Evidence map›Paper›PMID 28933241›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2017

Characterization of human S-adenosyl-homocysteine hydrolase in vitro and identification of its potential inhibitors.

Weiwei Hao, Yanhua Li, Qiuli Shan, Tian Han, Wencheng Li, Sheng He, Kongkai Zhu, Yumei Li, Xiaojun Tan, Jinsong Gu

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

Article in Journal of enzyme inhibition and medicinal chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact, top 78% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
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  4. Targeting one-carbon metabolism for cancer immunotherapy.Clinical and translational medicine · 2024
    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

10 authors at 1 institution in 1 country.

Weiwei Haoa School of Biological Science and Technology , University of Jinan , Jinan , China.
Yanhua Lia School of Biological Science and Technology , University of Jinan , Jinan , China.
Qiuli Shana School of Biological Science and Technology , University of Jinan , Jinan , China.
Tian Hana School of Biological Science and Technology , University of Jinan , Jinan , China.
Wencheng Lia School of Biological Science and Technology , University of Jinan , Jinan , China.
Sheng Hea School of Biological Science and Technology , University of Jinan , Jinan , China.
Kongkai Zhua School of Biological Science and Technology , University of Jinan , Jinan , China.
Yumei Lia School of Biological Science and Technology , University of Jinan , Jinan , China.
Xiaojun Tana School of Biological Science and Technology , University of Jinan , Jinan , China.
Jinsong Gua School of Biological Science and Technology , University of Jinan , Jinan , China.ORCID http://orcid.org/0000-0003-2540-9980
University of Jinan · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human S-adenosyl-homocysteine hydrolase (SAHH, E.C.3.3.1.1) has been considered to be an attractive target for the design of medicines to treat human disease, because of its important role in regulating biological methylation reactions to catalyse the reversible hydrolysis of S-adenosylhomocysteine (SAH) to adenosine (Ado) and l-homocysteine (Hcy). In this study, SAHH protein was successfully cloned and purified with optimized, Pichia pastoris (P. pastoris) expression system. The biological activity results revealed that, among the tested compounds screened by ChemMapper and SciFinder Scholar, 4-(3-hydroxyprop-1-en-1-yl)-2-methoxyphenol (coniferyl alcohol, CAS: 458-35-5, ZINC: 12359045) exhibited the highest inhibition against rSAHH (IC

Indexed as

AdenosylhomocysteinaseDose-Response Relationship, DrugEnzyme InhibitorsHumansHydrogen-Ion ConcentrationMolecular Docking SimulationMolecular StructurePhenolsStructure-Activity RelationshipTemperatureAdenosylhomocysteinaseconiferyl alcoholEnzyme InhibitorsPhenolsconiferyl alcoholinhibitorsl-homocysteine (Hcy)Pichia pastorisS-adenosyl-homocysteine hydrolase (SAHH)

Identifiers

PMID28933241
PMCPMC6445193
OpenAlexW2759726837

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.