His main research concerns Biochemistry, Cell biology, Protein tyrosine phosphatase, Acylphosphatase and Enzyme. His Biochemistry study frequently links to adjacent areas such as Redox. His study in Cell biology is interdisciplinary in nature, drawing from both Integrin, Cell adhesion and Cell growth.
His work is dedicated to discovering how Protein tyrosine phosphatase, Phosphatase are connected with Molecular biology and Tyrosine phosphorylation and other disciplines. His studies in Acylphosphatase integrate themes in fields like Crystallography, Protein aggregation and Protein secondary structure. His research in Enzyme tackles topics such as Stereochemistry which are related to areas like Substrate.
His primary areas of study are Biochemistry, Acylphosphatase, Enzyme, Molecular biology and Phosphatase. His study looks at the intersection of Acylphosphatase and topics like Stereochemistry with Binding site. His work deals with themes such as Amino acid and Mutant, which intersect with Enzyme.
While the research belongs to areas of Phosphatase, Giampietro Ramponi spends his time largely on the problem of Phosphate, intersecting his research to questions surrounding Alkaline phosphatase. As part of one scientific family, he deals mainly with the area of Protein tyrosine phosphatase, narrowing it down to issues related to the Tyrosine phosphorylation, and often Receptor tyrosine kinase. In his study, Growth factor is inextricably linked to Cell growth, which falls within the broad field of Cell biology.
Cell biology, Biochemistry, Acylphosphatase, Tyrosine phosphorylation and Protein tyrosine phosphatase are his primary areas of study. Giampietro Ramponi combines subjects such as Cell adhesion, Cell growth and Platelet-derived growth factor receptor with his study of Cell biology. His Acylphosphatase research is multidisciplinary, incorporating elements of Peptide, Protein secondary structure and Protein folding.
His research integrates issues of Crystallography, Heparan sulfate, Proteomics, Structural biology and Amyloidosis in his study of Protein folding. His Protein tyrosine phosphatase research includes themes of Cadherin, Cysteine and Intracellular. His work carried out in the field of Protein aggregation brings together such families of science as SH3 domain, Homocysteine, Hyperhomocysteinemia and Physiology.
His primary areas of investigation include Cell biology, Biochemistry, Proto-oncogene tyrosine-protein kinase Src, Cell adhesion and Acylphosphatase. His Cell biology course of study focuses on Cell growth and Platelet-derived growth factor receptor. Biochemistry and Redox are frequently intertwined in his study.
Giampietro Ramponi works mostly in the field of Cell adhesion, limiting it down to topics relating to Integrin and, in certain cases, Phosphorylation, Cytoskeleton organization, Actin remodeling, Cytoskeleton and Actin, as a part of the same area of interest. His Acylphosphatase research is multidisciplinary, incorporating perspectives in Protein aggregation, Protein secondary structure and Protein folding. His Protein folding research includes elements of SH3 domain, Structural biology, Physiology and Amyloidosis.
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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases.
Monica Bucciantini;Elisa Giannoni;Fabrizio Chiti;Fabrizio Chiti;Fabiana Baroni.
Rationalization of the effects of mutations on peptide and protein aggregation rates.
Fabrizio Chiti;Massimo Stefani;Niccolò Taddei;Giampietro Ramponi.
Intracellular Reactive Oxygen Species Activate Src Tyrosine Kinase during Cell Adhesion and Anchorage-Dependent Cell Growth
Elisa Giannoni;Francesca Buricchi;Giovanni Raugei;Giampietro Ramponi.
Molecular and Cellular Biology (2005)
Reactive oxygen species as essential mediators of cell adhesion: the oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion.
Paola Chiarugi;Giovambattista Pani;Elisa Giannoni;Letizia Taddei.
Journal of Cell Biology (2003)
Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
Fabrizio Chiti;Martino Calamai;Niccolò Taddei;Massimo Stefani.
Proceedings of the National Academy of Sciences of the United States of America (2002)
The Inactivation Mechanism of Low Molecular Weight Phosphotyrosine-protein Phosphatase by H2O2
Anna Caselli;Riccardo Marzocchini;Guido Camici;Giampaolo Manao.
Journal of Biological Chemistry (1998)
Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation.
Paola Chiarugi;Tania Fiaschi;Maria Letizia Taddei;Doriana Talini.
Journal of Biological Chemistry (2001)
The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase
Xiao-Dong Su;Niccolo' Taddei;Massimo Stefani;Giampietro Ramponi.
Redox Regulation of β-Actin during Integrin-mediated Cell Adhesion
Tania Fiaschi;Giacomo Cozzi;Giovanni Raugei;Lucia Formigli.
Journal of Biological Chemistry (2006)
Redox regulation of anoikis: reactive oxygen species as essential mediators of cell survival.
E Giannoni;F Buricchi;G Grimaldi;M Parri.
Cell Death & Differentiation (2008)
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