World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
84
Citations
21863
World Ranking
3378
National Ranking
258

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Gene
  • Amino acid

His scientific interests lie mostly in Biochemistry, Lipoxygenase, Enzyme, Cell biology and Phospholipid-hydroperoxide glutathione peroxidase. His study in Arachidonic acid, Metabolism, Low-density lipoprotein, Amino acid and Fatty acid is done as part of Biochemistry. The concepts of his Lipoxygenase study are interwoven with issues in Linoleic acid, Lipid peroxidation, Oxidative phosphorylation, Substrate and Isozyme.

His Enzyme study integrates concerns from other disciplines, such as Protein structure, Structural biology, Cholesterol and Complementary DNA. His research in Cell biology intersects with topics in Regulation of gene expression, Transdifferentiation, Granulocyte macrophage colony-stimulating factor and Gene isoform. His work deals with themes such as GPX4, GPX3, Hippocampus and GPX1, which intersect with Phospholipid-hydroperoxide glutathione peroxidase.

His most cited work include:

  • Specific inflammatory cytokines regulate the expression of human monocyte 15-lipoxygenase (329 citations)
  • Inflammation and immune regulation by 12/15-lipoxygenases. (305 citations)
  • Mammalian lipoxygenases and their biological relevance. (255 citations)

What are the main themes of his work throughout his whole career to date?

His primary areas of study are Biochemistry, Lipoxygenase, Enzyme, Arachidonic acid and Stereochemistry. His study in Biochemistry concentrates on Amino acid, Active site, ALOX15, Metabolism and Membrane. His Lipoxygenase research is multidisciplinary, relying on both Linoleic acid, Fatty acid, Reticulocyte, Chromatography and Substrate.

His work carried out in the field of Enzyme brings together such families of science as Structural biology and Gene, Mutant. His Stereochemistry research incorporates elements of Hydrogen atom abstraction, Mutagenesis, Catalysis and Ebselen. His research investigates the link between Regulation of gene expression and topics such as Cell biology that cross with problems in Molecular biology.

He most often published in these fields:

  • Biochemistry (53.14%)
  • Lipoxygenase (52.72%)
  • Enzyme (30.96%)

What were the highlights of his more recent work (between 2016-2021)?

  • Biochemistry (53.14%)
  • Lipoxygenase (52.72%)
  • Enzyme (30.96%)

In recent papers he was focusing on the following fields of study:

Hartmut Kühn focuses on Biochemistry, Lipoxygenase, Enzyme, Arachidonic acid and ALOX15. The Lipoxygenase study combines topics in areas such as Inflammation, Mutant, Pseudomonas aeruginosa, Zebrafish and Oxygenation. Hartmut Kühn combines subjects such as Amino acid, Lipid oxidation, Catalysis and Molecular mechanics with his study of Enzyme.

His Arachidonic acid research includes themes of Lipid signaling, Linoleic acid, Fatty acid, Eicosapentaenoic acid and ALOX15B. His work in Linoleic acid covers topics such as Mutagenesis which are related to areas like Stereochemistry. His studies in ALOX15 integrate themes in fields like Genome, Colitis, Pharmacology and Polyunsaturated fatty acid.

Between 2016 and 2021, his most popular works were:

  • Mammalian ALOX15 orthologs exhibit pronounced dual positional specificity with docosahexaenoic acid. (32 citations)
  • The crystal structure of Pseudomonas aeruginosa lipoxygenase Ala420Gly mutant explains the improved oxygen affinity and the altered reaction specificity. (14 citations)
  • The evolutionary hypothesis of reaction specificity of mammalian ALOX15 orthologs. (13 citations)

In his most recent research, the most cited papers focused on:

  • Enzyme
  • Gene
  • Amino acid

His main research concerns ALOX15, Biochemistry, Enzyme, Arachidonic acid and Lipoxygenase. His ALOX15 research is multidisciplinary, incorporating elements of Lipid oxidation, Cancer research, Tight junction and Colitis. His study in Seleninic acid extends to Biochemistry with its themes.

His Enzyme study integrates concerns from other disciplines, such as Genome, Gene, Evolution of mammals, Catalysis and Mutagenesis. Hartmut Kühn interconnects A549 cell and Fatty acid in the investigation of issues within Arachidonic acid. Hartmut Kühn performs multidisciplinary studies into Lipoxygenase and Ketogenic diet in his work.

Best Publications

  • Expanding expression of the 5-lipoxygenase pathway within the arterial wall during human atherogenesis

    Rainer Spanbroek;Rolf Gräbner;Katharina Lötzer;Markus Hildner

  • Mammalian lipoxygenases and their biological relevance.

    Hartmut Kuhn;Swathi Banthiya;Klaus van Leyen

  • Specific inflammatory cytokines regulate the expression of human monocyte 15-lipoxygenase

    Douglas J. Conrad;Hartmut Kuhn;Mary Mulkins;Ella Highland

  • Inflammation and immune regulation by 12/15-lipoxygenases.

    Hartmut Kühn;Valerie B. O’Donnell

  • Molecular enzymology of lipoxygenases.

    Igor Ivanov;Dagmar Heydeck;Katharina Hofheinz;Jana Roffeis

  • Regulation of enzymatic lipid peroxidation: the interplay of peroxidizing and peroxide reducing enzymes.

    Hartmut Kühn;Astrid Borchert

  • Oxygenation of biological membranes by the pure reticulocyte lipoxygenase.

    H Kuhn;J Belkner;R Wiesner;A R Brash

  • Mammalian arachidonate 15-lipoxygenases structure, function, and biological implications.

    Hartmut Kuhn;Matthias Walther;Ralf Jürgen Kuban

  • MACROPHAGE-MEDIATED 15-LIPOXYGENASE EXPRESSION PROTECTS AGAINST ATHEROSCLEROSIS DEVELOPMENT

    Jianhe Shen;Ed Herderick;J. Fredrick Cornhill;Eva M Zsigmond

  • The Selenoenzyme Phospholipid Hydroperoxide Glutathione Peroxidase Controls the Activity of the 15-Lipoxygenase with Complex Substrates and Preserves the Specificity of the Oxygenation Products

    Kerstin Schnurr;Jutta Belkner;Fulvio Ursini;Tankred Schewe

  • Expression of a Flax Allene Oxide Synthase cDNA Leads to Increased Endogenous Jasmonic Acid (JA) Levels in Transgenic Potato Plants but Not to a Corresponding Activation of JA-Responding Genes.

    Karsten Harms;Rainer Atzorn;Alan Brash;Hartmut Kuhn

  • In vivo action of 15-lipoxygenase in early stages of human atherogenesis.

    Hartmut Kühn;Dagmar Heydeck;Isabelle Hugou;Christina Gniwotta

  • Oxygenation of lipoproteins by mammalian lipoxygenases

    Jutta Belkner;Rainer Wiesner;Jörg Rathman;Jim Barnett

  • Enzymology and physiology of reticulocyte lipoxygenase: comparison with other lipoxygenases.

    Tankred Schewe;Samuel M. Rapoport;Hartmut Kühn

  • Molecular dioxygen enters the active site of 12/15-lipoxygenase via dynamic oxygen access channels

    Jan Saam;Igor Ivanov;Matthias Walther;Hermann-Georg Holzhütter

  • Structural and functional biology of arachidonic acid 15-lipoxygenase-1 (ALOX15)

    Igor Ivanov;Hartmut Kuhn;Dagmar Heydeck

  • Conversion of cucumber linoleate 13-lipoxygenase to a 9-lipoxygenating species by site-directed mutagenesis

    Ellen Hornung;Matthias Walther;Hartmut Kühn;Ivo Feussner

  • Shape and Specificity in Mammalian 15-Lipoxygenase Active Site: THE FUNCTIONAL INTERPLAY OF SEQUENCE DETERMINANTS FOR THE REACTION SPECIFICITY *

    Sabine Borngräber;Sabine Borngräber;Michelle Browner;Sarah Gillmor;Christa Gerth

  • IL-4-induced oxidative stress upregulates VCAM-1 gene expression in human endothelial cells.

    Yong Woo Lee;Hartmut Kühn;Bernhard Hennig;Andrew S. Neish

  • Flavonoids of Cocoa Inhibit Recombinant Human 5-Lipoxygenase

    Tankred Schewe;Hartmut Kühn;Helmut Sies

Frequent Co-Authors

Thomas Kietzmann
Thomas Kietzmann University of Oulu
Valerie B. O'Donnell
Valerie B. O'Donnell Cardiff University
Ivo Feussner
Ivo Feussner University of Göttingen
Claus Wasternack
Claus Wasternack Leibniz Association
José M. Lluch
José M. Lluch Autonomous University of Barcelona
Alberico L. Catapano
Alberico L. Catapano University of Milan
Shozo Yamamoto
Shozo Yamamoto Kyoto Women's University
Alan R. Brash
Alan R. Brash Vanderbilt University
Dror Harats
Dror Harats Sheba Medical Center
Mauro Maccarrone
Mauro Maccarrone University of L'Aquila

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