Evidence map›Paper›PMID 42504845›Full record

ArticleActa crystallographica. Section F, Structural biology communications2026

Structure of human aldehyde oxidase under tris(2-carboxyethyl)phosphine reducing conditions.

Carolina Videira, Mariam Esmaeeli, Silke Leimkühler, Maria João Romão, Cristiano Mota

Abstract read
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In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

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5 · Who and what money

Authors and funding

5 authors.

Carolina VideiraUCIBIO, Applied Molecular Biosciences Unit and Associate Laboratory i4HB - Institute for Health and Bioeconomy, Department of Chemistry NOVA School of Science and Technology, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal.
Mariam EsmaeeliDepartment of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, Potsdam, Germany.
Silke LeimkühlerDepartment of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, Potsdam, Germany.
Maria João RomãoUCIBIO, Applied Molecular Biosciences Unit and Associate Laboratory i4HB - Institute for Health and Bioeconomy, Department of Chemistry NOVA School of Science and Technology, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal.
Cristiano MotaUCIBIO, Applied Molecular Biosciences Unit and Associate Laboratory i4HB - Institute for Health and Bioeconomy, Department of Chemistry NOVA School of Science and Technology, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal.

Funding

Fundação para a Ciência e a Tecnologia 2023.18077.ICDTFundação para a Ciência e a Tecnologia LA/P/0140/2020Fundação para a Ciência e a Tecnologia UIDB/04378/2020Fundação para a Ciência e a Tecnologia UIDP/04378/2020
6 · The paper itself

Abstract

The importance of human aldehyde oxidase (hAOX1) has increased in recent decades due to its involvement in drug metabolism. Inhibition studies involving hAOX1 are extensive and a common reducing agent, dithiothreitol (DTT), was recently found to inactivate the enzyme. However, in previous crystallographic studies of hAOX1, DTT was found to be essential for crystallization. To surpass this concern, another reducing agent was used in crystallization trials. Using tris(2-carboxyethyl)phosphine (TCEP), a sulfur-free reducing agent, it was possible to obtain well ordered crystals of wild-type hAOX1 and a variant, hAOX1_6A, which diffracted beyond 2.3 Å resolution. Instead of the typical star-shaped crystals of hAOX1, at pH 4.7 plates are obtained in the orthorhombic space group P2

Indexed as

Aldehyde OxidasePhosphinesReducing AgentsCrystallizationCrystallography, X-RayDithiothreitolHumansOxidation-ReductionAldehyde OxidaseDithiothreitolPhosphinesReducing Agentstris(2-carboxyethyl)phosphinehuman aldehyde oxidaseprotein crystallizationTCEPX-ray crystallography

Identifiers

PMID42504845
PMCPMC13431053

What OpenQuestion holds

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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.