Evidence map›Paper›PMID 38923323›Full record

ArticleFEBS open bio2024

Inhibition of human mevalonate kinase by allosteric inhibitors of farnesyl pyrophosphate synthase.

Saman Salari, Hiu-Fung Lee, Youla S Tsantrizos, Jaeok Park

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS open bio, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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

4 authors.

Saman SalariDepartment of Biochemistry, Memorial University of Newfoundland, St. John's, Canada.
Hiu-Fung LeeDepartment of Chemistry, McGill University, Montreal, Canada.
Youla S TsantrizosDepartment of Chemistry, McGill University, Montreal, Canada.
Jaeok ParkDepartment of Biochemistry, Memorial University of Newfoundland, St. John's, Canada.ORCID 0000-0002-8180-3950

Funding

Natural Sciences and Engineering Research Council of Canada DGECR-2020-00007Natural Sciences and Engineering Research Council of Canada RGPIN-2020-04281
6 · The paper itself

Abstract

Mevalonate kinase is a key regulator of the mevalonate pathway, subject to feedback inhibition by the downstream metabolite farnesyl pyrophosphate. In this study, we validated the hypothesis that monophosphonate compounds mimicking farnesyl pyrophosphate can inhibit mevalonate kinase. Exploring compounds originally synthesized as allosteric inhibitors of farnesyl pyrophosphate synthase, we discovered mevalonate kinase inhibitors with nanomolar activity. Kinetic characterization of the two most potent inhibitors demonstrated K

Indexed as

Enzyme InhibitorsPhosphotransferases (Alcohol Group Acceptor)Allosteric RegulationGeranyltranstransferaseHumansKineticsPolyisoprenyl PhosphatesSesquiterpenesEnzyme Inhibitorsfarnesyl pyrophosphateGeranyltranstransferasemevalonate kinasePhosphotransferases (Alcohol Group Acceptor)Polyisoprenyl PhosphatesSesquiterpenesfarnesyl pyrophosphatefeedback inhibitionisoprenoid synthesismevalonate kinasemevalonate pathwayphosphonate compounds

Identifiers

PMID38923323
PMCPMC11301271

What OpenQuestion holds

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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.