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Michael A. McDonough

Michael A. McDonough

D-Index & Metrics

Chemistry

D-Index
57
Citations
13874
World Ranking
10969
National Ranking
623

Biology and Biochemistry

D-Index
58
Citations
13891
World Ranking
13065
National Ranking
1020

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Gene
  • Amino acid

His primary areas of study are Biochemistry, Transcription factor, Hydroxylation, Hypoxia-inducible factors and Enzyme. His study in Binding site, Oxygenase, Demethylase, Active site and Histone are all subfields of Biochemistry. His biological study spans a wide range of topics, including Nucleic acid, Stereochemistry and Small molecule.

His Transcription factor research incorporates elements of Oxidoreductase and Protein structure. The various areas that Michael A. McDonough examines in his Hydroxylation study include Hypoxia-Inducible Factor-Proline Dioxygenases, Hypoxia-Inducible Factor 1 and Ankyrin repeat. His Enzyme research is multidisciplinary, incorporating perspectives in Structure–activity relationship and Cephalosporin.

His most cited work include:

  • The Obesity-Associated FTO Gene Encodes a 2-Oxoglutarate–Dependent Nucleic Acid Demethylase (1095 citations)
  • The oncometabolite 2‐hydroxyglutarate inhibits histone lysine demethylases (655 citations)
  • Structural studies on 2-oxoglutarate oxygenases and related double-stranded β-helix fold proteins (329 citations)

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

His main research concerns Biochemistry, Stereochemistry, Oxygenase, Hydroxylation and Enzyme. His study in Biochemistry focuses on Binding site, Hypoxia-inducible factors, Transcription factor, Demethylase and Protein structure. His Stereochemistry research includes elements of Ligand, Hydrolase, Crystal structure, Active site and Carnitine biosynthesis.

His study looks at the relationship between Oxygenase and fields such as Small molecule, as well as how they intersect with chemical problems. His Hydroxylation research is multidisciplinary, relying on both Ribosomal protein, Asparagine, Substrate, Dioxygenase and Ankyrin repeat. His Enzyme study combines topics in areas such as Crystallography and Structure–activity relationship.

He most often published in these fields:

  • Biochemistry (55.63%)
  • Stereochemistry (40.40%)
  • Oxygenase (27.81%)

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

  • Stereochemistry (40.40%)
  • Biochemistry (55.63%)
  • Oxygenase (27.81%)

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

His primary scientific interests are in Stereochemistry, Biochemistry, Oxygenase, Active site and Enzyme. Michael A. McDonough combines subjects such as β lactamases, Ligand, Meropenem, Catalysis and Substrate with his study of Stereochemistry. Michael A. McDonough integrates Biochemistry and Toxoplasma gondii in his research.

He has researched Oxygenase in several fields, including Oxidoreductase, ASPH, Asparagine and Hydroxylation. His research integrates issues of Cofactor, Gene, Protein structure, Computational biology and Drug discovery in his study of Active site. His Enzyme research incorporates themes from Cell cycle and Gene expression.

Between 2016 and 2021, his most popular works were:

  • Cyclic Boronates Inhibit All Classes of β-Lactamases (60 citations)
  • NMR-filtered virtual screening leads to non-metal chelating metallo-β-lactamase inhibitors (35 citations)
  • Structural and stereoelectronic insights into oxygenase-catalyzed formation of ethylene from 2-oxoglutarate (26 citations)

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

  • Enzyme
  • Gene
  • Amino acid

Stereochemistry, Hydrolase, Enzyme, Active site and Meropenem are his primary areas of study. His Stereochemistry research is multidisciplinary, incorporating elements of Oxidoreductase, Oxygenase and β lactamases. The Hydrolase study which covers Serine that intersects with Antibiotic resistance, Bicyclic molecule and Transition state analog.

Biochemistry covers he research in Enzyme. His study in Active site is interdisciplinary in nature, drawing from both Protein structure, Combinatorial chemistry and Metal chelation. His Meropenem research includes themes of Crystallography, In vitro, Thiol and Isoquinoline.

Best Publications

  • The Obesity-Associated FTO Gene Encodes a 2-Oxoglutarate–Dependent Nucleic Acid Demethylase

    Thomas Gerken;Christophe A. Girard;Yi-Chun Loraine Tung;Celia J. Webby

  • The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases

    Rasheduzzaman Chowdhury;Kar Kheng Yeoh;Ya-Min Tian;Lars Hillringhaus

  • Structural studies on 2-oxoglutarate oxygenases and related double-stranded β-helix fold proteins

    Ian J. Clifton;Michael A. McDonough;Dominic Ehrismann;Nadia J. Kershaw

  • Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2).

    Michael A. McDonough;Vivian Li;Emily Flashman;Rasheduzzaman Chowdhury

  • Inhibition of 2-oxoglutarate dependent oxygenases

    Nathan R. Rose;Michael A. McDonough;Oliver N. F. King;Akane Kawamura

  • Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity.

    Stanley S. Ng;Kathryn L. Kavanagh;Michael A. McDonough;Danica Butler

  • Regulation of Jumonji-domain-containing histone demethylases by hypoxia-inducible factor (HIF)-1alpha.

    Patrick J. Pollard;Christoph Loenarz;David R. Mole;Michael A. McDonough

  • Posttranslational hydroxylation of ankyrin repeats in IκB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)

    Matthew E. Cockman;David E. Lancaster;Ineke P. Stolze;Kirsty S. Hewitson

  • Structural studies on human 2-oxoglutarate dependent oxygenases

    Michael A McDonough;Christoph Loenarz;Rasheduzzaman Chowdhury;Ian J Clifton

  • Structural and Mechanistic Studies on the Inhibition of the Hypoxia-inducible Transcription Factor Hydroxylases by Tricarboxylic Acid Cycle Intermediates

    Kirsty S. Hewitson;Benoit M. R. Liénard;Michael A. McDonough;Ian J. Clifton

  • Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates

    Jürgen Brem;Ricky Cain;Samuel Cahill;Michael A. McDonough

  • Inhibitor Scaffolds for 2-Oxoglutarate-Dependent Histone Lysine Demethylases.

    Nathan R Rose;Stanley S Ng;Jasmin Mecinović;Benoît M R Liénard

  • Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor

    Mathew L. Coleman;Michael A. McDonough;Kirsty S. Hewitson;Charlotte Coles

  • Structure of human RNA N6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation

    WeiShen Aik;John S. Scotti;Hwanho Choi;Lingzhi Gong

  • Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases

    Rasheduzzaman Chowdhury;Michael A. McDonough;Jasmin Mecinović;Christoph Loenarz

  • The enzymes of β-lactam biosynthesis

    Hamed Rb;Gomez-Castellanos;Henry L;Ducho C

  • Role of the jelly-roll fold in substrate binding by 2-oxoglutarate oxygenases.

    WeiShen Aik;Michael A McDonough;Armin Thalhammer;Rasheduzzaman Chowdhury

  • Structural Basis of Metallo-β-Lactamase Inhibition by Captopril Stereoisomers

    Jürgen Brem;Sander S. van Berkel;David Zollman;Sook Y. Lee

  • 5-Carboxy-8-hydroxyquinoline is a broad spectrum 2-oxoglutarate oxygenase inhibitor which causes iron translocation

    Richard J. Hopkinson;Anthony Tumber;Clarence Yapp;Rasheduzzaman Chowdhury

  • Selective inhibition of factor inhibiting hypoxia-inducible factor.

    Michael A McDonough;Luke A McNeill;Melanie Tilliet;Cyril A Papamicaël

  • Selective Inhibitors of the JMJD2 Histone Demethylases: Combined Nondenaturing Mass Spectrometric Screening and Crystallographic Approaches

    Nathan R. Rose;Esther C. Y. Woon;Guy L. Kingham;Oliver N. F. King

Frequent Co-Authors

Christopher J. Schofield
Christopher J. Schofield University of Oxford
Udo Oppermann
Udo Oppermann University of Oxford
Timothy D. W. Claridge
Timothy D. W. Claridge University of Oxford
Peter J. Ratcliffe
Peter J. Ratcliffe The Francis Crick Institute
Aled M. Edwards
Aled M. Edwards Structural Genomics Consortium
Cheryl H. Arrowsmith
Cheryl H. Arrowsmith Structural Genomics Consortium
Benedikt M. Kessler
Benedikt M. Kessler University of Oxford
Elspeth F. Garman
Elspeth F. Garman University of Oxford
Edith Sim
Edith Sim University of Oxford
Neil J. Oldham
Neil J. Oldham University of Nottingham

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