What is she best known for?
The fields of study she is best known for:
Her scientific interests lie mostly in Biochemistry, Stereochemistry, Protein structure, Protein folding and Thioredoxin.
Her Stereochemistry research includes themes of Glycogen phosphorylase, Active site, Acetylcholine receptor, Nicotinic acetylcholine receptor and Kinetics.
Her Protein folding research incorporates themes from Folding and Protein disulfide-isomerase.
Her study looks at the intersection of Protein disulfide-isomerase and topics like Periplasmic space with Endoplasmic reticulum.
Her studies in Thioredoxin integrate themes in fields like DsbA and Peptide sequence.
Her work carried out in the field of DsbA brings together such families of science as Cysteine, Function and Bacteria.
Her most cited work include:
- Thioredoxin —a fold for all reasons (675 citations)
- Human sulfotransferases and their role in chemical metabolism (465 citations)
- SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold. (407 citations)
What are the main themes of her work throughout her whole career to date?
Jennifer L. Martin mainly focuses on Biochemistry, Stereochemistry, DsbA, Protein structure and Enzyme.
Her work on Biochemistry deals in particular with Protein disulfide-isomerase, Protein folding, Thioredoxin fold, Peptide sequence and Membrane protein.
The Protein folding study combines topics in areas such as Thioredoxin and Cysteine.
Her Stereochemistry research integrates issues from Protease, Crystal structure, Binding site, Active site and Peptide.
Her research in DsbA intersects with topics in Oxidoreductase, Oxidative folding and Virulence.
Her study in the field of Transferase also crosses realms of Phenylethanolamine N-methyltransferase.
She most often published in these fields:
- Biochemistry (29.85%)
- Stereochemistry (28.00%)
- DsbA (21.23%)
What were the highlights of her more recent work (between 2014-2021)?
- DsbA (21.23%)
- Biochemistry (29.85%)
- Virulence (9.23%)
In recent papers she was focusing on the following fields of study:
Jennifer L. Martin mainly investigates DsbA, Biochemistry, Virulence, Stereochemistry and Protein disulfide-isomerase.
Her studies deal with areas such as Oxidoreductase, Enzyme and Oxidative folding as well as DsbA.
Cysteine, Active site, Membrane protein and Protein folding are the subjects of her Biochemistry studies.
Her Virulence research includes elements of Bacteria, Burkholderia pseudomallei and Melioidosis, Microbiology.
Jennifer L. Martin combines subjects such as Mutant, Peptide, Alanine, Small molecule and Binding site with her study of Stereochemistry.
As a part of the same scientific study, she usually deals with the Protein disulfide-isomerase, concentrating on Thioredoxin fold and frequently concerns with Immunoglobulin domain.
Between 2014 and 2021, her most popular works were:
- Targeting virulence not viability in the search for future antibacterials (89 citations)
- Application of Fragment-Based Screening to the Design of Inhibitors of Escherichia coli DsbA† (32 citations)
- Virulence of the melioidosis pathogen Burkholderia pseudomallei requires the oxidoreductase membrane protein DsbB. (31 citations)
In her most recent research, the most cited papers focused on:
Her primary areas of study are Biochemistry, DsbA, Protein disulfide-isomerase, Membrane protein and Virulence.
Cysteine and Protein structure are the primary areas of interest in her Biochemistry study.
Her research integrates issues of Oxidoreductase, Active site, Enzyme and Structure–activity relationship in her study of DsbA.
Her Oxidoreductase study combines topics in areas such as Peptide sequence and Protein folding.
Jennifer L. Martin has included themes like Stereochemistry and Small molecule in her Enzyme study.
Her Protein disulfide-isomerase research is multidisciplinary, incorporating elements of Periplasmic space, Proteus mirabilis and Peptide.
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