Evidence map›Paper›PMID 35493254›Full record

ArticleRSC advances2021

Chemical synthesis, inhibitory activity and molecular mechanism of 1-deoxynojirimycin-chrysin as a potent α-glucosidase inhibitor.

Ran Zhang, Yueyue Zhang, Gaiqun Huang, Xiangdong Xin, Liumei Tang, Hao Li, Kwang Sik Lee, Byung Rae Jin, Zhongzheng Gui

Open access · goldAbstract read
In one paragraph

Article in RSC advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 22% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

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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

9 authors at 2 institutions in 2 countries.

Ran ZhangSchool of Biotechnology, Jiangsu University of Science and Technology Zhenjiang 212100 Jiangsu People's Republic of China srizzgui@hotmail.com.ORCID https://orcid.org/0000-0003-3661-7785
Yueyue ZhangSchool of Biotechnology, Jiangsu University of Science and Technology Zhenjiang 212100 Jiangsu People's Republic of China srizzgui@hotmail.com.
Gaiqun HuangSchool of Biotechnology, Jiangsu University of Science and Technology Zhenjiang 212100 Jiangsu People's Republic of China srizzgui@hotmail.com.
Xiangdong XinSchool of Biotechnology, Jiangsu University of Science and Technology Zhenjiang 212100 Jiangsu People's Republic of China srizzgui@hotmail.com.
Liumei TangSchool of Biotechnology, Jiangsu University of Science and Technology Zhenjiang 212100 Jiangsu People's Republic of China srizzgui@hotmail.com.
Hao LiSchool of Biotechnology, Jiangsu University of Science and Technology Zhenjiang 212100 Jiangsu People's Republic of China srizzgui@hotmail.com.
Kwang Sik LeeCollege of Natural Resources and Life Science, Dong-A University Busan 49315 Republic of Korea.
Byung Rae JinCollege of Natural Resources and Life Science, Dong-A University Busan 49315 Republic of Korea.
Zhongzheng GuiSchool of Biotechnology, Jiangsu University of Science and Technology Zhenjiang 212100 Jiangsu People's Republic of China srizzgui@hotmail.com.ORCID https://orcid.org/0000-0003-3242-576X
Jiangsu University of Science and Technology · CNDong-A University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hyperglycemia can be efficaciously regulated by inhibiting α-glucosidase activity and this is regarded as an effective strategy to treat type 2 diabetes. 1-Deoxynojimycin, an α-glucosidase inhibitor, can penetrate cells rapidly to potently inhibit α-glucosidase in a competitive manner. However, the application of 1-deoxynojimycin is limited by its poor lipophilicity and low bioavailability. Herein, three 1-deoxynojimycin derivatives 4-6 were designed and synthesized by linking 1-deoxynojimycin and chrysin to ameliorate the limitations of 1-deoxynojimycin. Among them, compound 6, a conjugate of 1-deoxynojimycin and chrysin linked by an undecane chain, could better bind to the α-glucosidase catalytic site, thereby exhibiting excellent α-glucosidase inhibitory activity (IC

Identifiers

PMID35493254
PMCPMC9044198
OpenAlexW3215280398

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.