Robin J. Leatherbarrow mainly investigates Biochemistry, Binding site, Enzyme, Stereochemistry and Protein structure. His Biochemistry study frequently draws connections between adjacent fields such as Plasmodium vivax. He has researched Binding site in several fields, including Plasma protein binding, Human serum albumin, Saturated fatty acid, Leishmania donovani and Open reading frame.
His research in Enzyme intersects with topics in Cyclotides and Cyclotide. His research integrates issues of Equilibrium constant and Reaction mechanism in his study of Stereochemistry. His Protein structure research is multidisciplinary, incorporating elements of Cyclic peptide, Peptide library, Combinatorial chemistry and Chymotrypsin.
Robin J. Leatherbarrow spends much of his time researching Stereochemistry, Biochemistry, N-myristoyltransferase, Enzyme and Peptide. His studies deal with areas such as Protein engineering, Molecule and Chymotrypsin as well as Stereochemistry. His research on Biochemistry frequently connects to adjacent areas such as Plasmodium falciparum.
His work in N-myristoyltransferase addresses subjects such as Plasmodium vivax, which are connected to disciplines such as Benzofuran. His Enzyme research incorporates themes from Molecular biology, Tyrosine and Leishmania donovani. In his study, which falls under the umbrella issue of Peptide, Membrane is strongly linked to Combinatorial chemistry.
His scientific interests lie mostly in N-myristoyltransferase, Stereochemistry, Plasmodium vivax, Biochemistry and Leishmania major. His work carried out in the field of N-myristoyltransferase brings together such families of science as Combinatorial chemistry, Quinoline, Peptidomimetic and Microbiology. The study incorporates disciplines such as Cytoplasm, Enantiomeric excess, Picolinic acid, Fluorescence microscope and Derivative in addition to Stereochemistry.
His Plasmodium vivax research is multidisciplinary, relying on both Pyrazole, Thioester and Benzofuran. He combines subjects such as Plasmodium falciparum and Leishmania donovani with his study of Biochemistry. His biological study spans a wide range of topics, including Glycine, Small molecule, Peptide and Virus.
His primary scientific interests are in Biochemistry, Plasmodium falciparum, Transferase, Plasmodium vivax and Enzyme. His study in Plasmodium falciparum is interdisciplinary in nature, drawing from both Ligand efficiency, Pharmacology and Drug discovery. His Transferase research integrates issues from Myristoylation, N-myristoyltransferase, Drug target, Leishmania donovani and Combinatorial chemistry.
His Enzyme research includes themes of Glycine, Molecular biology, Small molecule and Fatty acid. Robin J. Leatherbarrow has included themes like Leishmaniasis and Stereochemistry in his Structure–activity relationship study. His work deals with themes such as Plasma protein binding and Ligand, which intersect with Stereochemistry.
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Effector functions of a monoclonal aglycosylated mouse IgG2a: binding and activation of complement component C1 and interaction with human monocyte Fc receptor.
Robin J. Leatherbarrow;Thomas W. Rademacher;Raymond A. Dwek;Jennifer M. Woof.
Molecular Immunology (1985)
Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering
Robin J. Leatherbarrow;Alan R. Fersht;Greg Winter.
Proceedings of the National Academy of Sciences of the United States of America (1985)
Using linear and non-linear regression to fit biochemical data
Robin J. Leatherbarrow.
Trends in Biochemical Sciences (1990)
Kinetics of Protein-Protein Interactions at the Surface of an Optical Biosensor
P.R. Edwards;A. Gill;D.V. Pollardknight;M. Hoare.
Analytical Biochemistry (1995)
Validation of N -myristoyltransferase as an antimalarial drug target using an integrated chemical biology approach
Megan H. Wright;Barbara Clough;Mark D. Rackham;Kaveri Rangachari.
Nature Chemistry (2014)
Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships.
Alan R. Fersht;Robin J. Leatherbarrow;Tim N. C. Wells.
Biochemistry (1987)
Studies on the mechanism of binding of serum albumins to immobilized cibacron blue F3G A
R J Leatherbarrow;P D Dean.
Biochemical Journal (1980)
N-Myristoyl transferase-mediated protein labelling in vivo.
William P. Heal;Sasala R. Wickramasinghe;Robin J. Leatherbarrow;Edward W. Tate.
Organic and Biomolecular Chemistry (2008)
Chemical and biomimetic total syntheses of natural and engineered MCoTI cyclotides
Panumart Thongyoo;Núria Roqué-Rosell;Robin J. Leatherbarrow;Edward W. Tate.
Organic and Biomolecular Chemistry (2008)
Crystal structure of foot-and-mouth disease virus 3C protease: New insights into catalytic mechanism and cleavage specificity
James R. Birtley;Stephen R. Knox;Agnès M. Jaulent;Peter Brick.
Journal of Biological Chemistry (2005)
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