Evidence map›Paper›PMID 36071810›Full record

ArticleIUCrJ2022

Organism-specific differences in the binding of ketoprofen to serum albumin.

Mateusz P Czub, Alan J Stewart, Ivan G Shabalin, Wladek Minor

Open access · goldAbstract read
In one paragraph

Article in IUCrJ, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

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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

4 authors at 2 institutions in 2 countries.

Mateusz P CzubDepartment of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA 22908, USA.ORCID https://orcid.org/0000-0001-8973-4569
Alan J StewartSchool of Medicine, University of St Andrews, St Andrews KY16 9TF, United Kingdom.ORCID https://orcid.org/0000-0003-4580-1840
Ivan G ShabalinDepartment of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA 22908, USA.ORCID https://orcid.org/0000-0003-3955-9242
Wladek MinorDepartment of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA 22908, USA.ORCID https://orcid.org/0000-0001-7075-7090
University of Virginia · USUniversity of St Andrews · GB

Funding

Reproducible, Unbiased Ligand Identification Assisted by Artificial Intelligence and Development of Ligand Reference LibrariesR01GM132595 · NIGMS · UNIVERSITY OF VIRGINIA · PI MINOR, WLADEK · 2019 to 2022
$2.3M
Metal binding sites in macromolecular structuresR01GM117325 · NIGMS · UNIVERSITY OF VIRGINIA · PI MINOR, WLADEK · 2016 to 2019
$1.3M
NIAID NIH HHS HHSN272201200026CNIAID NIH HHS HHSN272201700060CNIGMS NIH HHS R01 GM117325NIGMS NIH HHS R01 GM132595
6 · The paper itself

Abstract

Serum albumin is a circulatory transport protein that has a highly conserved sequence and structure across mammalian organisms. Its ligand-binding properties are of importance as albumin regulates the pharmacokinetics of many drugs. Due to the high degree of structural conservation between mammalian albumins, nonhuman albumins such as bovine serum albumin or animal models are often used to understand human albumin-drug interactions. Ketoprofen is a popular nonsteroidal anti-inflammatory drug that is transported by albumin. Here, it is revealed that ketoprofen exhibits different binding-site preferences when interacting with human serum albumin compared with other mammalian albumins, despite the conservation of binding sites across species. The reasons for the observed differences were explored, including identifying ketoprofen binding determinants at specific sites and the influence of fatty acids and other ligands on drug binding. The presented results reveal that the drug-binding properties of albumins cannot easily be predicted based only on a complex of albumin from another organism and the conservation of drug sites between species. This work shows that understanding organism-dependent differences is essential for assessing the suitability of particular albumins for structural or biochemical studies.

Indexed as

anti-inflammatory drugsdrug interactionsdrug transporthuman serum albuminketoprofenNSAIDsorganism-dependent studies

Identifiers

PMID36071810
PMCPMC9438504
OpenAlexW4285587587

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.