Evidence map›Paper›PMID 30603938›Full record

ArticleMolecular diversity2019

Hybrids of oxoisoaporphine-tetrahydroisoquinoline: novel multi-target inhibitors of inflammation and amyloid-β aggregation in Alzheimer's disease.

Yusi Chen, Chunlin Su, Li Wang, Jingfang Qin, Shenqi Wei, Huang Tang

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular diversity, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.3field-weighted citation impact, top 37% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Cupin-Type Dimethylsulfoniopropionate Lyase from Pelagibacter ubique (DddKAngewandte Chemie (International ed. in English) · 2025
    Article
  3. Article
  4. Review
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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

6 authors at 1 institution in 1 country.

Yusi ChenState Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, School of Chemistry and Pharmaceutical Sciences, Guangxi Normal University, Guilin City, Guangxi, China.
Chunlin SuState Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, School of Chemistry and Pharmaceutical Sciences, Guangxi Normal University, Guilin City, Guangxi, China.
Li WangState Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, School of Chemistry and Pharmaceutical Sciences, Guangxi Normal University, Guilin City, Guangxi, China.
Jingfang QinState Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, School of Chemistry and Pharmaceutical Sciences, Guangxi Normal University, Guilin City, Guangxi, China.
Shenqi WeiState Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, School of Chemistry and Pharmaceutical Sciences, Guangxi Normal University, Guilin City, Guangxi, China.
Huang TangState Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, School of Chemistry and Pharmaceutical Sciences, Guangxi Normal University, Guilin City, Guangxi, China. hyhth@163.com.ORCID http://orcid.org/0000-0002-0480-276X
Guangxi Normal University · CN

Funding

Guangxi Provincial Natural Science Foundation of China 2013GXNSFAA019132National Natural Science Foundation of China 81260471Program for Changjiang Scholars and Innovative Research Team in University of Ministry of Education of China IRT1225State Key Laboratory for Chemistry and Molecular Engineering of Medicinal Resources, Guangxi Normal University CMEMR2017-A09
6 · The paper itself

Abstract

A series of 8- and 11-substituted hybrids of oxoisoaporphine-tetrahydroisoquinoline have been designed and synthesized. The new derivatives strongly suppressed NO and iNOS production and modulated the production of cytokines by decreasing TNF-α and IL-1β formation in lipopolysaccharide-activated BV-2 microglia and RAW 264.7 macrophages. Meanwhile, incubation of these derivatives with SH-SY5Y cells that were transfected with human APP containing the Swedish mutations significantly decreased the secretion of Aβ

Indexed as

AcetylcholinesteraseAlzheimer DiseaseAmyloid beta-PeptidesAnimalsAnti-Inflammatory AgentsAporphinesButyrylcholinesteraseCell Line, TumorCholinesterase InhibitorsGene Expression Regulation, EnzymologicHumansInterleukin-1betaMiceMicrogliaMolecular Targeted TherapyNitric Oxide1,2,3,4-tetrahydroisoquinolineAcetylcholinesteraseAmyloid beta-Peptidesamyloid beta-protein (1-42)Anti-Inflammatory AgentsAporphinesButyrylcholinesteraseCholinesterase InhibitorsInterleukin-1betaNitric OxideNitric Oxide Synthase Type IIPeptide FragmentsProtein AggregatesTetrahydroisoquinolinesTumor Necrosis Factor-alphaAmyloid-β aggregationInflammationNeuroprotectionOxoisoaporphine derivatives

Identifiers

PMID30603938
OpenAlexW2908054343

What OpenQuestion holds

Textmetadata
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.