Evidence map›Paper›PMID 34485859›Full record

ArticleiScience2021

Redox manipulation of enzyme activity through physiologically active molecule.

Dao Lin, Yuhe Kan, Liang Yan, Yongqi Ke, Yang Zhang, Hang Luo, Xinjing Tang, Xiangjun Li, Yujian He, Li Wu

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in iScience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 58% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

10 authors at 2 institutions in 1 country.

Dao LinSchool of Chemical Sciences, University of Chinese Academy of Sciences, Beijing 101408, China.
Yuhe KanSchool of Chemical Sciences, University of Chinese Academy of Sciences, Beijing 101408, China.
Liang YanSchool of Chemical Sciences, University of Chinese Academy of Sciences, Beijing 101408, China.
Yongqi KeSchool of Chemical Sciences, University of Chinese Academy of Sciences, Beijing 101408, China.
Yang ZhangSchool of Chemical Sciences, University of Chinese Academy of Sciences, Beijing 101408, China.
Hang LuoSchool of Chemical Sciences, University of Chinese Academy of Sciences, Beijing 101408, China.
Xinjing TangState Key Laboratory of Natural and Biomimetic Drugs, School of Pharmaceutical Sciences, Peking University, Beijing 100191, China.
Xiangjun LiSchool of Chemical Sciences, University of Chinese Academy of Sciences, Beijing 101408, China.
Yujian HeSchool of Chemical Sciences, University of Chinese Academy of Sciences, Beijing 101408, China.
Li WuSchool of Chemical Sciences, University of Chinese Academy of Sciences, Beijing 101408, China.
University of Chinese Academy of Sciences · CNPeking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The effective utility of physiologically active molecules is crucial in numerous biological processes. However, the regulation of enzyme functions through active substances remains challenging at present. Here, glutathione (GSH), produced in cells, was used to modulate the catalytic activity of thrombin without external stimulus. It was found that high concentrations of GSH was more conducive to initiate the cleavage of compound AzoDiTAB in the range of concentration used to mimic the difference between cancer and normal cells, which has practical implications for targeting cancel cells since GSH is overexpressed in cancer cells. Importantly, GSH treatment caused the deformation of G4 structure by cleaving AzoDiTAB and thus triggered the transition of thrombin from being free to be inhibited in complex biological systems. This work would open up a new route for the specific manipulation of enzyme-catalyzed systems in cancer cells.

Indexed as

Biochemical MechanismBiochemistry ApplicationsCancerMedical Biochemistry

Identifiers

PMID34485859
PMCPMC8405983
OpenAlexW3195932461

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.