Evidence map›Paper›PMID 38691589›Full record

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

Catalysis driven by an amyloid-substrate complex.

Taka Sawazaki, Daisuke Sasaki, Youhei Sohma

Open access · hybridAbstract read
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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Article
  3. Amyloid-reoriented enzyme catalysis.Nature communications · 2025
    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.

Taka SawazakiDepartment of Medicinal Chemistry, School of Pharmaceutical Sciences, Wakayama Medical University, Wakayama 640-8156, Japan.ORCID 0000-0001-5650-998X
Daisuke SasakiDepartment of Medicinal Chemistry, School of Pharmaceutical Sciences, Wakayama Medical University, Wakayama 640-8156, Japan.ORCID 0000-0002-2224-1900
Youhei SohmaDepartment of Medicinal Chemistry, School of Pharmaceutical Sciences, Wakayama Medical University, Wakayama 640-8156, Japan.ORCID 0000-0002-1154-3903
Wakayama Medical University · JP

Funding

MEXT | Japan Society for the Promotion of Science (JSPS) JP21H02602MEXT | Japan Society for the Promotion of Science (JSPS) JP21K20727MEXT | Japan Society for the Promotion of Science (JSPS) JP23K14325
6 · The paper itself

Abstract

Amine modification through nucleophilic attack of the amine functionality is a very common chemical transformation. Under biorelevant conditions using acidic-to-neutral pH buffer, however, the nucleophilic reaction of alkyl amines (pKa ≈ 10) is not facile due to the generation of ammonium ions lacking nucleophilicity. Here, we disclose a unique molecular transformation system,

Indexed as

AmyloidAminesCatalysisHumansHydrogen BondingHydrogen-Ion ConcentrationIslet Amyloid PolypeptideAminesAmyloidIslet Amyloid Polypeptideamyloidamyloid catalystcatalysisnucleophilic reaction

Identifiers

PMID38691589
PMCPMC11087796
OpenAlexW4396541898

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.