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 87 Citations 23,512 268 World Ranking 1420 National Ranking 588

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Gene
  • Amino acid

His main research concerns Myoglobin, Stereochemistry, Heme, Histidine and Ligand. His Myoglobin research is multidisciplinary, relying on both Crystallography, Hemin, Ligand, Hydrogen bond and Hemeprotein. John S. Olson integrates many fields in his works, including Stereochemistry and Side chain.

The various areas that he examines in his Heme study include Hemoglobin, Reaction rate constant and Carbon monoxide. His research in Histidine tackles topics such as Oxygen binding which are related to areas like Hydrogen peroxide and Peroxide. The Ligand study combines topics in areas such as Amino acid, Ligand binding assay, Molecular dynamics, Steric effects and Binding site.

His most cited work include:

  • Watching a Protein as it Functions with 150-ps Time-Resolved X-ray Crystallography (619 citations)
  • Mechanisms of Ligand Recognition in Myoglobin (566 citations)
  • Mechanism of NO-Induced Oxidation of Myoglobin and Hemoglobin† (528 citations)

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

John S. Olson spends much of his time researching Stereochemistry, Heme, Hemoglobin, Myoglobin and Biochemistry. His Stereochemistry research is multidisciplinary, incorporating elements of Reaction rate constant, Histidine, Hydrogen bond and Ligand. John S. Olson has researched Heme in several fields, including Carbon monoxide, Plasma protein binding and Binding site.

His research investigates the connection with Hemoglobin and areas like Oxygen which intersect with concerns in Analytical chemistry. The study incorporates disciplines such as Crystallography, Steric effects, Ligand and Hemeprotein in addition to Myoglobin. His study on Mutant, Recombinant DNA and Escherichia coli is often connected to Cerebratulus lacteus as part of broader study in Biochemistry.

He most often published in these fields:

  • Stereochemistry (46.48%)
  • Heme (41.90%)
  • Hemoglobin (39.44%)

What were the highlights of his more recent work (between 2010-2020)?

  • Hemoglobin (39.44%)
  • Heme (41.90%)
  • Stereochemistry (46.48%)

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

John S. Olson mainly investigates Hemoglobin, Heme, Stereochemistry, Biochemistry and Hemin. His studies deal with areas such as Ferric, Biophysics, Protein subunit and Plasma protein binding as well as Hemoglobin. His work carried out in the field of Heme brings together such families of science as Myoglobin, Recombinant DNA, Autoxidation, Methemoglobin and Globin.

John S. Olson merges many fields, such as Myoglobin and Side chain, in his writings. John S. Olson interconnects Oxygen binding, Ligand, Protein structure, Redox and Binding site in the investigation of issues within Stereochemistry. In general Biochemistry, his work in Mutant, Escherichia coli, Methionine and Extracellular is often linked to Platelet adhesiveness linking many areas of study.

Between 2010 and 2020, his most popular works were:

  • Fixed target matrix for femtosecond time-resolved and in situ serial micro-crystallography. (82 citations)
  • A "sliding scale rule" for selectivity among NO, CO, and O₂ by heme protein sensors. (68 citations)
  • Development of Recombinant Hemoglobin-Based Oxygen Carriers (65 citations)

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

  • Enzyme
  • Gene
  • Amino acid

His primary areas of investigation include Stereochemistry, Heme, Hemoglobin, Oxygen binding and Ligand. His Stereochemistry research incorporates elements of Hemeprotein and Binding site. His Heme research is mostly focused on the topic Hemin.

His Hemoglobin study introduces a deeper knowledge of Biochemistry. His work deals with themes such as Protein structure, Ligand and Ligand Binding Protein, which intersect with Oxygen binding. His study in Ligand is interdisciplinary in nature, drawing from both Active site, Myoglobin and Histidine.

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

Watching a Protein as it Functions with 150-ps Time-Resolved X-ray Crystallography

Friedrich Schotte;Manho Lim;Timothy Albert Jackson;Aleksandr V. Smirnov.
Science (2003)

917 Citations

Mechanisms of Ligand Recognition in Myoglobin

Barry A. Springer;Stephen G. Sligar;John S. Olson;George N. Jr. Phillips.
Chemical Reviews (1994)

892 Citations

Mechanism of NO-Induced Oxidation of Myoglobin and Hemoglobin†

Raymund F. Eich;Tiansheng Li;Douglas D. Lemon;Daniel H. Doherty.
Biochemistry (1996)

739 Citations

Rate of reaction with nitric oxide determines the hypertensive effect of cell-free hemoglobin

Daniel H. Doherty;Michael P. Doyle;Shawn R. Curry;Rita J. Vali.
Nature Biotechnology (1998)

485 Citations

The mechanism of autooxidation of myoglobin.

R E Brantley;S J Smerdon;A J Wilkinson;E W Singleton.
Journal of Biological Chemistry (1993)

467 Citations

High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin.

Michael L. Quillin;Robert M. Arduini;John S. Olson;George N. Phillips.
Journal of Molecular Biology (1994)

465 Citations

Structural Determinants of the Stretching Frequency of CO Bound to Myoglobin

Tiansheng Li;Michael L. Quillin;George N. Phillips;John S. Olson.
Biochemistry (1994)

410 Citations

The Mechanism of Action of Xanthine Oxidase

John S. Olson;David P. Ballou;Graham Palmer;Vincent Massey.
Journal of Biological Chemistry (1974)

409 Citations

Mapping the pathways for O2 entry into and exit from myoglobin.

Emily E. Scott;Quentin H. Gibson;John S. Olson.
Journal of Biological Chemistry (2001)

402 Citations

Kinetic Pathways and Barriers for Ligand Binding to Myoglobin

John S. Olson;George N. Phillips.
Journal of Biological Chemistry (1996)

371 Citations

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