What is he best known for?
The fields of study he is best known for:
- Gene
- Amino acid
- Biochemistry
Campylobacter jejuni, Biochemistry, Glycosylation, Flagellin and Glycan are his primary areas of study.
His study explores the link between Campylobacter jejuni and topics such as Campylobacter that cross with problems in Mutant.
His work deals with themes such as Neuroprotection and Cell biology, which intersect with Biochemistry.
The study incorporates disciplines such as Peptide sequence and N-linked glycosylation in addition to Glycosylation.
His work in Flagellin tackles topics such as Flagellum which are related to areas like Motility, Bacterial adhesin, GroEL, GroES and Dehydratase.
His Glycan research is multidisciplinary, relying on both Archaellum and Proteomics.
His most cited work include:
- Structure of the N-Linked Glycan Present on Multiple Glycoproteins in the Gram-negative Bacterium, Campylobacter jejuni (360 citations)
- Identification of the Carbohydrate Moieties and Glycosylation Motifs in Campylobacter jejuni Flagellin (300 citations)
- Definition of the bacterial N-glycosylation site consensus sequence. (287 citations)
What are the main themes of his work throughout his whole career to date?
John F. Kelly mainly investigates Biochemistry, Glycan, Glycosylation, Flagellin and Microbiology.
His studies link Campylobacter jejuni with Biochemistry.
His study focuses on the intersection of Glycan and fields such as Pilin with connections in the field of Pilus assembly.
His research on Glycosylation often connects related areas such as Mutant.
His Flagellin study integrates concerns from other disciplines, such as Molecular biology, Flagellum and Borrelia burgdorferi.
He works mostly in the field of Microbiology, limiting it down to topics relating to Francisella tularensis and, in certain cases, Proteome and In vivo.
He most often published in these fields:
- Biochemistry (49.50%)
- Glycan (23.76%)
- Glycosylation (21.78%)
What were the highlights of his more recent work (between 2012-2021)?
- Biochemistry (49.50%)
- Glycan (23.76%)
- Antibody (9.90%)
In recent papers he was focusing on the following fields of study:
His primary areas of investigation include Biochemistry, Glycan, Antibody, Glycosylation and Methanococcus maripaludis.
The study incorporates disciplines such as Microbiology and Mass spectrometry in addition to Biochemistry.
His Glycan research includes themes of Peptide sequence and Chinese hamster ovary cell.
Many of his research projects under Antibody are closely connected to Disulfide Linkage and Molecular mass with Disulfide Linkage and Molecular mass, tying the diverse disciplines of science together.
His research integrates issues of Cell growth, Metabolic engineering, Recombinant DNA, HEK 293 cells and Metabolism in his study of Glycosylation.
The various areas that John F. Kelly examines in his Methanococcus maripaludis study include S-layer, Tetrasaccharide, Archaellum and Glycobiology.
Between 2012 and 2021, his most popular works were:
- Production of α2,6-sialylated IgG1 in CHO cells (55 citations)
- Antibody light chain variable domains and their biophysically improved versions for human immunotherapy (30 citations)
- Posttranslational Modification of Flagellin FlaB in Shewanella oneidensis (29 citations)
In his most recent research, the most cited papers focused on:
The scientist’s investigation covers issues in Biochemistry, Glycan, Glycosylation, Flagellin and Antibody.
John F. Kelly studies Single-Chain Antibodies which is a part of Biochemistry.
His study looks at the relationship between Glycan and fields such as Mutant, as well as how they intersect with chemical problems.
As a member of one scientific family, John F. Kelly mostly works in the field of Glycosylation, focusing on Threonine and, on occasion, Borrelia burgdorferi.
His study looks at the relationship between Flagellin and topics such as Microbiology, which overlap with Campylobacter, Conserved sequence and Campylobacter jejuni.
His work on Single-domain antibody, Phage display, Immunoglobulin light chain and Protein L is typically connected to Disulfide Linkage as part of general Antibody study, connecting several disciplines of science.
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