World's Best Scientists 2026 revealed!
Michael A. McDonough

Michael A. McDonough

D-Index & Metrics

Biology and Biochemistry

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

Chemistry

D-Index
57
Citations
13874
World Ranking
10967
National Ranking
623

Michael A. McDonough publication distribution in Chemistry in 2026

The chart shows the distribution of publications by all Research.com ranked scientists in the field of Chemistry in 2026. The highlighted bar marks where Michael A. McDonough sits on this spectrum.

61–80 publications: 66 scientists 81–100 publications: 302 scientists 101–120 publications: 623 scientists 121–140 publications: 918 scientists 141–160 publications: 1,218 scientists 161–180 publications: 1,350 scientists 181–200 publications: 1,344 scientists 201–220 publications: 1,281 scientists 221–240 publications: 1,216 scientists 241–260 publications: 1,100 scientists 261–280 publications: 979 scientists 281–300 publications: 939 scientists 301–320 publications: 764 scientists 321–340 publications: 643 scientists 341–360 publications: 628 scientists 361–380 publications: 522 scientists 381–400 publications: 459 scientists 401–420 publications: 397 scientists 421–440 publications: 327 scientists 441–460 publications: 270 scientists 461–480 publications: 265 scientists 481–500 publications: 252 scientists 501–520 publications: 201 scientists 521–540 publications: 185 scientists 541–560 publications: 148 scientists 561–580 publications: 148 scientists 581–600 publications: 132 scientists 601–620 publications: 114 scientists 621–640 publications: 104 scientists 641–660 publications: 91 scientists 661–680 publications: 92 scientists 681–700 publications: 73 scientists 701–720 publications: 57 scientists 721–740 publications: 54 scientists 741–760 publications: 67 scientists 761–780 publications: 45 scientists 781–800 publications: 46 scientists 801–820 publications: 39 scientists 821–840 publications: 32 scientists 841–860 publications: 36 scientists 861–880 publications: 29 scientists 881–900 publications: 26 scientists 901–920 publications: 24 scientists 921–940 publications: 14 scientists 941–960 publications: 23 scientists 961–980 publications: 28 scientists 981–1,000 publications: 15 scientists 1,001–1,020 publications: 29 scientists 1,021–1,040 publications: 12 scientists 1,041–1,060 publications: 19 scientists 1,061–1,080 publications: 12 scientists 1,081–1,100 publications: 6 scientists 1,101–1,120 publications: 8 scientists 1,121–1,140 publications: 12 scientists 1,141–1,160 publications: 5 scientists 1,161–1,180 publications: 6 scientists 1,181–1,200 publications: 14 scientists 1,201–1,220 publications: 7 scientists 1,221–1,240 publications: 2 scientists 1,241–1,260 publications: 6 scientists 1,261–1,280 publications: 4 scientists 1,281–1,294 publications: 6 scientists 1,295+ publications: 100 scientists
61 publications 1,295+

This scientist: 301 publications — 63rd percentile

63% of scientists in this discipline score the same or lower.

The last bar groups every scientist with 1,295 publications or more.

Michael A. McDonough D-index placement in Chemistry in 2026

The chart shows the D-index (discipline H-index) distribution of Chemistry scientists ranked by Research.com in 2026. The highlighted bar marks where Michael A. McDonough sits on this spectrum.

40–41 D-Index: 289 scientists 42–43 D-Index: 612 scientists 44–45 D-Index: 808 scientists 46–47 D-Index: 776 scientists 48–49 D-Index: 835 scientists 50–51 D-Index: 861 scientists 52–53 D-Index: 872 scientists 54–55 D-Index: 933 scientists 56–57 D-Index: 1,051 scientists 58–59 D-Index: 930 scientists 60–61 D-Index: 882 scientists 62–63 D-Index: 834 scientists 64–65 D-Index: 731 scientists 66–67 D-Index: 775 scientists 68–69 D-Index: 683 scientists 70–71 D-Index: 646 scientists 72–73 D-Index: 561 scientists 74–75 D-Index: 501 scientists 76–77 D-Index: 437 scientists 78–79 D-Index: 388 scientists 80–81 D-Index: 354 scientists 82–83 D-Index: 292 scientists 84–85 D-Index: 275 scientists 86–87 D-Index: 254 scientists 88–89 D-Index: 235 scientists 90–91 D-Index: 185 scientists 92–93 D-Index: 192 scientists 94–95 D-Index: 155 scientists 96–97 D-Index: 163 scientists 98–99 D-Index: 125 scientists 100–101 D-Index: 105 scientists 102–103 D-Index: 105 scientists 104–105 D-Index: 112 scientists 106–107 D-Index: 88 scientists 108–109 D-Index: 68 scientists 110–111 D-Index: 69 scientists 112–113 D-Index: 65 scientists 114–115 D-Index: 79 scientists 116–117 D-Index: 61 scientists 118–119 D-Index: 44 scientists 120–121 D-Index: 37 scientists 122–123 D-Index: 40 scientists 124–125 D-Index: 33 scientists 126–127 D-Index: 26 scientists 128–129 D-Index: 34 scientists 130–131 D-Index: 35 scientists 132–133 D-Index: 25 scientists 134–135 D-Index: 27 scientists 136–137 D-Index: 17 scientists 138–139 D-Index: 16 scientists 140–141 D-Index: 20 scientists 142–143 D-Index: 20 scientists 144–145 D-Index: 15 scientists 146–147 D-Index: 9 scientists 148–149 D-Index: 9 scientists 150–151 D-Index: 16 scientists 152–153 D-Index: 11 scientists 154–155 D-Index: 9 scientists 156–157 D-Index: 3 scientists 158 D-Index: 3 scientists 159+ D-Index: 98 scientists
40 D-Index 159+

This scientist: 57 D-Index — 39th percentile

39% of scientists in this discipline score the same or lower.

The last bar groups every scientist with 159 D-Index or more.

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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