A role of Gln596 in fine-tuning mammalian ALOX15 specificity, protein stability and allosteric properties-Reference-Cited by-同舟云学术

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A role of Gln596 in fine-tuning mammalian ALOX15 specificity, protein stability and allosteric properties

Published:2020-07 Issue:7 Volume:1865 Page:158680
ISSN:1388-1981
Container-title:Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids

Author:

Cruz Alejandro,Di Venere Almerinda,Mei Giampiero,Zhuravlev Alexander,Golovanov Alexey,Stehling Sabine,Heydeck Dagmar,Lluch José M.,González-Lafont Àngels,Kuhn Hartmut,Ivanov Igor

Funder

Deutsche Forschungsgemeinschaft

Russian Foundation for Basic Research

Alexander von Humboldt Foundation

Ministerio de Ciencia, Innovación y Universidades

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference48 articles.

1. Positional specificity of a reticulocyte lipoxygenase. Conversion of arachidonic acid to 15-S-hydroperoxy-eicosatetraenoic acid;Bryant;J. Biol. Chem.,1982

2. On singular or dual positional specificity of lipoxygenases. The number of chiral products varies with alignment of methylene groups at the active site of the enzyme;Kuhn;J. Biol. Chem.,1990

3. Molecular cloning and primary structure of human 15-lipoxygenase;Sigal;Biochem. Biophys. Res. Commun.,1988

4. Overexpression, purification and characterization of human recombinant 15-lipoxygenase;Kuhn;Biochim. Biophys. Acta,1993

5. Leukotriene signaling in the extinct human subspecies Homo denisovan and Homo neanderthalensis. Structural and functional comparison with Homo sapiens;Adel;Arch. Biochem. Biophys.,2015

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1. Development of novel ALOX15 inhibitors combining dual machine learning filtering and fragment substitution optimisation approaches, molecular docking and dynamic simulation methods;Journal of Enzyme Inhibition and Medicinal Chemistry;2024-01-12

2. Different Structures—Similar Effect: Do Substituted 5-(4-Methoxyphenyl)-1H-indoles and 5-(4-Methoxyphenyl)-1H-imidazoles Represent a Common Pharmacophore for Substrate Selective Inhibition of Linoleate Oxygenase Activity of ALOX15?;Molecules;2023-07-14

3. Identification of Novel Arachidonic Acid 15-Lipoxygenase Inhibitors Based on the Bayesian Classifier Model and Computer-Aided High-Throughput Virtual Screening;Pharmaceuticals;2022-11-20

4. N-Substituted 5-(1H-Indol-2-yl)-2-methoxyanilines Are Allosteric Inhibitors of the Linoleate Oxygenase Activity of Selected Mammalian ALOX15 Orthologs: Mechanism of Action;Journal of Medicinal Chemistry;2022-01-25

5. Functionalized Homologues and Positional Isomers of Rabbit 15-Lipoxygenase RS75091 Inhibitor;Medicinal Chemistry;2021-06-04

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