Random acceleration and steered molecular dynamics simulations reveal the (un)binding tunnels in adenosine deaminase and critical residues in tunnels.

Yue Pan, Renrui Qi, Minghao Li, Bingda Wang, Honglan Huang, Weiwei Han

Open access · goldAbstract read

In one paragraph

Article in RSC advances, 2020. 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 53% 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, 5 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

6 authors at 1 institution in 3 countries.

Yue PanKey Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Science, Jilin University 2699 Qianjin Street Changchun 130012 China weiweihan@jlu.edu.cn.

Renrui QiKey Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Science, Jilin University 2699 Qianjin Street Changchun 130012 China weiweihan@jlu.edu.cn.

Minghao LiKey Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Science, Jilin University 2699 Qianjin Street Changchun 130012 China weiweihan@jlu.edu.cn.

Bingda WangKey Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Science, Jilin University 2699 Qianjin Street Changchun 130012 China weiweihan@jlu.edu.cn.

Honglan HuangDepartment of Pathobiology, College of Basic Medical Sciences, Jilin University Changchun China hhl@jlu.edu.cn.

Weiwei HanKey Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Science, Jilin University 2699 Qianjin Street Changchun 130012 China weiweihan@jlu.edu.cn.ORCID https://orcid.org/0000-0002-1931-9316

Jilin University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adenosine deaminase (ADA) is an important enzyme related to purine nucleoside metabolism in human serum and various tissues. Abnormal ADA levels are related to a wide variety of diseases such as rheumatoid arthritis, AIDS, anemia, lymphoma, and leukemia and ADA is considered as a useful target for various diseases. Currently, ADA can be divided into open conformation and closed conformation according to the inhibitors of binding. As a consequence, we chose two inhibitors, namely, 6-hydroxy-1,6-dihydro purine nucleoside (PRH) and

Identifiers

PMID35517169

DOI10.1039/d0ra07796h

PMCPMC9058408

OpenAlexW3113058822

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.