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 50 Citations 6,664 190 World Ranking 10842 National Ranking 834
Biology and Biochemistry D-index 50 Citations 6,678 190 World Ranking 13357 National Ranking 953

Overview

What is she best known for?

The fields of study she is best known for:

  • Enzyme
  • Gene
  • Amino acid

Her primary areas of study are Biochemistry, Molybdenum cofactor, Molybdopterin, Rhodobacter and Cofactor. She focuses mostly in the field of Biochemistry, narrowing it down to matters related to Stereochemistry and, in some cases, Oxidoreductase and Active site. Her Molybdenum cofactor study integrates concerns from other disciplines, such as Amino acid, Molecular biology and Protein subunit.

Within one scientific family, Silke Leimkühler focuses on topics pertaining to Peptide sequence under Molybdopterin, and may sometimes address concerns connected to Cofactor binding, Molybdopterin synthase and Molecular mass. Her studies examine the connections between Rhodobacter and genetics, as well as such issues in NAD+ kinase, with regards to Formate dehydrogenase, Formate and Formate oxidation. Her work carried out in the field of Cofactor brings together such families of science as Nitrogen assimilation, Bacteria, Anaerobic respiration and Metalloprotein.

Her most cited work include:

  • Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus (148 citations)
  • A Sulfurtransferase Is Required in the Transfer of Cysteine Sulfur in the in Vitro Synthesis of Molybdopterin from Precursor Z in Escherichia coli (110 citations)
  • Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli. (107 citations)

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

Silke Leimkühler mainly investigates Biochemistry, Molybdenum cofactor, Cofactor, Molybdopterin and Enzyme. Her research related to Biosynthesis, Rhodobacter, Escherichia coli, Xanthine dehydrogenase and Aldehyde oxidase might be considered part of Biochemistry. The various areas that Silke Leimkühler examines in her Molybdenum cofactor study include Molybdenum, Sulfurtransferase, Protein subunit, Stereochemistry and Transfer RNA.

Her study looks at the relationship between Stereochemistry and topics such as Active site, which overlap with Substrate. Her research investigates the connection between Cofactor and topics such as Oxidoreductase that intersect with issues in Aldehyde and Redox. Silke Leimkühler has included themes like Cysteine, Nucleotide and Sulfite oxidase in her Molybdopterin study.

She most often published in these fields:

  • Biochemistry (55.96%)
  • Molybdenum cofactor (42.49%)
  • Cofactor (24.87%)

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

  • Biochemistry (55.96%)
  • Molybdenum cofactor (42.49%)
  • Enzyme (20.21%)

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

Her scientific interests lie mostly in Biochemistry, Molybdenum cofactor, Enzyme, Stereochemistry and Escherichia coli. Her study in Molybdenum cofactor is interdisciplinary in nature, drawing from both Transfer RNA, Xanthine dehydrogenase, Molybdopterin and Bacteria. Her Enzyme study combines topics from a wide range of disciplines, such as Amino acid and Metabolism.

Her Stereochemistry research is multidisciplinary, relying on both Molybdenum, Formate dehydrogenase, Cofactor, Pterin and Ligand. Her work deals with themes such as Rhodobacter, Cysteine and Guanine, which intersect with Cofactor. The Escherichia coli study combines topics in areas such as Plasma protein binding, Iron–sulfur cluster, Chaperone and Metabolic pathway.

Between 2015 and 2021, her most popular works were:

  • Bacterial molybdoenzymes: old enzymes for new purposes (65 citations)
  • Structure and function of mammalian aldehyde oxidases (50 citations)
  • The continuous oxidation of HMF to FDCA and the immobilisation and stabilisation of periplasmic aldehyde oxidase (PaoABC) (40 citations)

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

  • Enzyme
  • Gene
  • Amino acid

Silke Leimkühler mostly deals with Biochemistry, Enzyme, Cofactor, Molybdenum cofactor and Aldehyde oxidase. All of her Biochemistry and Amino acid, Biosynthesis, Oxidoreductase, Heme and Succinate dehydrogenase investigations are sub-components of the entire Biochemistry study. Her research integrates issues of Stereochemistry and Metabolism in her study of Enzyme.

While the research belongs to areas of Cofactor, Silke Leimkühler spends her time largely on the problem of Escherichia coli, intersecting her research to questions surrounding Mutant. Her study looks at the intersection of Molybdenum cofactor and topics like Transfer RNA with Molybdopterin. Silke Leimkühler combines subjects such as Furfural, Galactose oxidase, Drug metabolism, Isozyme and Superoxide with her study of Aldehyde oxidase.

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

Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus

James J Truglio;Karsten Theis;Silke Leimkühler;Roberto Rappa.
Structure (2002)

224 Citations

Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli.

Chantal Iobbi-Nivol;Silke Leimkühler.
Biochimica et Biophysica Acta (2013)

190 Citations

A Sulfurtransferase Is Required in the Transfer of Cysteine Sulfur in the in Vitro Synthesis of Molybdopterin from Precursor Z in Escherichia coli

Silke Leimkühler;K.V. Rajagopalan.
Journal of Biological Chemistry (2001)

169 Citations

Characterization of Escherichia coli MoeB and Its Involvement in the Activation of Molybdopterin Synthase for the Biosynthesis of the Molybdenum Cofactor

Silke Leimkühler;Margot M. Wuebbens;K.V. Rajagopalan.
Journal of Biological Chemistry (2001)

168 Citations

Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans.

Andreas Matthies;K. V. Rajagopalan;Ralf R. Mendel;Silke Leimkühler.
Proceedings of the National Academy of Sciences of the United States of America (2004)

163 Citations

The History of the Discovery of the Molybdenum Cofactor and Novel Aspects of its Biosynthesis in Bacteria

Silke Leimkühler;Margot M. Wuebbens;K.V. Rajagopalan.
Coordination Chemistry Reviews (2011)

160 Citations

Enzyme cascade reactions: synthesis of furandicarboxylic acid (FDCA) and carboxylic acids using oxidases in tandem

Shane M. McKenna;Silke Leimkühler;Susanne Herter;Nicholas J. Turner.
Green Chemistry (2015)

148 Citations

The oxygen-tolerant and NAD+-dependent formate dehydrogenase from Rhodobacter capsulatus is able to catalyze the reduction of CO2 to formate.

Tobias Hartmann;Silke Leimkühler.
FEBS Journal (2013)

137 Citations

A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis.

Zvonimir Marelja;Walter Stöcklein;Manfred Nimtz;Silke Leimkühler.
Journal of Biological Chemistry (2008)

136 Citations

Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulatus is more similar to its eukaryotic counterparts than to prokaryotic molybdenum enzymes.

Silke Leimkühler;Monika Kern;Peter S. Solomon;Alastair G. McEwan.
Molecular Microbiology (1998)

130 Citations

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