What is he best known for?
The fields of study he is best known for:
His primary areas of study are Biochemistry, Transfer RNA, Aminoacyl tRNA synthetase, Aminoacylation and Amino acid.
His Transfer RNA study combines topics in areas such as Genetic code, Stereochemistry and Protein biosynthesis.
His biological study spans a wide range of topics, including Translation and Angiogenesis.
His Aminoacyl tRNA synthetase research is multidisciplinary, relying on both Restriction map, Amino Acyl-tRNA Synthetases, Protein secondary structure, Protein structure and Transfer RNA Aminoacylation.
His Aminoacylation research is multidisciplinary, incorporating perspectives in Base pair and Alanine.
His work deals with themes such as Computational biology and Nucleotide, which intersect with RNA.
His most cited work include:
- Biophysical Chemistry: Part II: Techniques for the Study of Biological Structure and Function (842 citations)
- Chimeric peptides for neuropeptide delivery through the blood-brain barrier. (567 citations)
- Biophysical chemistry. Part III, The behavior of biologicalmacromolecules (491 citations)
What are the main themes of his work throughout his whole career to date?
Paul Schimmel mainly investigates Transfer RNA, Biochemistry, Amino acid, Aminoacylation and Aminoacyl tRNA synthetase.
Paul Schimmel usually deals with Transfer RNA and limits it to topics linked to Stereochemistry and Binding site.
His work on Biochemistry deals in particular with Enzyme, Peptide sequence, Escherichia coli, Gene and Protein biosynthesis.
His Amino acid research incorporates themes from Protein structure, RNA editing, Amino acid activation and Active site.
Paul Schimmel interconnects Alanine, Alanine—tRNA ligase, T arm and Nucleotide in the investigation of issues within Aminoacylation.
Many of his studies involve connections with topics such as Amino Acyl-tRNA Synthetases and Aminoacyl tRNA synthetase.
He most often published in these fields:
- Transfer RNA (59.85%)
- Biochemistry (58.75%)
- Amino acid (27.62%)
What were the highlights of his more recent work (between 2006-2021)?
- Transfer RNA (59.85%)
- Biochemistry (58.75%)
- Aminoacyl tRNA synthetase (25.78%)
In recent papers he was focusing on the following fields of study:
Paul Schimmel focuses on Transfer RNA, Biochemistry, Aminoacyl tRNA synthetase, Genetics and Aminoacylation.
He combines subjects such as Amino acid, Genetic code, Translation and Protein biosynthesis with his study of Transfer RNA.
His Genetic code study combines topics from a wide range of disciplines, such as Evolutionary biology, Base pair and Transfer RNA Aminoacylation.
His Biochemistry study frequently draws connections to adjacent fields such as Cell biology.
The Aminoacyl tRNA synthetase study combines topics in areas such as Myositis, Enzyme, Amino acid activation, Computational biology and splice.
In his research on the topic of Aminoacylation, Adenylate kinase and Scaffold protein is strongly related with Microphthalmia-associated transcription factor.
Between 2006 and 2021, his most popular works were:
- Aminoacyl tRNA synthetases and their connections to disease (323 citations)
- Ribosome stalling induced by mutation of a CNS-specific tRNA causes neurodegeneration (244 citations)
- New functions of aminoacyl-tRNA synthetases beyond translation (242 citations)
In his most recent research, the most cited papers focused on:
Paul Schimmel mainly focuses on Transfer RNA, Biochemistry, Genetics, Aminoacyl tRNA synthetase and Aminoacylation.
The various areas that he examines in his Transfer RNA study include Amino acid, Genetic code and Protein biosynthesis.
His research investigates the connection with Genetic code and areas like Transfer RNA Aminoacylation which intersect with concerns in Wobble base pair, Base pair and TRNA aminoacylation.
His research in Protein biosynthesis focuses on subjects like Translation, which are connected to RNA.
His study brings together the fields of Stereochemistry and Biochemistry.
His Aminoacyl tRNA synthetase study combines topics in areas such as DNA ligase and Enzyme.
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