Evidence map›Paper›PMID 40376397›Full record

ReviewBiophysical reviews2025

Non-hyperbolic enzyme kinetics: the case of P-type ATPases.

S E Faraj, M R Montes, R D Peluffo, R M González-Lebrero, R C Rossi

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Biophysical reviews, 2025. 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
–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

1 citing paper in PubMed.

  1. 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

5 authors.

S E FarajFacultad de Farmacia y Bioquímica, Departamento de Química Biológica, Universidad de Buenos Aires, Buenos Aires, Argentina.
M R MontesFacultad de Farmacia y Bioquímica, Departamento de Química Biológica, Universidad de Buenos Aires, Buenos Aires, Argentina.ORCID 0000-0003-1589-0256
R D PeluffoGroup of Biophysical Chemistry, Department of Biological Sciences, CENUR Litoral Norte, Universidad de La República, Rivera 1350, CP: 50000, Salto, Uruguay.
R M González-LebreroFacultad de Farmacia y Bioquímica, Departamento de Química Biológica, Universidad de Buenos Aires, Buenos Aires, Argentina.ORCID 0000-0002-3832-2270
R C RossiFacultad de Farmacia y Bioquímica, Departamento de Química Biológica, Universidad de Buenos Aires, Buenos Aires, Argentina.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many enzymes operate through mechanisms that comply with the Michaelis-Menten equation (hyperbolic kinetics). The theoretical framework for analyzing these enzymes, widely developed in the literature, is largely based on the ability to linearize the equation and apply linear regression to experimental data. However, certain systems, such as P-type ATPases, present mechanisms that do not fit into hyperbolic models, requiring the development of more complex equations. This study explores the underlying causes of the non-hyperbolic behavior observed for P-type ATPases and reviews some methodologies used for their analysis. Here, we propose to employ rational equations, whose form limits the range of possible kinetic models applicable to the system, offering a structured approach to its analysis.

Indexed as

Albers-Post schemeEmpirical equationsHill equationIon-transporting ATPasesMichaelis–Menten

Identifiers

PMID40376397
PMCPMC12075054

What OpenQuestion holds

Textmetadata
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Registered trials

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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.