David W. Christianson

What is he best known for?

The fields of study he is best known for:

• Enzyme
• Gene
• Amino acid

His main research concerns Stereochemistry, Biochemistry, Active site, Protein structure and Hydrolase. His Stereochemistry research incorporates elements of Lyase, Cyclase, ATP synthase, Enzyme and Carbocation. He combines subjects such as Site-directed mutagenesis and Farnesyl diphosphate synthase with his study of Active site.

The Protein structure study combines topics in areas such as Metalloprotein, Structural biology, Biophysics and Histidine. The concepts of his Hydrolase study are interwoven with issues in Structure–activity relationship, Epoxide, Hydrogen bond, Acetyllysine and Binding site. His study looks at the relationship between Binding site and fields such as Molecule, as well as how they intersect with chemical problems.

His most cited work include:

• Structural biology and chemistry of the terpenoid cyclases. (527 citations)
• HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle (383 citations)
• Crystal structure of pentalenene synthase: Mechanistic insights on terpenoid cyclization reactions in biology (336 citations)

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

His primary areas of investigation include Stereochemistry, Active site, Biochemistry, Crystal structure and Arginase. His Stereochemistry study integrates concerns from other disciplines, such as Hydrolase, Lyase, Enzyme, Protein structure and Binding site. His Lyase study which covers Cyclase that intersects with Terpenoid.

In his research on the topic of Active site, Side chain is strongly related with Carbonic anhydrase II. His study in Crystal structure is interdisciplinary in nature, drawing from both Substrate, Danio and HDAC10. David W. Christianson has researched Arginase in several fields, including Nitric oxide synthase, Nitric oxide and Manganese.

He most often published in these fields:

• Stereochemistry (60.85%)
• Active site (26.76%)
• Biochemistry (26.20%)

What were the highlights of his more recent work (between 2017-2021)?

• Stereochemistry (60.85%)
• HDAC10 (6.48%)
• Crystal structure (23.94%)

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

His primary areas of investigation include Stereochemistry, HDAC10, Crystal structure, HDAC6 and Danio. His work deals with themes such as Cyclase, Catalysis, Active site, Molecule and Prenyltransferase, which intersect with Stereochemistry. David W. Christianson is investigating Active site as part of his Biochemistry and Enzyme and Active site study.

His HDAC6 study combines topics from a wide range of disciplines, such as Selectivity, Structure–activity relationship, Isozyme and Zebrafish. His Isozyme research includes elements of Protein structure and Epigenetics. His research investigates the connection between Danio and topics such as Cell biology that intersect with problems in Mutant.

Between 2017 and 2021, his most popular works were:

• Synthesis and Biological Investigation of Phenothiazine-Based Benzhydroxamic Acids as Selective Histone Deacetylase 6 Inhibitors (37 citations)
• Histone Deacetylase 6-Selective Inhibitors and the Influence of Capping Groups on Hydroxamate-Zinc Denticity (36 citations)
• Discovery of the First-in-Class Dual Histone Deacetylase-Proteasome Inhibitor. (29 citations)

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

• Enzyme
• Gene
• Amino acid

David W. Christianson spends much of his time researching HDAC6, Stereochemistry, Active site, Isozyme and Selectivity. His studies in Stereochemistry integrate themes in fields like Amino acid, Plasma protein binding, Hydrolase, HDAC10 and Protein structure. His Hydrolase study incorporates themes from Ketone, Binding site and Binding selectivity.

His research integrates issues of Carbocation, Lyase, Cyclase and Organic synthesis in his study of Protein structure. Active site connects with themes related to Stereospecificity in his study. His Isozyme research is under the purview of Biochemistry.