Evidence map›Paper›PMID 41293019›Full record

ArticlebioRxiv : the preprint server for biology2025

Activation parameters, enthalpy-entropy compensation and the temperature-dependent activity of enzymes.

Matthew J McLeod, Robert E Thorne

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Matthew J McLeodDepartment of Physics, Cornell University, 142 Sciences Dr., Ithaca New York, USA 14850.
Robert E ThorneDepartment of Physics, Cornell University, 142 Sciences Dr., Ithaca New York, USA 14850.ORCID 0000-0002-7489-8074

Funding

Technology Development for High-Throughput Biomolecular CryoSAXSR01GM127528 · NIGMS · CORNELL UNIVERSITY · PI THORNE, ROBERT E. · 2018 to 2021
$1.5M
NIGMS NIH HHS R01 GM127528
6 · The paper itself

Abstract

The increase in enzyme-catalyzed reaction rates with temperature is typically modeled using Arrhenius or Eyring relations. Interpretation of extracted parameters is subject to multiple caveats. Here we analyze the impact of expected small temperature variations of underlying activation/Eyring parameters on this modeling. Linear Arrhenius/Eyring behavior can still be observed when the underlying activation energy

Indexed as

activityArrheniusbindingenthalpy-entropy compensationenzymeenzyme kineticsEyringtemperature dependencevan ‘t Hoff

Identifiers

PMID41293019
PMCPMC12642627

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.