What is he best known for?
The fields of study he is best known for:
His primary areas of study are Molecular biology, Escherichia coli, Microbiology, Shiga-like toxin and Repressor.
His Molecular biology research includes elements of Cholera toxin, Mutant, Gene, Promoter and Molecular cloning.
Randall K. Holmes specializes in Escherichia coli, namely Structural gene.
His specific area of interest is Microbiology, where Randall K. Holmes studies Toxin.
The various areas that Randall K. Holmes examines in his Toxin study include Shiga toxin, Enterobacteriaceae and Shigella dysenteriae.
The concepts of his Repressor study are interwoven with issues in DNA, Corynebacterium diphtheriae, Crystallography and Diphtheria toxin.
His most cited work include:
- Shiga and Shiga-like toxins. (594 citations)
- Shiga-like toxin-converting phages from Escherichia coli strains that cause hemorrhagic colitis or infantile diarrhea (503 citations)
- Two toxin-converting phages from Escherichia coli O157:H7 strain 933 encode antigenically distinct toxins with similar biologic activities. (483 citations)
What are the main themes of his work throughout his whole career to date?
His primary scientific interests are in Microbiology, Molecular biology, Cholera toxin, Escherichia coli and Biochemistry.
His Microbiology research incorporates themes from Virology, Gene and Vibrio cholerae.
The Molecular biology study combines topics in areas such as Diphtheria toxin, Antiserum, Repressor, Corynebacterium diphtheriae and Operon.
His work deals with themes such as Protein subunit, Antigen, Endoplasmic reticulum, Ganglioside and Bacterial adhesin, which intersect with Cholera toxin.
The Escherichia coli study which covers Plasmid that intersects with Molecular cloning and Extracellular.
He has included themes like Shigella and Shigella dysenteriae in his Shiga toxin study.
He most often published in these fields:
- Microbiology (34.64%)
- Molecular biology (34.64%)
- Cholera toxin (34.08%)
What were the highlights of his more recent work (between 2003-2020)?
- Cholera toxin (34.08%)
- Microbiology (34.64%)
- Biochemistry (27.37%)
In recent papers he was focusing on the following fields of study:
Randall K. Holmes mainly investigates Cholera toxin, Microbiology, Biochemistry, Escherichia coli and Protein subunit.
His work carried out in the field of Cholera toxin brings together such families of science as Virology, Cholera vaccine, Vibrio cholerae, Toxin and Immunogenicity.
Randall K. Holmes is involved in the study of Microbiology that focuses on Diphtheria toxin in particular.
His Biochemistry research focuses on subjects like Biophysics, which are linked to Protein structure and Protein folding.
His study of Enterotoxin is a part of Escherichia coli.
Randall K. Holmes interconnects AB5 toxin, Molecular biology and Conformational change in the investigation of issues within Protein subunit.
Between 2003 and 2020, his most popular works were:
- Structural Characterization of the SARS-Coronavirus Spike S Fusion Protein Core (161 citations)
- Structural basis for the activation of cholera toxin by human ARF6-GTP. (124 citations)
- Cellular internalization of cytolethal distending toxin: a new end to a known pathway. (88 citations)
In his most recent research, the most cited papers focused on:
Randall K. Holmes spends much of his time researching Biochemistry, Cholera toxin, Cell biology, Endoplasmic reticulum and Vibrio cholerae.
As part of the same scientific family, he usually focuses on Biochemistry, concentrating on Biophysics and intersecting with Protein structure, Fusion protein and Peptide sequence.
His Cholera toxin research is multidisciplinary, incorporating elements of Plasmid, Toxin, Escherichia coli, Endocytosis and ADP-ribosylation.
His biological study spans a wide range of topics, including Mutagenesis, Microbiology and Active site.
As a part of the same scientific family, Randall K. Holmes mostly works in the field of Cell biology, focusing on Cell membrane and, on occasion, Brefeldin A.
His Endoplasmic reticulum study incorporates themes from Plasma protein binding, Ganglioside and Endoplasmic-reticulum-associated protein degradation.
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