Evidence map›Paper›PMID 33807076›Full record

ArticleInternational journal of molecular sciences2021

Conformational Heterogeneity and Cooperative Effects of Mammalian ALOX15.

Igor Ivanov, Alejandro Cruz, Alexander Zhuravlev, Almerinda Di Venere, Eleonora Nicolai, Sabine Stehling, José M Lluch, Àngels González-Lafont, Hartmut Kuhn

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 29% 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

8 citing papers in PubMed, 8 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

9 authors at 4 institutions in 4 countries.

Igor IvanovLomonosov Institute of Fine Chemical Technologies, MIREA-Russian Technological University, Vernadskogo pr. 86, 119571 Moscow, Russia.ORCID 0000-0003-0543-2067
Alejandro CruzDepartament de Química, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain.ORCID 0000-0003-0928-0718
Alexander ZhuravlevLomonosov Institute of Fine Chemical Technologies, MIREA-Russian Technological University, Vernadskogo pr. 86, 119571 Moscow, Russia.
Almerinda Di VenereDepartment of Experimental Medicine, University of Tor Vergata, Via Montpellier 1, 00133 Rome, Italy.
Eleonora NicolaiDepartment of Experimental Medicine, University of Tor Vergata, Via Montpellier 1, 00133 Rome, Italy.ORCID 0000-0003-1415-9808
Sabine StehlingInstitute of Biochemistry, Charite-University Medicine Berlin, Corporate member of Free University Berlin, Humboldt University Berlin and Berlin Institute of Health, Charitéplatz 1, D-10117 Berlin, Germany.
José M LluchDepartament de Química, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain.ORCID 0000-0002-7536-1869
Àngels González-LafontDepartament de Química, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain.ORCID 0000-0003-0729-2483
Hartmut KuhnInstitute of Biochemistry, Charite-University Medicine Berlin, Corporate member of Free University Berlin, Humboldt University Berlin and Berlin Institute of Health, Charitéplatz 1, D-10117 Berlin, Germany.ORCID 0000-0001-8142-3192
Universitat Autònoma de Barcelona · ESBerlin Institute of Health at Charité - Universitätsmedizin Berlin · DEMIREA - Russian Technological University · RUUniversity of Rome Tor Vergata · IT

Funding

Deutsche Forschungsgemeinschaft KU 961/14-1Russian Foundation for Basic Research 19-54-12002 and 19-04-00082Spanish "Ministerio de Ciencia, Innovación y Universidades" CTQ2017-83745-P
6 · The paper itself

Abstract

Arachidonic acid lipoxygenases (ALOXs) have been suggested to function as monomeric enzymes, but more recent data on rabbit ALOX15 indicated that there is a dynamic monomer-dimer equilibrium in aqueous solution. In the presence of an active site ligand (the ALOX15 inhibitor RS7) rabbit ALOX15 was crystalized as heterodimer and the X-ray coordinates of the two monomers within the dimer exhibit subtle structural differences. Using native polyacrylamide electrophoresis, we here observed that highly purified and predominantly monomeric rabbit ALOX15 and human ALOX15B are present in two conformers with distinct electrophoretic mobilities. In silico docking studies, molecular dynamics simulations, site directed mutagenesis experiments and kinetic measurements suggested that in aqueous solutions the two enzymes exhibit motional flexibility, which may impact the enzymatic properties.

Indexed as

Models, MolecularProtein ConformationAmino Acid SubstitutionAnimalsArachidonate 15-LipoxygenaseCatalysisHumansIsoenzymesKineticsMutationProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationRabbitsArachidonate 15-LipoxygenaseIsoenzymescooperative effectscrystal structurelipoxygenasesmolecular dynamicsprotein–protein interactions

Identifiers

PMID33807076
PMCPMC8004969
OpenAlexW3140773363

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.