D-Index & Metrics Best Publications

D-Index & Metrics D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines.

Discipline name D-index D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines. Citations Publications World Ranking National Ranking
Chemistry D-index 62 Citations 9,951 222 World Ranking 5858 National Ranking 347

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Gene
  • Amino acid

The scientist’s investigation covers issues in Stereochemistry, Biochemistry, Cytochrome P450, Active site and Oxidoreductase. His work deals with themes such as Biocatalysis, Chemical physics, Catalysis, Substrate and Electron transfer, which intersect with Stereochemistry. His study in the fields of Enzyme, Cofactor and Mutagenesis under the domain of Biochemistry overlaps with other disciplines such as PARG and Dehalobacter.

His Cytochrome P450 research is multidisciplinary, incorporating elements of Protein structure, Mycobacterium tuberculosis, Binding site and Heme. The Active site study combines topics in areas such as Steady state, Fatty-acid peroxygenase and Hydroxylation. His work carried out in the field of Oxidoreductase brings together such families of science as Dicoumarol, NADH Dehydrogenase, NAD+ kinase and Coumarin.

His most cited work include:

  • P450 BM3: the very model of a modern flavocytochrome. (323 citations)
  • Atomic description of an enzyme reaction dominated by proton tunneling (236 citations)
  • The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase. (213 citations)

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

David Leys mainly focuses on Stereochemistry, Biochemistry, Enzyme, Cofactor and Oxidoreductase. His studies deal with areas such as Crystal structure, Heme, Active site, Substrate and Flavin group as well as Stereochemistry. David Leys has researched Active site in several fields, including Lyase and Binding site.

His Enzyme research includes themes of Mutagenesis, Mutant and Escherichia coli. His research investigates the connection with Cofactor and areas like Carboxylation which intersect with concerns in Biocatalysis. He has included themes like Halogenation and Fumarate reductase in his Oxidoreductase study.

He most often published in these fields:

  • Stereochemistry (52.14%)
  • Biochemistry (30.77%)
  • Enzyme (24.36%)

What were the highlights of his more recent work (between 2015-2021)?

  • Stereochemistry (52.14%)
  • Cofactor (17.95%)
  • Enzyme (24.36%)

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

His scientific interests lie mostly in Stereochemistry, Cofactor, Enzyme, Flavin group and Biochemistry. His Stereochemistry study combines topics from a wide range of disciplines, such as Oxidoreductase, Carboxylation, Active site, Decarboxylation and Substrate. His biological study spans a wide range of topics, including Lyase, Carboxylic acid and Electron transfer.

Reduction Activity, Sequence, Nonribosomal peptide, Docking and Adenylylation is closely connected to Aldehyde in his research, which is encompassed under the umbrella topic of Enzyme. His Flavin group research is multidisciplinary, relying on both Hydrolase, Isomerization and Prenylation, Prenyltransferase. His Cytochrome P450 study incorporates themes from Imidazole and Mycobacterium tuberculosis.

Between 2015 and 2021, his most popular works were:

  • Structures of carboxylic acid reductase reveal domain dynamics underlying catalysis. (61 citations)
  • P450-Catalyzed Regio- and Diastereoselective Steroid Hydroxylation: Efficient Directed Evolution Enabled by Mutability Landscaping (49 citations)
  • The UbiX-UbiD system: The biosynthesis and use of prenylated flavin (prFMN). (44 citations)

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

  • Enzyme
  • Gene
  • Amino acid

Stereochemistry, Cofactor, Enzyme, Biocatalysis and Active site are his primary areas of study. His studies in Stereochemistry integrate themes in fields like Oxidoreductase, Decarboxylation, Substrate, Flavin group and Prenyltransferase. His Cofactor study necessitates a more in-depth grasp of Biochemistry.

His work on Flavin mononucleotide, Binding site and Monoterpene as part of general Biochemistry research is often related to Streptomyces clavuligerus and Linalool, thus linking different fields of science. The concepts of his Enzyme study are interwoven with issues in Photosynthesis, Docking and Aldehyde. His Active site research incorporates themes from Combinatorial chemistry and Fragment-based lead discovery.

This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.

Best Publications

P450 BM3: the very model of a modern flavocytochrome.

Andrew W Munro;David G Leys;Kirsty J McLean;Ker R Marshall.
Trends in Biochemical Sciences (2002)

482 Citations

Atomic description of an enzyme reaction dominated by proton tunneling

Laura Masgrau;Anna Roujeinikova;Linus O. Johannissen;Parvinder Hothi.
Science (2006)

377 Citations

The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase.

Dea Slade;Mark S. Dunstan;Eva Barkauskaite;Ria Weston.
Nature (2011)

337 Citations

Overview of organohalide-respiring bacteria and a proposal for a classification system for reductive dehalogenases

Laura A. Hug;Farai Maphosa;David Leys;Frank E. Löffler;Frank E. Löffler.
Philosophical Transactions of the Royal Society B (2013)

271 Citations

Reductive dehalogenase structure suggests a mechanism for B12-dependent dehalogenation

Karl A. P. Payne;Carolina P. Quezada;Karl Fisher;Mark S. Dunstan.
Nature (2014)

240 Citations

Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1.

David Leys;Alexandre S. Tsapin;Kenneth H. Nealson;Terrance E. Meyer.
Nature Structural & Molecular Biology (1999)

184 Citations

New cofactor supports α,β-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition

Karl A. P. Payne;Mark D. White;Karl Fisher;Basile Khara.
Nature (2015)

183 Citations

Atomic structure of Mycobacterium tuberculosis CYP121 to 1.06 Å reveals novel features of cytochrome P450

David G Leys;Christopher G. Mowat;Kirsty J McLean;Alison Richmond.
Journal of Biological Chemistry (2003)

182 Citations

Reengineering orthogonally selective riboswitches

Neil Dixon;John N. Duncan;Torsten Geerlings;Mark S. Dunstan.
Proceedings of the National Academy of Sciences of the United States of America (2010)

173 Citations

UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis

Mark D. White;Karl A. P. Payne;Karl Fisher;Stephen A. Marshall.
Nature (2015)

163 Citations

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