What is he best known for?
The fields of study he is best known for:
His scientific interests lie mostly in Biochemistry, Transfer RNA, Aminoacyl tRNA synthetase, Stereochemistry and Binding site.
Enzyme, Protein structure, Transcription and DNA are among the areas of Biochemistry where the researcher is concentrating his efforts.
His research combines Base pair and Transfer RNA.
His Aminoacyl tRNA synthetase research is multidisciplinary, incorporating perspectives in Amino acid, RNA editing, Amino Acyl-tRNA Synthetases and Protein biosynthesis.
The concepts of his Stereochemistry study are interwoven with issues in Trypsin, Active site, Substrate, Glutamine and Ribose.
His study in Binding site is interdisciplinary in nature, drawing from both Peptide sequence and Chymotrypsin.
His most cited work include:
- Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution (752 citations)
- Structural basis of substrate specificity in the serine proteases (709 citations)
- Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase. (306 citations)
What are the main themes of his work throughout his whole career to date?
John J. Perona mainly focuses on Biochemistry, Transfer RNA, Stereochemistry, Aminoacyl tRNA synthetase and Amino acid.
The Transfer RNA study which covers Nucleotide that intersects with Tyrosine—tRNA ligase.
The concepts of his Stereochemistry study are interwoven with issues in DNA, Active site, Substrate, Binding site and EcoRV.
His study looks at the relationship between Binding site and fields such as Base pair, as well as how they intersect with chemical problems.
His study on Aminoacyl tRNA synthetase also encompasses disciplines like
- Sequence alignment together with Nucleic acid structure,
- Leucine—tRNA ligase and related Leucyl-tRNA synthetase.
His study looks at the intersection of Amino acid and topics like TRNA aminoacylation with Glutamine binding and Glutamine.
He most often published in these fields:
- Biochemistry (83.19%)
- Transfer RNA (57.14%)
- Stereochemistry (38.66%)
What were the highlights of his more recent work (between 2010-2018)?
- Biochemistry (83.19%)
- Transfer RNA (57.14%)
- Aminoacylation (29.41%)
In recent papers he was focusing on the following fields of study:
The scientist’s investigation covers issues in Biochemistry, Transfer RNA, Aminoacylation, Amino acid and Aminoacyl tRNA synthetase.
His work in the fields of Biochemistry, such as Protein biosynthesis, Methanosarcina acetivorans and Enzyme, intersects with other areas such as Sulfide.
His research in Transfer RNA intersects with topics in Protein structure, Biophysics, Stereochemistry and Amino acid binding.
His biological study spans a wide range of topics, including Leucine—tRNA ligase and Leucyl-tRNA synthetase.
His work in Amino acid covers topics such as RNA editing which are related to areas like Isoleucine—tRNA ligase and Binding site.
His Aminoacyl tRNA synthetase research focuses on subjects like Amino Acyl-tRNA Synthetases, which are linked to Protein engineering.
Between 2010 and 2018, his most popular works were:
- Synthetic and Editing Mechanisms of Aminoacyl-tRNA Synthetases (92 citations)
- Synthetic and Editing Mechanisms of Aminoacyl-tRNA Synthetases (92 citations)
- Structural diversity and protein engineering of the aminoacyl-tRNA synthetases. (63 citations)
In his most recent research, the most cited papers focused on:
John J. Perona mainly investigates Biochemistry, Transfer RNA, Aminoacylation, Amino acid and Aminoacyl tRNA synthetase.
His study in Protein biosynthesis, Enzyme, Protein structure, Amino Acyl-tRNA Synthetases and TRNA binding falls under the purview of Biochemistry.
He has researched Protein biosynthesis in several fields, including Leucine—tRNA ligase, Stereochemistry and Leucyl-tRNA synthetase.
His work deals with themes such as Protein engineering and Genetic code, which intersect with Protein structure.
Amino Acyl-tRNA Synthetases is a subfield of RNA that John J. Perona investigates.
His Aminoacylation research is multidisciplinary, incorporating elements of Mutation, Nucleotide, Methanocaldococcus, Directed evolution and Tyrosine—tRNA ligase.
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