Giuseppe Zanotti mostly deals with Stereochemistry, Biochemistry, Binding site, Protein kinase A and Binding protein. His study in Stereochemistry is interdisciplinary in nature, drawing from both Ligand, Cofactor, Crystal structure, Fatty acid and Side chain. His Biochemistry study frequently draws parallels with other fields, such as Cell biology.
His Binding site research is multidisciplinary, incorporating elements of Protein structure and Hydrogen bond. His Protein kinase A research includes elements of Emodin, Transferase, Cancer cell, Active site and GTP'. Giuseppe Zanotti interconnects Peptide sequence and Retinol binding protein in the investigation of issues within Binding protein.
Giuseppe Zanotti mainly investigates Biochemistry, Stereochemistry, Crystallography, Crystal structure and Helicobacter pylori. His Biochemistry study frequently draws connections between related disciplines such as Transthyretin. His Stereochemistry study integrates concerns from other disciplines, such as Transferase, Kinase, Protein kinase A, Active site and Binding site.
His research in Crystallography intersects with topics in X-ray crystallography, Crystallization, Molecule and Protein structure. His work deals with themes such as Human pathogen, Pathogenicity island and Microbiology, which intersect with Helicobacter pylori. His Peptide sequence research includes themes of Plasma protein binding and Retinol binding.
His main research concerns Biochemistry, Helicobacter pylori, Microbiology, Biophysics and Crystal structure. His study brings together the fields of Transthyretin and Biochemistry. His Helicobacter pylori research incorporates elements of Cancer, Interleukin 23, Interleukin 6 and Human pathogen, Bacteria.
His research integrates issues of Gene and Function in his study of Microbiology. His work carried out in the field of Biophysics brings together such families of science as Membrane and Cytosol. His study in Stereochemistry extends to Crystal structure with its themes.
Giuseppe Zanotti spends much of his time researching Biochemistry, Plasma protein binding, Protein structure, Transthyretin and Cell biology. Enzyme, Mutant, Protein Data Bank, Wild type and Transport protein are the primary areas of interest in his Biochemistry study. His biological study spans a wide range of topics, including Molecular biology, Peptide sequence, Clostridium botulinum and Metalloproteinase.
The concepts of his Protein structure study are interwoven with issues in Chlorophyll fluorescence and Pathogenicity island. His Transthyretin research is multidisciplinary, relying on both Native state, Cooperative binding, Binding site and Cooperativity. His studies deal with areas such as Tetrameric protein, Stereochemistry, Tetramer and Ligand Binding Protein as well as Cooperative binding.
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Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 A resolution.
Hugo L. Monaco;Giuseppe Zanotti;Paola Spadon;Martino Bolognesi.
Journal of Molecular Biology (1987)
Toward the rational design of protein kinase casein kinase-2 inhibitors.
Stefania Sarno;Stefano Moro;Flavio Meggio;Giuseppe Zagotto.
Pharmacology & Therapeutics (2002)
Three-dimensional structure of recombinant human muscle fatty acid-binding protein.
G Zanotti;G Scapin;P Spadon;J.H. Veerkamp.
Journal of Biological Chemistry (1992)
Plasma retinol-binding protein: structure and interactions with retinol, retinoids, and transthyretin.
Giuseppe Zanotti;Rodolfo Berni.
Vitamins and Hormones Series (2004)
Structural features underlying selective inhibition of protein kinase CK2 by ATP site‐directed tetrabromo‐2‐benzotriazole
Roberto Battistutta;Erika De Moliner;Stefania Sarno;Giuseppe Zanotti.
Protein Science (2008)
Structure of the Neutrophil-activating Protein from Helicobacter pylori
Giuseppe Zanotti;Elena Papinutto;William G. Dundon;Roberto Battistutta.
Journal of Molecular Biology (2002)
The replacement of ATP by the competitive inhibitor emodin induces conformational modifications in the catalytic site of protein kinase CK2.
Roberto Battistutta;Stefania Sarno;Erika De Moliner;Elena Papinutto.
Journal of Biological Chemistry (2000)
Biochemical and three-dimensional-structural study of the specific inhibition of protein kinase CK2 by [5-oxo-5,6-dihydroindolo-(1,2-a)quinazolin-7-yl]acetic acid (IQA).
Stefania Sarno;Erika De Moliner;Maria Ruzzene;Mario A. Pagano.
Biochemical Journal (2003)
Structure of Two Iron-binding Proteins from Bacillus anthracis
Elena Papinutto;William George Dundon;N Pitulis;Roberto Battistutta.
Journal of Biological Chemistry (2002)
Bicyclic peptide inhibitor reveals large contact interface with a protease target.
Alessandro Angelini;Laura Cendron;Shiyu Chen;Jeremy Touati.
ACS Chemical Biology (2012)
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