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 61 Citations 14,899 126 World Ranking 5918 National Ranking 195

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Gene
  • Amino acid

His main research concerns Active site, Hydrogenase, Crystallography, Protein structure and Stereochemistry. His Active site research integrates issues from Ether and Ethylene glycol. His Hydrogenase research is multidisciplinary, incorporating perspectives in Inorganic chemistry and Photochemistry.

In general Crystallography, his work in Crystal structure and Resolution is often linked to Moorella thermoacetica linking many areas of study. Juan C. Fontecilla-Camps has researched Protein structure in several fields, including Plasma protein binding, Complementarity determining region, Immunology, Molecule and Binding site. His Stereochemistry study combines topics in areas such as Biochemistry, Enzyme, Carboxydothermus hydrogenoformans, Carbon monoxide dehydrogenase and Scorpion Venoms.

His most cited work include:

  • Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center. (1058 citations)
  • Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. (554 citations)
  • A novel FeS cluster in Fe-only hydrogenases. (337 citations)

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

His scientific interests lie mostly in Stereochemistry, Crystallography, Active site, Biochemistry and Hydrogenase. Juan C. Fontecilla-Camps combines subjects such as Androctonus australis, Crystal structure, Molecule, Substrate and Protein structure with his study of Stereochemistry. The Protein structure study which covers Binding site that intersects with Peptide sequence.

His study in the fields of Resolution and Crystal under the domain of Crystallography overlaps with other disciplines such as Micelle. His Active site research includes themes of Carbon monoxide dehydrogenase and Nickel. His Hydrogenase research incorporates themes from Sulfur, Inorganic chemistry, Redox, Ligand and Photochemistry.

He most often published in these fields:

  • Stereochemistry (39.07%)
  • Crystallography (27.81%)
  • Active site (22.52%)

What were the highlights of his more recent work (between 2013-2021)?

  • Stereochemistry (39.07%)
  • Active site (22.52%)
  • Cofactor (8.61%)

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

His primary areas of study are Stereochemistry, Active site, Cofactor, Tryptophan and Biochemistry. The various areas that Juan C. Fontecilla-Camps examines in his Stereochemistry study include Tyrosine, Lyase, Metal, Substrate and Protein structure. As a part of the same scientific study, he usually deals with the Protein structure, concentrating on Mutagenesis and frequently concerns with Crystal structure and Hydrogenase.

Hydrogenase is closely attributed to Redox in his study. Juan C. Fontecilla-Camps connects Active site with Electron paramagnetic resonance in his study. His work is dedicated to discovering how Mutant, Hydrogen bond are connected with Enzyme and other disciplines.

Between 2013 and 2021, his most popular works were:

  • Crystal Structure of Tryptophan Lyase (NosL): Evidence for Radical Formation at the Amino Group of Tryptophan. (58 citations)
  • Crystallographic Studies of [Nife]-Hydrogenase Mutants: Towards Consensus Structures for the Elusive Unready Oxidized States. (40 citations)
  • Crystallographic Studies of [Nife]-Hydrogenase Mutants: Towards Consensus Structures for the Elusive Unready Oxidized States. (40 citations)

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

  • Enzyme
  • Gene
  • Amino acid

Juan C. Fontecilla-Camps spends much of his time researching Ligand, Stereochemistry, Lyase, Tryptophan and Peroxide. His study in Ligand is interdisciplinary in nature, drawing from both Formate, Moiety, Medicinal chemistry and Rhodium. He performs multidisciplinary study in Stereochemistry and Nosiheptide in his work.

His Lyase study combines topics from a wide range of disciplines, such as Hydrogen bond, Mutant and Aromatic amino acids. His Peroxide research integrates issues from Fourier transform infrared spectroscopy, Crystallography, Hydroxide and Sulfenic acid. His work deals with themes such as Tyrosine, Active site, Indole test, Photochemistry and Substrate, which intersect with Radical.

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

Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center.

Yvain Nicolet;Claudine Piras;Pierre Legrand;Claude E Hatchikian.
Structure (1999)

1555 Citations

Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products.

Yvain Nicolet;Oksana Lockridge;Patrick Masson;Juan C. Fontecilla-Camps.
Journal of Biological Chemistry (2003)

810 Citations

A novel FeS cluster in Fe-only hydrogenases.

Yvain Nicolet;Brian J Lemon;Juan C Fontecilla-Camps;John W Peters.
Trends in Biochemical Sciences (2000)

504 Citations

Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase.

Claudine Darnault;Anne Volbeda;Eun Jin Kim;Pierre Legrand.
Nature Structural & Molecular Biology (2003)

474 Citations

Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics.

Yaël Montet;Patricia Amara;Anne Volbeda;Xavier Vernede.
Nature Structural & Molecular Biology (1997)

452 Citations

The Crystal Structure of the Globular Head of Complement Protein C1q Provides a Basis for Its Versatile Recognition Properties

Christine Gaboriaud;Jordi Juanhuix;Arnaud Gruez;Monique Lacroix.
Journal of Biological Chemistry (2003)

446 Citations

Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases

Anne Volbeda;Lydie Martin;Christine Cavazza;Michaël Matho.
Journal of Biological Inorganic Chemistry (2005)

392 Citations

Crystal structure of a T cell receptor bound to an allogeneic MHC molecule

Jean-Baptiste Reiser;Claudine Darnault;Annick Guimezanes;Claude Grégoire.
Nature Immunology (2000)

296 Citations

A T Cell Receptor CDR3β Loop Undergoes Conformational Changes of Unprecedented Magnitude Upon Binding to a Peptide/MHC Class I Complex

Jean Baptiste Reiser;Claude Grégoire;Claudine Darnault;Thomas Mosser.
Immunity (2002)

285 Citations

The structure of a complex of human 17β-hydroxysteroid dehydrogenase with estradiol and NADP+ identifies two principal targets for the design of inhibitors

Rock Breton;Dominique Housset;Catherine Mazza;Juan Carlos Fontecilla-Camps.
Structure (1996)

284 Citations

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