Evidence map›Paper›PMID 34981773›Full record

ArticleActa crystallographica. Section F, Structural biology communications2022

Crystal structures of FolM alternative dihydrofolate reductase 1 from Brucella suis and Brucella canis.

Imani Porter, Trinity Neal, Zion Walker, Dylan Hayes, Kayla Fowler, Nyah Billups, Anais Rhoades, Christian Smith, Kaelyn Smith, Bart L Staker and 6 more

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

Article in Acta crystallographica. Section F, Structural biology communications, 2022. 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 79% 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, 3 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

16 authors at 2 institutions in 1 country.

Imani PorterDepartment of Chemistry and Biochemistry, Hampton University, 100 William R. Harvey Way, Hampton, VA 23668, USA.
Trinity NealDepartment of Chemistry and Biochemistry, Hampton University, 100 William R. Harvey Way, Hampton, VA 23668, USA.ORCID 0000-0003-3376-1327
Zion WalkerDepartment of Chemistry and Biochemistry, Hampton University, 100 William R. Harvey Way, Hampton, VA 23668, USA.ORCID 0000-0001-5331-8467
Dylan HayesDepartment of Chemistry and Biochemistry, Hampton University, 100 William R. Harvey Way, Hampton, VA 23668, USA.
Kayla FowlerDepartment of Chemistry and Biochemistry, Hampton University, 100 William R. Harvey Way, Hampton, VA 23668, USA.
Nyah BillupsDepartment of Chemistry and Biochemistry, Hampton University, 100 William R. Harvey Way, Hampton, VA 23668, USA.
Anais RhoadesDepartment of Chemistry and Biochemistry, Hampton University, 100 William R. Harvey Way, Hampton, VA 23668, USA.
Christian SmithDepartment of Chemistry and Biochemistry, Hampton University, 100 William R. Harvey Way, Hampton, VA 23668, USA.
Kaelyn SmithDepartment of Chemistry and Biochemistry, Hampton University, 100 William R. Harvey Way, Hampton, VA 23668, USA.
Bart L StakerSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, Washington, USA.
David M DranowSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, Washington, USA.
Stephen J MayclinSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, Washington, USA.
Sandhya SubramanianSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, Washington, USA.
Thomas E EdwardsSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, Washington, USA.ORCID 0000-0002-0474-8003
Peter J MylerSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, Washington, USA.
Oluwatoyin A AsojoDepartment of Chemistry and Biochemistry, Hampton University, 100 William R. Harvey Way, Hampton, VA 23668, USA.ORCID 0000-0002-4043-2700
Hampton University · USCenter for Infectious Disease Research · US

Funding

HU-CHEM: Deploying evidence-based interventions in Chemistry at Hampton University to plug leaks in the biomedical training pipelineU01GM138433 · NIGMS · HAMPTON UNIVERSITY · PI ASOJO, OLUWATOYIN AJIBOLA · 2020 to 2022
$1.1M
NIAID NIH HHS HHSN272200700057CNIAID NIH HHS HHSN272201200025CNIAID NIH HHS HHSN272201700059CNIGMS NIH HHS 1U01GM138433NIGMS NIH HHS U01 GM138433
6 · The paper itself

Abstract

Members of the bacterial genus Brucella cause brucellosis, a zoonotic disease that affects both livestock and wildlife. Brucella are category B infectious agents that can be aerosolized for biological warfare. As part of the structural genomics studies at the Seattle Structural Genomics Center for Infectious Disease (SSGCID), FolM alternative dihydrofolate reductases 1 from Brucella suis and Brucella canis were produced and their structures are reported. The enzymes share ∼95% sequence identity but have less than 33% sequence identity to other homologues with known structure. The structures are prototypical NADPH-dependent short-chain reductases that share their highest tertiary-structural similarity with protozoan pteridine reductases, which are being investigated for rational therapeutic development.

Indexed as

Brucella canisBrucella suisBrucellosisTetrahydrofolate DehydrogenaseCrystallography, X-RayHumansTetrahydrofolate DehydrogenaseBrucella canisBrucella suisdihydrofolate reductasesNADPHoxidoreductasesSeattle Structural Genomics Center for Infectious Diseaseshort-chain dehydrogenase/reductase familySSGCID

Identifiers

PMID34981773
PMCPMC8725004
OpenAlexW4200290533

What OpenQuestion holds

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LicenceCC BY
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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.