Evidence map›Paper›PMID 38030974›Full record

ArticleCellular & molecular biology letters2023

Knock-in mice expressing a humanized arachidonic acid 15-lipoxygenase (Alox15) carry a partly dysfunctional erythropoietic system.

Florian Reisch, Dagmar Heydeck, Marjann Schäfer, Michael Rothe, Jiaxing Yang, Sabine Stehling, Gerhard P Püschel, Hartmut Kuhn

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cellular & molecular biology letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

6 citing papers in PubMed, 6 citations in OpenAlex.

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  6. Review
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

8 authors at 3 institutions in 1 country.

Florian ReischDepartment of Biochemistry, Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt Universität Zu Berlin, Charitéplatz 1, 10117, Berlin, Germany.
Dagmar HeydeckDepartment of Biochemistry, Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt Universität Zu Berlin, Charitéplatz 1, 10117, Berlin, Germany.
Marjann SchäferDepartment of Biochemistry, Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt Universität Zu Berlin, Charitéplatz 1, 10117, Berlin, Germany.
Michael RotheLipidomix GmbH, Robert-Rössle-Straße 10, 13125, Berlin, Germany.
Jiaxing YangDepartment of Biochemistry, Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt Universität Zu Berlin, Charitéplatz 1, 10117, Berlin, Germany.
Sabine StehlingDepartment of Biochemistry, Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt Universität Zu Berlin, Charitéplatz 1, 10117, Berlin, Germany.
Gerhard P PüschelInstitute for Nutritional Sciences, University of Potsdam, Arthur-Scheunert-Allee 114-116, 14558, Nuthetal, Germany.
Hartmut KuhnDepartment of Biochemistry, Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt Universität Zu Berlin, Charitéplatz 1, 10117, Berlin, Germany. hartmut.kuehn@charite.de.ORCID http://orcid.org/0000-0001-8142-3192
Humboldt-Universität zu Berlin · DEUniversity of Potsdam · DELipidomix (Germany) · DE

Funding

Deutsche Forschungsgemeinschaft HE8295/1-1Deutsche Forschungsgemeinschaft KU961/13-1Deutsche Forschungsgemeinschaft KU961/14-1
6 · The paper itself

Abstract

Arachidonic acid 15-lipoxygenases (ALOX15) play a role in mammalian erythropoiesis but they have also been implicated in inflammatory processes. Seven intact Alox genes have been detected in the mouse reference genome and the mouse Alox15 gene is structurally similar to the orthologous genes of other mammals. However, mouse and human ALOX15 orthologs have different functional characteristics. Human ALOX15 converts C

Indexed as

Arachidonate 15-LipoxygenaseHydrogen PeroxideAnimalsArachidonate 12-LipoxygenaseArachidonic AcidFemaleHumansMaleMammalsMiceAlox15 protein, mouseArachidonate 12-LipoxygenaseArachidonate 15-LipoxygenaseArachidonic AcidHydrogen PeroxideEicosanoidsErythropoiesisLipid peroxidationOxidative stressPolyenoic fatty acids

Identifiers

PMID38030974
PMCPMC10685687
OpenAlexW4389145686

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.