What is he best known for?
The fields of study he is best known for:
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.
His most cited work include:
- Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 A resolution. (271 citations)
- Toward the rational design of protein kinase casein kinase-2 inhibitors. (145 citations)
- Three-dimensional structure of recombinant human muscle fatty acid-binding protein. (144 citations)
What are the main themes of his work throughout his whole career to date?
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.
He most often published in these fields:
- Biochemistry (31.93%)
- Stereochemistry (21.75%)
- Crystallography (18.60%)
What were the highlights of his more recent work (between 2012-2021)?
- Biochemistry (31.93%)
- Helicobacter pylori (9.12%)
- Microbiology (7.37%)
In recent papers he was focusing on the following fields of study:
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.
Between 2012 and 2021, his most popular works were:
- Helicobacter pylori secreted peptidyl prolyl cis, trans-isomerase drives Th17 inflammation in gastric adenocarcinoma (90 citations)
- The first non Clostridial botulinum-like toxin cleaves VAMP within the juxtamembrane domain (59 citations)
- A MICU1 Splice Variant Confers High Sensitivity to the Mitochondrial Ca2+ Uptake Machinery of Skeletal Muscle (56 citations)
In his most recent research, the most cited papers focused on:
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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