute for Basic Science (IBS), Seoul 03722, Republic of Korea.ORCID https://orcid.org/0000-0002-7585-1841
Jeong-Mo ChoiDepartment of Chemistry, Pusan National University, Busan 46241, Republic of Korea.
Hugh I KimDepartment of Chemistry, Korea University, Seoul 02841, Republic of Korea.ORCID https://orcid.org/0000-0001-9205-1806

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fibrillar amyloid aggregates are the pathological hallmarks of multiple neurodegenerative diseases. The amyloid-β (1-42) protein, in particular, is a major component of senile plaques in the brains of patients with Alzheimer's disease and a primary target for disease treatment. Determining the essential domains of amyloid-β (1-42) that facilitate its oligomerization is critical for the development of aggregation inhibitors as potential therapeutic agents. In this study, we identified three key hydrophobic sites (

Identifiers

PMID37124297
PMCPMC10131210

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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.