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.
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.
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.
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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Thioredoxin —a fold for all reasons
Jennifer L Martin.
Human sulfotransferases and their role in chemical metabolism
Niranjali Gamage;Amanda Barnett;Nadine Hempel;Ronald G. Duggleby.
Toxicological Sciences (2006)
Functional-Group Contributions to Drug Receptor Interactions
P. R. Andrews;D. J. Craik;J. L. Martin.
Journal of Medicinal Chemistry (1984)
SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold.
Jennifer L Martin;Fiona M McMillan.
Current Opinion in Structural Biology (2002)
Crystal structure of the DsbA protein required for disulphide bond formation in vivo
Jennifer L. Martin;Jennifer L. Martin;James C. A. Bardwell;James C. A. Bardwell;James C. A. Bardwell;John Kuriyan.
Protein disulfide isomerase: the structure of oxidative folding
Christian W. Gruber;Maša Čemažar;Begoña Heras;Jennifer L. Martin.
Trends in Biochemical Sciences (2006)
Activity of Recombinant Dengue 2 Virus NS3 Protease in the Presence of a Truncated NS2B Co-factor, Small Peptide Substrates, and Inhibitors
Donmienne Leung;Kate Schroder;Helen White;Ning-Xia Fang.
Journal of Biological Chemistry (2001)
DSB proteins and bacterial pathogenicity
Begona Heras;Stephen R Shouldice;Makrina Totsika;Martin Scanlon.
Nature Reviews Microbiology (2009)
Post-crystallization treatments for improving diffraction quality of protein crystals
Begoña Heras;Jennifer L. Martin.
Acta Crystallographica Section D-biological Crystallography (2005)
In vivo growth characteristics of leucine and methionine auxotrophic mutants of Mycobacterium bovis BCG generated by transposon mutagenesis.
R A McAdam;T R Weisbrod;J Martin;J D Scuderi.
Infection and Immunity (1995)
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