ThermoSlope: A Software for Determining Thermodynamic Parameters from Single Steady-State Experiments.

Open access · goldAbstract read

In one paragraph

Article in Molecules (Basel, Switzerland), 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 50% 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, 3 citations in OpenAlex.

Computational design of the temperature optimum of an enzyme reaction.Science advances · 2023
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

2 authors at 1 institution in 1 country.

Bjarte Aarmo LundHylleraas Centre for Quantum Molecular Sciences, Department of Chemistry, Faculty of Science and Technology, UiT The Arctic University of Norway, N9037 Tromsø, Norway.ORCID 0000-0001-9141-0555

Bjørn Olav BrandsdalHylleraas Centre for Quantum Molecular Sciences, Department of Chemistry, Faculty of Science and Technology, UiT The Arctic University of Norway, N9037 Tromsø, Norway.

UiT The Arctic University of Norway · NO

Funding

The Research Council of Norway 262695The Research Council of Norway 274858

6 · The paper itself

Abstract

The determination of the temperature dependence of enzyme catalysis has traditionally been a labourious undertaking. We have developed a new approach to the classical Arrhenius parameter estimation by fitting the change in velocity under a gradual change in temperature. The evaluation with a simulated dataset shows that the approach is valid. The approach is demonstrated as a useful tool by characterizing the

Indexed as

Arrhenius equationenzyme kineticsMichaelis–Menten kineticsthermodynamicstransition state theory

Identifiers

PMID34885737

DOI10.3390/molecules26237155

PMCPMC8658824

OpenAlexW3217380371

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.