The scientist’s investigation covers issues in Stereochemistry, Crystallography, Protein structure, Crystal structure and Binding site. His Stereochemistry research includes elements of Galactose oxidase, Lysozyme, DNA, Active site and Peptide sequence. His research in Crystallography intersects with topics in Myoglobin and Hydrogen bond.
While the research belongs to areas of Myoglobin, he spends his time largely on the problem of Oxygen storage, intersecting his research to questions surrounding Residue, Inorganic chemistry, Steric effects, Tetramer and Histidine. His Protein structure research incorporates elements of Biophysics and Protein secondary structure. His Binding site research is multidisciplinary, relying on both Binding protein, Multiple isomorphous replacement and Ligand.
His primary scientific interests are in Stereochemistry, Biochemistry, Crystallography, Crystal structure and DNA. His Stereochemistry research is multidisciplinary, incorporating elements of Galactose oxidase, Amine oxidase, Active site, Protein structure and Binding site. His work carried out in the field of Galactose oxidase brings together such families of science as Cofactor and Thioether.
Simon E. V. Phillips combines subjects such as Crystallization, Molecule, Hydrogen bond and Myoglobin with his study of Crystallography. His Crystal structure research focuses on subjects like Hydroxymethyl, which are linked to Monoclinic crystal system. His study in DNA is interdisciplinary in nature, drawing from both Transcription and Repressor.
His scientific interests lie mostly in Stereochemistry, Capsid, Andrology, Intracellular and Molecular biology. Simon E. V. Phillips has included themes like Mutagenesis, DNA, Escherichia coli, Arginine and Epigenetics in his Stereochemistry study. As a part of the same scientific family, Simon E. V. Phillips mostly works in the field of Arginine, focusing on Alanine and, on occasion, Crystallography.
The Capsid study combines topics in areas such as RNA and Genome. His Intracellular research incorporates themes from Antibody and Small molecule. His research in Molecular biology intersects with topics in Protein structure, Plasmid, Rolling circle replication and TUNEL assay.
Capsid, Genetics, RNA, Genome and Small molecule are his primary areas of study. Simon E. V. Phillips interconnects Gene expression, Conformational change and Single-Stranded RNA in the investigation of issues within Capsid. Simon E. V. Phillips has researched RNA in several fields, including Protein structure, Biophysics, Computational biology and Protein Data Bank.
As a member of one scientific family, Simon E. V. Phillips mostly works in the field of Protein structure, focusing on Active site and, on occasion, Stereochemistry. The concepts of his Stereochemistry study are interwoven with issues in Guanidine and Arginine. His Small molecule research integrates issues from Mutant RAS and Effector, Intracellular, Cell biology.
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Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution
A. G. Amit;R. A. Mariuzza;S. E. V. Phillips;R. J. Poljak.
Science (1986)
Novel thioether bond revealed by a 1.7 Å crystal structure of galactose oxidase
Nobutoshi Ito;Simon E. V. Phillips;Conrad Stevens;Zumrut B. Ogel.
Nature (1994)
Structure and refinement of oxymyoglobin at 1·6 Å resolution
Simon E.V. Phillips.
Journal of Molecular Biology (1980)
Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin.
Simon E. V. Phillips;Simon E. V. Phillips;Benno P. Schoenborn.
Nature (1981)
Crystal structure of a free radical enzyme, galactose oxidase.
Nobutoshi Ito;Simon E.V. Phillips;Kapil D.S. Yadav;Peter F. Knowles.
Journal of Molecular Biology (1994)
Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography.
Zsolt Böcskei;Colin R. Groom;Darren R. Flower;Darren R. Flower;Charles E. Wright.
Nature (1992)
Crystal structure of the met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands.
William S. Somers;Simon E. V. Phillips.
Nature (1992)
The structural basis of antigen-antibody recognition.
R. A. Mariuzza;S. E. V. Phillips;R. J. Poljak.
Annual Review of Biophysics and Biophysical Chemistry (1987)
Three-dimensional structure of an antigen-antibody complex at 6 A resolution.
A. G. Amit;R. A. Mariuzza;S. E. V. Phillips;R. J. Poljak.
Nature (1985)
Mutations in 15-hydroxyprostaglandin dehydrogenase cause primary hypertrophic osteoarthropathy
Sandeep Uppal;Sandeep Uppal;Christine P Diggle;Ian M Carr;Colin W G Fishwick.
Nature Genetics (2008)
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