Enrico A. Stura mostly deals with Stereochemistry, Biochemistry, Peptide sequence, Peptide and Protein structure. His Stereochemistry research is multidisciplinary, incorporating perspectives in Cyclase, MHC class I, Catalysis, Substrate and Binding site. His biological study spans a wide range of topics, including Epitope, Crystallization and Structure–activity relationship.
He has researched Peptide in several fields, including Receptor, Alanine, Molecular biology and T-cell receptor. His Molecular biology course of study focuses on Antigen and Protein A, B-cell receptor and Antibody. His studies deal with areas such as V3 loop and Lipid bilayer fusion as well as Protein structure.
Enrico A. Stura focuses on Stereochemistry, Biochemistry, Crystallography, Crystallization and Crystal structure. His Stereochemistry research incorporates elements of Binding site, Active site, Protein structure, Monoclonal antibody and Peptide. His Protein structure research is multidisciplinary, relying on both Biophysics and Peptide sequence.
While the research belongs to areas of Monoclonal antibody, Enrico A. Stura spends his time largely on the problem of Antigen, intersecting his research to questions surrounding Virology. The study of Biochemistry is intertwined with the study of Antibody in a number of ways. The study incorporates disciplines such as Molecular biology, Erythropoietin and Cell biology in addition to Receptor.
Enrico A. Stura mainly investigates Transthyretin, Stereochemistry, Biochemistry, Matrix metalloproteinase and Combinatorial chemistry. His Transthyretin study also includes fields such as
His Biochemistry research integrates issues from Chalcone and Cancer research. His Matrix metalloproteinase study incorporates themes from Hydrolase, Carboxylate, Thiourea and Chelation. The Combinatorial chemistry study combines topics in areas such as Crystallization, Organic chemistry and Solubilization.
His primary areas of study are Biochemistry, Stereochemistry, Matrix metalloproteinase inhibitor, Matrix metalloproteinase and In vitro. His studies in Biochemistry integrate themes in fields like Cancer research and Lymphoma. Enrico A. Stura has included themes like Peptide, Peptide chemical synthesis, Acid-sensing ion channel and Sodium channel in his Stereochemistry study.
His Matrix metalloproteinase inhibitor research is multidisciplinary, incorporating perspectives in Hydrolase and Structure–activity relationship. Enrico A. Stura focuses mostly in the field of Structure–activity relationship, narrowing it down to matters related to Zinc and, in some cases, Combinatorial chemistry. His work in the fields of In vitro, such as Matrigel, intersects with other areas such as Conjugate and Linker.
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Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb.
Daved H. Fremont;Masazumi Matsumura;Enrico A. Stura;Per A. Peterson.
Functional Mimicry of a Protein Hormone by a Peptide Agonist: The EPO Receptor Complex at 2.8 Å
Oded Livnah;Enrico A. Stura;Dana L. Johnson;Steven A. Middleton.
Crystal Structure of Mouse CD1: An MHC-Like Fold with a Large Hydrophobic Binding Groove
Z.-H. Zeng;A. R. Castaño;B. W. Segelke;E. A. Stura.
Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation.
Oded Livnah;Enrico A. Stura;Steven A. Middleton;Dana L. Johnson.
Crystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: Structural basis for recognition of B-cell receptors and superantigen activity
Marc Graille;Enrico A. Stura;Adam L. Corper;Brian J. Sutton.
Proceedings of the National Academy of Sciences of the United States of America (2000)
Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation
Stéphane Bressanelli;Karin Stiasny;Steven L Allison;Enrico A Stura.
The EMBO Journal (2004)
Immune Versus Natural Selection: Antibody Aldolases with Enzymic Rates But Broader Scope
Carlos F. Barbas;Andreas Heine;Guofu Zhong;Torsten Hoffmann.
Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity.
Marie Hélène Le Du;Torgny Stigbrand;Michael J. Taussig;André Ménez.
Journal of Biological Chemistry (2001)
Crystal Structure of the Principal Neutralization Site of HIV-1
Jayant B. Ghiara;Enrico A. Stura;Robyn L. Stanfield;Albert T. Profy.
Crystal structure of an H-2Kb-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove.
Daved H. Fremont;Enrico A. Stura;Masazaumi Matsumura;Per A. Peterson.
Proceedings of the National Academy of Sciences of the United States of America (1995)
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