What is he best known for?
The fields of study he is best known for:
His main research concerns Stereochemistry, Biochemistry, Enzyme, Mandelate racemase and Enolase superfamily.
His Stereochemistry research includes themes of Cleavage, Catalysis, Active site, Isomerase and Phosphodiester bond.
His work deals with themes such as Genetics, Function, Operon and Protein superfamily, which intersect with Enzyme.
His Mandelate racemase study combines topics from a wide range of disciplines, such as Racemization and Homology.
His study in Enolase superfamily is interdisciplinary in nature, drawing from both Divergent evolution, Lysine racemase and Enzyme kinetics.
His Divergent evolution study incorporates themes from Protein sequencing and Computational biology.
His most cited work include:
- Divergent Evolution of Enzymatic Function: Mechanistically Diverse Superfamilies and Functionally Distinct Suprafamilies (430 citations)
- The Low Barrier Hydrogen Bond in Enzymatic Catalysis (402 citations)
- Enzyme Function Initiative-Enzyme Similarity Tool (EFI-EST): A web tool for generating protein sequence similarity networks. (332 citations)
What are the main themes of his work throughout his whole career to date?
His primary scientific interests are in Stereochemistry, Crystal structure, Biochemistry, Binding protein and Enzyme.
His Stereochemistry research incorporates elements of Orotidine, Catalysis, Active site, Substrate and Mandelate racemase.
His Active site research is multidisciplinary, incorporating elements of Protein structure and Lyase.
His Crystal structure research is multidisciplinary, incorporating perspectives in Glutathione S-transferase, Glutathione and Glutathione transferase.
All of his Biochemistry and Enolase superfamily, Escherichia coli, Pseudomonas putida, Isomerase and ATP synthase investigations are sub-components of the entire Biochemistry study.
He interconnects Mutant and Function in the investigation of issues within Enzyme.
He most often published in these fields:
- Stereochemistry (49.81%)
- Crystal structure (48.46%)
- Biochemistry (33.98%)
What were the highlights of his more recent work (between 2010-2021)?
- Crystal structure (48.46%)
- Stereochemistry (49.81%)
- Biochemistry (33.98%)
In recent papers he was focusing on the following fields of study:
John A. Gerlt spends much of his time researching Crystal structure, Stereochemistry, Biochemistry, Binding protein and Periplasmic space.
His biological study spans a wide range of topics, including Glutathione S-transferase, Glutathione, Glutathione transferase and Molecular biology.
His work in Stereochemistry addresses issues such as Substrate, which are connected to fields such as Orotidine.
In general Biochemistry study, his work on Enzyme and Enolase superfamily often relates to the realm of Mycobacterium smegmatis, thereby connecting several areas of interest.
Within one scientific family, John A. Gerlt focuses on topics pertaining to Transporter under Binding protein, and may sometimes address concerns connected to Carbohydrate.
His research on Periplasmic space frequently links to adjacent areas such as Glucuronate.
Between 2010 and 2021, his most popular works were:
- Enzyme Function Initiative-Enzyme Similarity Tool (EFI-EST): A web tool for generating protein sequence similarity networks. (332 citations)
- The Enzyme Function Initiative (128 citations)
- Roles of small laccases from Streptomyces in lignin degradation. (111 citations)
In his most recent research, the most cited papers focused on:
John A. Gerlt mostly deals with Crystal structure, Stereochemistry, Biochemistry, Binding protein and Enzyme.
In his work, Protein subunit is strongly intertwined with Glutathione, which is a subfield of Crystal structure.
His Stereochemistry research is multidisciplinary, relying on both Orotidine, Active site, Phosphate, Substrate and ATP synthase.
His Biochemistry study frequently intersects with other fields, such as Metabolomics.
His research in Enzyme focuses on subjects like Genome, which are connected to Protein family.
The various areas that John A. Gerlt examines in his Enolase superfamily study include Homology, Sugar acids, Dehydratase and Mandelate racemase.
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