Evidence map›Paper›PMID 33905074›Full record

ArticleJournal of computer-aided molecular design2021

Discovery of novel IDO1 inhibitors via structure-based virtual screening and biological assays.

Huizhen Ge, Longfei Mao, Jie Zhao, Yuwei Wang, Danfeng Shi, Xing Yang, Xiaorui Wang, Huanxiang Liu, Xiaojun Yao

Abstract read
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In one paragraph

Article in Journal of computer-aided molecular design, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 47% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. 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 at 3 institutions in 2 countries.

Huizhen GeSchool of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000, China.
Longfei MaoSchool of Chemistry and Chemical Engineering, Henan Normal University, Xinxiang, 453007, China.
Jie ZhaoSchool of Chemistry and Chemical Engineering, Henan Normal University, Xinxiang, 453007, China.
Yuwei WangState Key Laboratory of Quality Research in Chinese Medicine, Macau Institute for Applied Research in Medicine and Health, Macau University of Science and Technology, Taipa, Macau, China.
Danfeng ShiSchool of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000, China.
Xing YangSchool of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000, China.
Xiaorui WangSchool of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000, China.
Huanxiang LiuSchool of Pharmacy, Lanzhou University, Lanzhou, 730000, China.
Xiaojun YaoSchool of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000, China. xjyao@lzu.edu.cn.ORCID 0000-0002-6972-2971
Lanzhou University · CNHenan Normal University · CNMacau University of Science and Technology · MO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Indoleamine 2,3-dioxygenase 1 (IDO1) is a heme-containing enzyme that catalyzes the first and rate-limiting step in catabolism of tryptophan via the kynurenine pathway, which plays a pivotal role in the proliferation and differentiation of T cells. IDO1 has been proven to be an attractive target for many diseases, such as breast cancer, lung cancer, colon cancer, prostate cancer, etc. In this study, docking-based virtual screening and bioassays were conducted to identify novel inhibitors of IDO1. The cellular assay demonstrated that 24 compounds exhibited potent inhibitory activity against IDO1 at micromolar level, including 8 compounds with IC

Indexed as

Drug DiscoveryDrug DesignEnzyme InhibitorsHumansIndoleamine-Pyrrole 2,3,-DioxygenaseMolecular Docking SimulationMolecular Dynamics SimulationSmall Molecule LibrariesStructure-Activity RelationshipEnzyme InhibitorsIDO1 protein, humanIndoleamine-Pyrrole 2,3,-DioxygenaseSmall Molecule LibrariesIDO1 inhibitorMM-GBSA calculationMolecular dockingMolecular dynamics simulationsVirtual screening

Identifiers

PMID33905074
OpenAlexW3157718659

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.