Cryo-kinetics Reveal Dynamic Effects on the Chemistry of Human Dihydrofolate Reductase.

Aduragbemi S Adesina, Louis Y P Luk, Rudolf K Allemann

Open access · hybridAbstract read

In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

0.2field-weighted citation impact, top 52% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

Cryo-kinetics Reveal Dynamic Effects on the Chemistry of Human Dihydrofolate Reductase.Chembiochem : a European journal of chemical biology · 2021
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.

Aduragbemi S AdesinaSchool of Chemistry, Cardiff University, Park Place, Cardiff, CF10 3AT, UK.

Louis Y P LukSchool of Chemistry, Cardiff University, Park Place, Cardiff, CF10 3AT, UK.

Rudolf K AllemannSchool of Chemistry, Cardiff University, Park Place, Cardiff, CF10 3AT, UK.ORCID 0000-0002-1323-8830

Cardiff University · GB

Funding

BBSRC BB/J005266BBSRC BB/L020394Cardiff University

6 · The paper itself

Abstract

Effects of isotopic substitution on the rate constants of human dihydrofolate reductase (HsDHFR), an important target for anti-cancer drugs, have not previously been characterized due to its complex fast kinetics. Here, we report the results of cryo-measurements of the kinetics of the HsDHFR catalyzed reaction and the effects of protein motion on catalysis. Isotopic enzyme labeling revealed an enzyme KIE (k

Indexed as

Tetrahydrofolate DehydrogenaseBiocatalysisHumansKineticsTetrahydrofolate Dehydrogenasecryo-kineticsDHFRs and protein motionsheavy enzymehuman dihydrofolate reductase

Identifiers

PMID33876533

DOI10.1002/cbic.202100017

PMCPMC8360168

OpenAlexW3156658336

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.