What is he best known for?
The fields of study he is best known for:
Andrew G. Plaut mainly focuses on Microbiology, Biochemistry, Proteases, Antibody and Protease.
His Microbiology research is multidisciplinary, relying on both Astrovirus, Lactoferrin and Small intestine.
His work on Serine protease, Enzyme and Molecular mass as part of general Biochemistry research is frequently linked to Aminopeptidase, thereby connecting diverse disciplines of science.
Andrew G. Plaut has researched Serine protease in several fields, including Concanavalin A, T cell, Dipeptide and Molecular biology.
His biological study spans a wide range of topics, including Neisseria meningitidis, Pathogenic bacteria, Bacteria and Virology.
His Neisseria gonorrhoeae study deals with Proteolytic enzymes intersecting with Enzyme inhibitor, Peptide and Active site.
His most cited work include:
- Studies of intestinal microflora. II. Microorganisms of the small intestine and their relations to oral and fecal flora. (270 citations)
- Studies of intestinal microflora. V. Fecal microbial ecology in ulcerative colitis and regional enteritis: relationship to severity of disease and chemotherapy. (228 citations)
- The IgA1 Proteases of Pathogenic Bacteria (226 citations)
What are the main themes of his work throughout his whole career to date?
His primary areas of study are Microbiology, Proteases, Protease, Biochemistry and Antibody.
His study in Microbiology is interdisciplinary in nature, drawing from both Bacteria, Proteolytic enzymes, Immunoglobulin A and Virology.
Andrew G. Plaut works mostly in the field of Proteolytic enzymes, limiting it down to concerns involving Neisseria gonorrhoeae and, occasionally, Neisseria meningitidis.
His Proteases research includes elements of Cleave, Dermatitis herpetiformis, Secretion, Immune system and Iga deposition.
His Protease study integrates concerns from other disciplines, such as Isotype, Proteolysis, Molecular biology, Fragment crystallizable region and Streptococcus.
His Antibody research is multidisciplinary, incorporating elements of Neisseria and Antigen.
He most often published in these fields:
- Microbiology (48.46%)
- Proteases (36.92%)
- Protease (35.38%)
What were the highlights of his more recent work (between 2001-2014)?
- Microbiology (48.46%)
- Proteases (36.92%)
- Biochemistry (27.69%)
In recent papers he was focusing on the following fields of study:
His primary areas of study are Microbiology, Proteases, Biochemistry, Protease and Dermatitis herpetiformis.
His Microbiology research incorporates elements of Lactoferrin, In vitro and Immunoglobulin A.
His Proteases research includes themes of Nephropathy, Immunology, Antibody, Immune system and Proteolysis.
His Antibody study combines topics from a wide range of disciplines, such as Antigen and Virology.
The various areas that Andrew G. Plaut examines in his Biochemistry study include Deposition and IgA-specific metalloendopeptidase.
Andrew G. Plaut works in the field of Protease, namely Serine protease.
Between 2001 and 2014, his most popular works were:
- Neisseria meningitidis GNA2132, a heparin-binding protein that induces protective immunity in humans (190 citations)
- Diarrhea in American infants and young children in the community setting: incidence, clinical presentation and microbiology. (117 citations)
- Human milk lactoferrin is a serine protease that cleaves Haemophilus surface proteins at arginine-rich sites. (89 citations)
In his most recent research, the most cited papers focused on:
His primary areas of investigation include Microbiology, Proteases, Protease, Serine protease and Biochemistry.
Andrew G. Plaut specializes in Microbiology, namely Haemophilus influenzae.
His research in Proteases intersects with topics in Lactoferrin, Antibody and Virology.
His Protease research integrates issues from Cleavage, Glycan, Immunoglobulin A and Fragment crystallizable region.
His studies in Serine protease integrate themes in fields like Immunoglobulin Fc Fragments, Serine and Proteolysis.
The concepts of his Biochemistry study are interwoven with issues in Immunoglobulin binding and Isotype.
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