His primary areas of study are Biochemistry, Stereochemistry, Protein structure, Cell biology and Active site. His study in the fields of Cofactor, Oxidoreductase, Binding site and Bacterial outer membrane under the domain of Biochemistry overlaps with other disciplines such as Polymyxin B1. Richard B. Sessions combines subjects such as Antiparallel, Sequence, Ethylenediamine, Peptide and Histidine with his study of Stereochemistry.
His Protein structure study combines topics in areas such as Hydrogen bond and Protein folding. His Hydrogen bond research incorporates themes from Amino acid and Crystallography. His Cell biology research includes themes of Integral membrane protein, Vitronectin and Integrin binding.
Richard B. Sessions mostly deals with Biochemistry, Biophysics, Stereochemistry, Lactate dehydrogenase and Cell biology. Enzyme, Binding site, Cofactor, NAD+ kinase and Protein structure are among the areas of Biochemistry where Richard B. Sessions concentrates his study. The Protein structure study combines topics in areas such as Side chain, Peptide and Protein folding.
His biological study spans a wide range of topics, including Crystallography and Protein engineering. His studies deal with areas such as Protein subunit, Receptor, Membrane, Transmembrane domain and Small molecule as well as Biophysics. His research on Cell biology often connects related topics like Mutant.
Richard B. Sessions spends much of his time researching Biophysics, Cell biology, Receptor, Nicotinic agonist and Acetylcholine receptor. Richard B. Sessions has included themes like Allosteric regulation, Small molecule, Transmembrane domain and Clathrin in his Biophysics study. His work deals with themes such as Insulin, Mutant and Docking, which intersect with Cell biology.
In Polymerization, Richard B. Sessions works on issues like Mechanism of action, which are connected to Stereochemistry. His Fatty acid study is focused on Biochemistry in general. Specifically, his work in Biochemistry is concerned with the study of Target protein.
Richard B. Sessions focuses on Synthetic biology, Cell biology, Peptide, Protein structure and Protein design. His Cell biology research integrates issues from Mutation, Secretion, Secretory protein and Mutant. He interconnects Biophysics, Protein folding, Peptide sequence, Endocytosis and Molecular model in the investigation of issues within Protein structure.
His Protein design study incorporates themes from Crystallography and Self-assembly. His study looks at the intersection of Crystallography and topics like Polyproline helix with Protein engineering. The study of Biochemistry and Enzyme are components of his Protein engineering research.
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.
Self-Assembling Cages from Coiled-Coil Peptide Modules
Jordan M. Fletcher;Robert L. Harniman;Frederick R. H. Barnes;Aimee L. Boyle.
Science (2013)
Anion receptor molecules. Synthesis and anion-binding properties of polyammonium macrocycles
B Dietrich;M W Hosseini;J M Lehn;Richard B Sessions.
Journal of the American Chemical Society (1981)
Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase
J A Read;V J Winter;C M Eszes;Richard B Sessions.
Proteins (2001)
Interaction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sites
Darragh B. Freir;Andrew J. Nicoll;Igor Klyubin;Silvia Panico.
Nature Communications (2011)
Neuropilin-1 is a host factor for SARS-CoV-2 infection.
James L. Daly;Boris Simonetti;Katja Klein;Kai En Chen.
Science (2020)
Neuropilin-1 is a host factor for SARS-CoV-2 infection
James L. Daly;Boris Simonetti;Carlos Antón-Plágaro;Maia Kavanagh Williamson.
bioRxiv (2020)
Computational design of water-soluble α-helical barrels
Andrew R. Thomson;Christopher W. Wood;Antony J. Burton;Gail J. Bartlett.
Science (2014)
Determinants of strand register in antiparallel beta-sheets of proteins
EG Hutchinson;RB Sessions;JM Thornton;DN Woolfson.
Protein Science (1998)
A de novo peptide hexamer with a mutable channel
Nathan R Zaccai;Bertie Chi;Andrew R Thomson;Aimee L Boyle.
Nature Chemical Biology (2011)
Tyrphostin A23 Inhibits Internalization of the Transferrin Receptor by Perturbing the Interaction between Tyrosine Motifs and the Medium Chain Subunit of the AP-2 Adaptor Complex
David N. Banbury;Jacqueline D. Oakley;Richard B. Sessions;George Banting.
Journal of Biological Chemistry (2003)
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