Stereochemistry, Crystallography, Protein structure, Antibody and Biochemistry are her primary areas of study. Her Stereochemistry research is multidisciplinary, incorporating perspectives in Amino acid, Peptide and Binding site. The Crystallography study combines topics in areas such as Protein primary structure, Nuclear magnetic resonance spectroscopy and Sequence.
Her research in Protein structure intersects with topics in Biophysics, DNA, Fusion protein and Protein folding. Her studies in Antibody integrate themes in fields like Molecular biology, Glycosylation and Glycan. Her Glycosylation research incorporates elements of Epitope, Humoral immunity and Neutralization.
Carole A. Bewley focuses on Stereochemistry, Biochemistry, Sponge, Nuclear magnetic resonance spectroscopy and Virology. Carole A. Bewley has researched Stereochemistry in several fields, including Amino acid, Peptide, Amidase and Mycothiol. Glycan, Binding site, Protein structure, Enzyme and Glycoprotein are among the areas of Biochemistry where the researcher is concentrating her efforts.
The concepts of her Sponge study are interwoven with issues in Glycopeptide, Bicyclic molecule, Antifungal and Cyclic peptide. Her research integrates issues of Crystallography, Affinities and Carbohydrate in her study of Nuclear magnetic resonance spectroscopy. Her work carried out in the field of Virology brings together such families of science as Epitope, Antibody and Gp41.
Carole A. Bewley mainly investigates Biochemistry, Stereochemistry, Virology, Glycan and Glycoprotein. Her work in the fields of Biochemistry, such as Glycosylation, Envelope glycoprotein GP120 and Blasticidin S, overlaps with other areas such as Transporter and Multidrug Resistance-Associated Proteins. Her Stereochemistry study integrates concerns from other disciplines, such as Iminosugar, Sponge and Streptomyces.
Her studies in Virology integrate themes in fields like Antibody and Immunology. As a part of the same scientific study, Carole A. Bewley usually deals with the Glycan, concentrating on Binding site and frequently concerns with Griffithsin and Epitope. In her research, Characterization, Viral envelope, Immunogenicity and Mode of action is intimately related to Lectin, which falls under the overarching field of Glycoprotein.
The scientist’s investigation covers issues in Virology, Glycoprotein, Neutralization, Antibody and Glycan. Her work carried out in the field of Virology brings together such families of science as Lectin, Mode of action, Immunogenicity and Griffithsin. She has included themes like Host protein, Therapeutic targeting, Maraviroc, Neuroscience and Microbicide in her Glycoprotein study.
Her studies deal with areas such as Oligosaccharide, Biochemistry, Humoral immunity, Epitope and Viral protein as well as Neutralization. Her study in Epitope is interdisciplinary in nature, drawing from both Binding site, Monoclonal antibody and Simian immunodeficiency virus. The concepts of her Glycan study are interwoven with issues in Trimer, Glycosylation and Neutralizing antibody.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
Jason S. McLellan;Marie Pancera;Chris Carrico;Jason Gorman.
Nature (2011)
Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4.
Chih Chin Huang;Son N. Lam;Priyamvada Acharya;Min Tang.
Science (2007)
The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif.
J R Huth;C A Bewley;M S Nissen;J N Evans.
Nature Structural & Molecular Biology (1997)
Two classes of metabolites from Theonella swinhoei are localized in distinct populations of bacterial symbionts.
C. A. Bewley;N. D. Holland;D. J. Faulkner.
Cellular and Molecular Life Sciences (1996)
Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B and G
Guillaume B.E. Stewart-Jones;Cinque Soto;Thomas Lemmin;Thomas Lemmin;Gwo Yu Chuang.
Cell (2016)
Minor Groove-Binding Architectural Proteins: Structure, Function, and DNA Recognition
Carole A. Bewley;and Angela M. Gronenborn;G. Marius Clore.
Annual Review of Biophysics and Biomolecular Structure (1998)
Structural basis for diverse N-glycan recognition by HIV-1–neutralizing V1–V2–directed antibody PG16
Marie Pancera;Syed Shahzad-Ul-Hussan;Nicole A. Doria-Rose;Jason S. McLellan.
Nature Structural & Molecular Biology (2013)
Solution structure of cyanovirin-N, a potent HIV-inactivating protein
C A Bewley;K R Gustafson;M R Boyd;D G Covell.
Nature Structural & Molecular Biology (1998)
Lithistid Sponges: Star Performers or Hosts to the Stars.
Carole A. Bewley;D. John Faulkner.
Angewandte Chemie (1998)
Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops
Young Do Kwon;Andrés Finzi;Xueling Wu;Cajetan Dogo-Isonagie.
Proceedings of the National Academy of Sciences of the United States of America (2012)
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