His scientific interests lie mostly in Biochemistry, Peptide sequence, Amylin, Internal medicine and Endocrinology. His Biochemistry study is mostly concerned with Affinity chromatography, Phosphorylation, Tyrosine, Receptor and Glycoprotein. Antony C. Willis has included themes like Complementary DNA and Nucleic acid sequence in his Affinity chromatography study.
His Peptide sequence research incorporates elements of Amino acid, Glycosylation, Molecular mass, Molecular biology and Binding site. His Glycosylation study incorporates themes from Antibody, Fragment crystallizable region, N-linked glycosylation and Recombinant DNA. His Amylin research includes elements of Glycogen synthase, Collagenase, Peptide and Pancreatic islets.
His primary areas of study are Biochemistry, Molecular biology, Peptide sequence, Antigen and Antibody. Biochemistry is closely attributed to Conglutinin in his study. His Molecular biology research incorporates themes from Complementary DNA, Monoclonal antibody, Protein primary structure and Immunoglobulin superfamily.
His Peptide sequence research is multidisciplinary, incorporating elements of Amino acid, Polyacrylamide gel electrophoresis, Protein structure and Peptide. His Peptide study integrates concerns from other disciplines, such as Endocrinology, Amylin, Pancreatic Extracts, Internal medicine and Pancreatic islets. In the field of Antibody, his study on Antigenicity overlaps with subjects such as Echinococcus granulosus.
His primary areas of investigation include Biochemistry, Immunology, Biophysics, Affinity chromatography and Glycosylation. His work in Biochemistry is not limited to one particular discipline; it also encompasses Molecular biology. His studies deal with areas such as Oxygenase and Molecular mass as well as Molecular biology.
His Immunology course of study focuses on Binding protein and Antigen. His Affinity chromatography research is multidisciplinary, incorporating elements of Lectin, Mannan-binding lectin, Protease inhibitor, Macroglobulin and Monoclonal antibody. As part of one scientific family, Antony C. Willis deals mainly with the area of Glycosylation, narrowing it down to issues related to the Glycan, and often Heterologous and Recombinant DNA.
His primary scientific interests are in Biochemistry, Context, Cyclin A, Tyrosine phosphorylation and Cyclin-dependent kinase 2. His study in Biogenesis, Lyase, Cytochrome c, Heme and Cytochrome falls under the purview of Biochemistry. Context is integrated with TSG-6, Chondroitin sulfate, Stereochemistry, Cofactor and Moiety in his research.
Cyclin A is intertwined with Cyclin-dependent kinase 1, Phosphorylation cascade, Cell biology and Phosphorylation in his study.
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.
Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients
G. J. S. Cooper;A. C. Willis;A. Clark;R. C. Turner.
Proceedings of the National Academy of Sciences of the United States of America (1987)
Molecular analysis of the association of HLA-B53 and resistance to severe malaria.
A V Hill;J Elvin;A C Willis;M Aidoo.
Lymphoid/neuronal cell surface OX2 glycoprotein recognizes a novel receptor on macrophages implicated in the control of their function.
G J Wright;M J Puklavec;A C Willis;R M Hoek.
The Glycosylation and Structure of Human Serum IgA1, Fab, and Fc Regions and the Role of N-Glycosylation on Fcα Receptor Interactions
Taj S. Mattu;Richard J. Pleass;Antony C. Willis;Mogens Kilian.
Journal of Biological Chemistry (1998)
Amylin found in amyloid deposits in human type 2 diabetes mellitus may be a hormone that regulates glycogen metabolism in skeletal muscle
G. J S Cooper;B. Leighton;G. D. Dimitriadis;M. Parry-Billings.
Proceedings of the National Academy of Sciences of the United States of America (1988)
Islet amyloid formed from diabetes-associated peptide may be pathogenic in type-2 diabetes.
A Clark;C.E Lewis;A.C Willis;G.J.S Cooper.
The Lancet (1987)
A new macrophage differentiation antigen which is a member of the scavenger receptor superfamily
S. K. A. Law;K. J. Micklem;J. M. Shaw;Xi-Ping Zhang.
European Journal of Immunology (1993)
The reaction mechanism of the internal thioester in the human complement component C4
Alister W. Dodds;Xiang-Dong Ren;Xiang-Dong Ren;Antony C. Willis;S. K. Alex Law.
Isolation and characterization of a new member of the scavenger receptor superfamily, glycoprotein-340 (gp-340), as a lung surfactant protein-D binding molecule
Uffe Holmskov;Peter Lawson;Børge Teisner;Ida Tornøe.
Journal of Biological Chemistry (1997)
CD47 is a ligand for rat macrophage membrane signal regulatory protein SIRP (OX41) and human SIRPalpha 1.
E F Vernon-Wilson;W J Kee;A C Willis;A N Barclay.
European Journal of Immunology (2000)
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below: