Evidence map›Paper›PMID 32014994›Full record

ArticleThe Journal of biological chemistry2020

Tuning of p

Warintra Pitsawong, Pirom Chenprakhon, Taweesak Dhammaraj, Dheeradhach Medhanavyn, Jeerus Sucharitakul, Chanakan Tongsook, Willem J H van Berkel, Pimchai Chaiyen, Anne-Frances Miller

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

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 40% 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

5 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
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 7 institutions in 3 countries.

Warintra PitsawongDepartment of Chemistry, University of Kentucky, Lexington, Kentucky 40506-0055.
Pirom ChenprakhonInstitute for Innovative Learning, Mahidol University, Nakhon Pathom 73170, Thailand.
Taweesak DhammarajFaculty of Pharmacy, Mahasarakham University, Maha Sarakham 44150, Thailand.
Dheeradhach MedhanavynDepartment of Biochemistry and Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University, Bangkok 10400, Thailand.
Jeerus SucharitakulDepartment of Biochemistry, Faculty of Dentistry, Chulalongkorn University, Bangkok 10300, Thailand.
Chanakan TongsookDepartment of Chemistry, Faculty of Science, Silpakorn University, Nakhon Pathom 73000, Thailand.
Willem J H van BerkelLaboratory of Food Chemistry, Wageningen University and Research, Bornse Weilanden 9, 6708 WG, Wageningen, The Netherlands.ORCID 0000-0002-6551-2782
Pimchai ChaiyenSchool of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology, Wangchan Valley, 555 Moo 1 Payupnai, Wangchan, Rayong 21210, Thailand pimchai.chaiyen@vistec.ac.th.ORCID 0000-0002-8533-1604
Anne-Frances MillerDepartment of Chemistry, University of Kentucky, Lexington, Kentucky 40506-0055 afmill3r2@gmail.com.ORCID 0000-0003-4973-2061
Mahidol University · THUniversity of Kentucky · USChulalongkorn University · THMahasarakham University · THSilpakorn University · THVidyasirimedhi Institute of Science and Technology · THWageningen University & Research · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hydroxylation of substituted phenols by flavin-dependent monooxygenases is the first step of their biotransformation in various microorganisms. The reaction is thought to proceed via electrophilic aromatic substitution, catalyzed by enzymatic deprotonation of substrate, in single-component hydroxylases that use flavin as a cofactor (group A). However, two-component hydroxylases (group D), which use reduced flavin as a co-substrate, are less amenable to spectroscopic investigation. Herein, we employed

Indexed as

4-Hydroxybenzoate-3-MonooxygenaseBacterial ProteinsBinding SitesBiocatalysisCatalytic DomainFlavinsHydrogen BondingHydrogen-Ion ConcentrationKineticsMixed Function OxygenasesMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularPhenylacetatesRhodococcusSubstrate Specificity3-fluoro-4-hydroxyphenylacetic acid4-Hydroxybenzoate-3-MonooxygenaseBacterial ProteinsFlavinsMixed Function OxygenasesPhenylacetates19F NMRenzyme kineticsenzyme mechanismflavinflavin-dependent monooxygenaseflavoproteinnuclear magnetic resonance (NMR)pKa tuning

Identifiers

PMID32014994
PMCPMC7086025
OpenAlexW3004026661

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.