Andrea Mozzarelli mainly investigates Stereochemistry, Crystallography, Biochemistry, Ligand and Allosteric regulation. Her studies deal with areas such as Pyridoxal, Active site, Protein ligand, Protein quaternary structure and Binding site as well as Stereochemistry. Her Crystallography research incorporates elements of Ion, Bohr effect and Hemoglobin.
Her work on Structure–activity relationship and Rigor mortis is typically connected to Cell type and Meat tenderness as part of general Biochemistry study, connecting several disciplines of science. Her Ligand study integrates concerns from other disciplines, such as Computational chemistry, Molecule, Force field and Plasma protein binding. Andrea Mozzarelli combines subjects such as Protein structure, Oxygen binding and Tryptophan synthase with her study of Allosteric regulation.
Stereochemistry, Biochemistry, Hemoglobin, Crystallography and Enzyme are her primary areas of study. Her Stereochemistry research includes themes of Pyridoxal, Cofactor, Active site, Tryptophan synthase and Allosteric regulation. The study incorporates disciplines such as Lyase and Substrate in addition to Active site.
Her Hemoglobin study combines topics from a wide range of disciplines, such as Oxygen and Heme. Her work deals with themes such as Protein structure and Molecule, which intersect with Crystallography. Her research in Oxygen binding intersects with topics in Oxygen transport, Cooperativity and Protein quaternary structure.
Her primary areas of study are Biochemistry, Enzyme, Hemoglobin, Active site and Cysteine. Her research integrates issues of Plasmodium falciparum and Stereochemistry in her study of Enzyme. Her Stereochemistry research is multidisciplinary, relying on both Glycine, Dicarboxylic acid, Cofactor, Malonic acid and Tetramer.
The various areas that Andrea Mozzarelli examines in her Hemoglobin study include Oxidative stress, Oxidative phosphorylation, Pharmacology and Heme. Andrea Mozzarelli has researched Active site in several fields, including Lyase, Mutagenesis, Allosteric regulation and Methionine. Her work investigates the relationship between Cysteine and topics such as Pyridoxal phosphate that intersect with problems in Rational design.
Andrea Mozzarelli mostly deals with Biochemistry, Stereochemistry, Hemoglobin, Enzyme and Serine racemase. Her research on Biochemistry focuses in particular on Cysteine. Her Stereochemistry study combines topics in areas such as Pyridoxal and Dicarboxylic acid.
Her research investigates the link between Hemoglobin and topics such as Oxidative stress that cross with problems in Heme, Oxidative phosphorylation, Western blot, Reagent and Chromogenic. Her Serine racemase research is multidisciplinary, incorporating elements of Glycine, Inhibitory postsynaptic potential, Binding affinities and Allosteric regulation. The concepts of her Allosteric regulation study are interwoven with issues in Crystallography, Serine racemase activity, Binding site and Active site.
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Is cooperative oxygen binding by hemoglobin really understood
William A. Eaton;Eric R. Henry;James Hofrichter;Andrea Mozzarelli.
Nature Structural & Molecular Biology (1999)
Delay time of hemoglobin S polymerization prevents most cells from sickling in vivo
Andrea Mozzarelli;James Hofrichter;William A. Eaton.
Pyridoxal 5-Phosphate Enzymes as Targets for Therapeutic Agents
Alessio Amadasi;Mariarita Bertoldi;Roberto Contestabile;Stefano Bettati.
Current Medicinal Chemistry (2007)
Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity.
Andrea Mattevi;Marco W. Fraaije;Andrea Mozzarelli;Luca Olivi.
Structures of gamma-aminobutyric acid (GABA) aminotransferase, a pyridoxal 5'-phosphate, and [2Fe-2S] cluster-containing enzyme, complexed with gamma-ethynyl-GABA and with the antiepilepsy drug vigabatrin.
Paola Storici;Daniela De Biase;Francesco Bossa;Stefano Bruno.
Journal of Biological Chemistry (2004)
Simple, intuitive calculations of free energy of binding for protein-ligand complexes. 1. Models without explicit constrained water.
Pietro Cozzini;Micaela Fornabaio;Anna Marabotti;Donald J. Abraham.
Journal of Medicinal Chemistry (2002)
"Muscle to meat" molecular events and technological transformations: The proteomics insight ☆
Gianluca Paredi;Samanta Raboni;Emøke Bendixen;André M. de Almeida.
Journal of Proteomics (2012)
T State Hemoglobin Binds Oxygen Noncooperatively with Allosteric Effects of Protons, Inositol Hexaphosphate, and Chloride
Stefano Bettati;Andrea Mozzarelli.
Journal of Biological Chemistry (1997)
Oxygen binding by single crystals of hemoglobin.
Claudio Rivetti;Andrea Mozzarelli;Gian Luigi Rossi;Eric R. Henry.
PROTEIN FUNCTION IN THE CRYSTAL
Andrea Mozzarelli;Gian Luigi Rossi.
Annual Review of Biophysics and Biomolecular Structure (1996)
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