Evidence map›Paper›PMID 37165541›Full record

ArticleProtein science : a publication of the Protein Society2023

Biochemical and structural characterization of meningococcal methylenetetrahydrofolate reductase.

Wanita Pantong, Jordan L Pederick, Somchart Maenpuen, Ruchanok Tinikul, Jaime J Jayapalan, Blagojce Jovcevski, Kate L Wegener, John B Bruning, Wanisa Salaemae

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

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. The T120P or M172V mutation onEmerging microbes & infections · 2024
    Article
  3. 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 5 institutions in 3 countries.

Wanita PantongDivision of Health and Applied Sciences, Faculty of Science, Prince of Songkla University, Songkhla, Thailand.
Jordan L PederickDepartment of Molecular and Biomedical Science, School of Biological Sciences, The University of Adelaide, Adelaide, South Australia, Australia.
Somchart MaenpuenDepartment of Biochemistry, Faculty of Science, Burapha University, Chonburi, Thailand.
Ruchanok TinikulDepartment of Biochemistry and Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University, Bangkok, Thailand.
Jaime J JayapalanDepartment of Molecular Medicine, Faculty of Medicine, Universiti Malaya, Kuala Lumpur, Malaysia.
Blagojce JovcevskiInstitute for Photonics and Advanced Sensing (IPAS), School of Biological Sciences, The University of Adelaide, Adelaide, South Australia, Australia.
Kate L WegenerDepartment of Molecular and Biomedical Science, School of Biological Sciences, The University of Adelaide, Adelaide, South Australia, Australia.
John B BruningDepartment of Molecular and Biomedical Science, School of Biological Sciences, The University of Adelaide, Adelaide, South Australia, Australia.
Wanisa SalaemaeDivision of Health and Applied Sciences, Faculty of Science, Prince of Songkla University, Songkhla, Thailand.ORCID 0000-0001-6015-3904
The University of Adelaide · AUPrince of Songkla University · THBurapha University · THMahidol University · THUniversity of Malaya · MY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methylenetetrahydrofolate reductase (MTHFR) is a key metabolic enzyme in colonization and virulence of Neisseria meningitidis, a causative agent of meningococcal diseases. Here, the biochemical and structural properties of MTHFR from a virulent strain of N. meningitidis serogroup B (NmMTHFR) were characterized. Unlike other orthologs, NmMTHFR functions as a unique homohexamer, composed of three homo-dimerization partners, as shown in our 2.7 Å resolution crystal structure. Six active sites were formed solely within monomers and located away from the oligomerization interfaces. Flavin adenine dinucleotide cofactor formed hydrogen bonds with conserved sidechains, positioning its isoalloxazine ring adjacent to the overlapping binding sites of nicotinamide adenine dinucleotide (NADH) coenzyme and CH

Indexed as

Methylenetetrahydrofolate Reductase (NADPH2)Neisseria meningitidisAdenineFolic AcidHumansModels, MolecularNADNADPAdenineFolic AcidMethylenetetrahydrofolate Reductase (NADPH2)NADNADPfolate cyclemethionine biosynthesismethylenetetrahydrofolate reductaseNeisseria meningitidisX-ray crystal structure

Identifiers

PMID37165541
PMCPMC10201697
OpenAlexW4376131331

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.