Evidence map›Paper›PMID 37607127›Full record

ArticleAngewandte Chemie (International ed. in English)2023

Electrochemical Nanoreactor Provides a Comprehensive View of Isocitrate Dehydrogenase Cancer-drug Kinetics.

Ryan A Herold, Christopher J Schofield, Fraser A Armstrong

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
5.8field-weighted citation impact, top 4% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Electroenzymatic COAngewandte Chemie (International ed. in English) · 2026
    Review
  2. Lessons, connections, hypotheses and predictions from protein film electrochemistry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Review
  3. Review
  4. Building Localized NADP(H) Recycling Circuits to Advance Enzyme Cascadetronics.Angewandte Chemie (International ed. in English) · 2025
    Article
  5. Article
  6. 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

3 authors at 1 institution in 1 country.

Ryan A HeroldInorganic Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford, OX1 3QR, UK.ORCID 0000-0001-7935-6269
Christopher J SchofieldDepartment of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Mansfield Road, Oxford, OX1 3QY, UK.ORCID 0000-0002-0290-6565
Fraser A ArmstrongInorganic Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford, OX1 3QR, UK.ORCID 0000-0001-8041-2491
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/P023797/1Cancer Research UK 28285Wellcome TrustWellcome Trust 106244/Z14/Z
6 · The paper itself

Abstract

The ability to control enzyme cascades entrapped in a nanoporous electrode material (the "Electrochemical Leaf", e-Leaf) has been exploited to gain detailed kinetic insight into the mechanism of an anti-cancer drug. Ivosidenib, used to treat acute myeloid leukemia, acts on a common cancer-linked variant of isocitrate dehydrogenase 1 (IDH1 R132H) inhibiting its "gain-of-function" activity-the undesired reduction of 2-oxoglutarate (2OG) to the oncometabolite 2-hydroxyglutarate (2HG). The e-Leaf quantifies the kinetics of IDH1 R132H inhibition across a wide and continuous range of conditions, efficiently revealing factors underlying the inhibitor residence time. Selective inhibition of IDH1 R132H by Ivosidenib and another inhibitor, Novartis 224, is readily resolved as a two-stage process whereby initial rapid non-inhibitory binding is followed by a slower step to give the inhibitory complex. These kinetic features are likely present in other allosteric inhibitors of IDH1/2. Such details, essential for understanding inhibition mechanisms, are not readily resolved in conventional steady-state kinetics or by techniques that rely only on measuring binding. Extending the new method and analytical framework presented here to other enzyme systems will be straightforward and should rapidly reveal insight that is difficult or often impossible to obtain using other methods.

Indexed as

Antineoplastic AgentsLeukemia, Myeloid, AcuteHumansIsocitrate DehydrogenaseMutationNanotechnologyAntineoplastic AgentsIsocitrate DehydrogenaseEnzyme InhibitionEnzyme MechanismIsocitrate DehydrogenaseKineticsNanoconfinement

Identifiers

PMID37607127
PMCPMC10962598
OpenAlexW4386027269

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.