A5032609098- Protein Structure and Dynamics
- Alzheimer's disease research and treatments
- Enzyme Structure and Function
- Biochemical and Molecular Research
- Prion Diseases and Protein Misfolding
- Endoplasmic Reticulum Stress and Disease
- Psoriasis: Treatment and Pathogenesis
- melanin and skin pigmentation
- Protein Tyrosine Phosphatases
- Blood properties and coagulation
- Alkaline Phosphatase Research Studies
- Photosynthetic Processes and Mechanisms
- Enzyme function and inhibition
- Amyloidosis: Diagnosis, Treatment, Outcomes
- Ocular Diseases and Behçet’s Syndrome
- Skin Protection and Aging
- Protein Kinase Regulation and GTPase Signaling
- Glycosylation and Glycoproteins Research
- Sirtuins and Resveratrol in Medicine
- Atherosclerosis and Cardiovascular Diseases
- Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- ATP Synthase and ATPases Research
- Electrochemical sensors and biosensors
- Inflammasome and immune disorders
- Trace Elements in Health
University of Florence
2016-2025
University of Parma
2016
Don Carlo Gnocchi Foundation
2014
GF Biochemicals (Italy)
2010
Michigan State University
2009
University of Cambridge
2002-2006
University of Oxford
1991-1999
Stockholm University
1998
University of Siena
1991
We have been able to convert a small alpha/beta protein, acylphosphatase, from its soluble and native form into insoluble amyloid fibrils of the type observed in range pathological conditions. This was achieved by allowing slow growth solution containing moderate concentrations trifluoroethanol. When analyzed with electron microscopy, protein aggregate present sample after long incubation times consisted extended, unbranched filaments 30-50 A width that assemble subsequently higher order...
Protein aggregation and the formation of highly insoluble amyloid structures is associated with a range debilitating human conditions, which include Alzheimer's disease, Parkinson's Creutzfeldt–Jakob disease. Muscle acylphosphatase (AcP) has already provided significant insights into mutational changes that modulate formation. In present paper, we have used this system to investigate effects mutations modify charge state protein without affecting significantly hydrophobicity or secondary...
More than 40 human diseases are associated with fibrillar deposits of specific peptides or proteins in tissue. Amyloid fibrils, their precursors, can be highly toxic to cells, suggesting key role disease pathogenesis. Proteins not any able form oligomers and amyloid assemblies vitro displaying structures cytotoxicity comparable those aggregates disease-related polypeptides. In isolated such toxicity has been shown result from increased membrane permeability disruption ion homeostasis...
Background— Behçet disease (BD) is a systemic vasculitis with broad range of organ involvement, characterized by multisystemic, immune-inflammatory disorder involving vessels all sizes and often complicated thrombosis. Systemic redox imbalance circulating neutrophil hyperactivation have been observed in BD patients are thought to be responsible for impaired coagulation. We here focused on the pathogenetic mechanisms potentially linking immune cell activation thrombosis, specifically examined...
Among plasma proteins, fibrinogen represents a major target of oxidative modifications. In patients with post-acute myocardial infarction (6 months after the acute event), oxidation-induced carbonyls and function were estimated using in vitro ex vivo approaches. Fibrinogen structural features clot architecture also explored.In 39 28 age-, sex-, risk factor-matched controls, stress markers (in purified fractions), thrombin-catalyzed fibrin polymerization, plasmin-induced lysis estimated....
Charged polyelectrolytes such as glycosaminoglycans and nucleic acids have frequently been found associated with the proteinaceous deposits in tissues of patients amyloid diseases. We investigated nature generality this phenomenon by studying ability different polyanions, including DNA, ATP, heparin, heparan sulfate, to promote aggregation amyloidogenic proteins bind resulting aggregates. Preformed fibrils human muscle acylphosphatase lysozyme, a net positive charge at physiological pH...
Among the many parameters that have been proposed to promote amyloid fibril formation is pi-stacking of aromatic residues. We studied aggregation several mutants human muscle acylphosphatase in which an residue was substituted with a non-aromatic one. The rate determined using Thioflavin T test under conditions variants populated initially ensemble partially unfolded conformations. Substitutions aggregation-promoting fragments sequence result dramatically decreased protein, confirming...
BackgroundPsoriasis is a chronic hyperproliferative inflammatory skin disease, characterized by generalized redox imbalance. Anti-tumor necrosis factor (TNF)-α therapy widely used for the treatment of this but its effect on blood status hasn't been explored.ObjectiveTo investigate effects anti-TNF-α in psoriatic patients.MethodsTwenty-nine patients (PSO) were divided into two groups: one remained untreated (NRT) and to another was prescribed (TR). The levels main oxidative stress markers...
Abstract Vitiligo is an acquired and progressive hypomelanotic disease that manifests as circumscribed depigmented patches on the skin. The aetiology of vitiligo remains unclear, but recent experimental data underline interactions between melanocytes other typical skin cells, particularly keratinocytes. Our previous results indicate keratinocytes from perilesional show features damaged cells. Sirtuins (silent mating type information regulation 2 homolog) 1, well‐known modulators lifespan in...
Psoriasis, a multisystem chronic disease characterized by abnormal keratinocyte proliferation, has an unclear pathogenesis where systemic inflammation and oxidative stress play mutual roles. Dermal fibroblasts, which are known to provide crucial microenvironment for epidermal function, represented the selected experimental model in our study aimed clarify potential role of SIRT1 pathogenetic mechanisms disease. We firstly detected presence (lipid peroxidation total antioxidant capacity),...
A potentially amyloidogenic protein has to be at least partially unfolded form amyloid aggregates. However, aggregation of the or totally state a is modulated by three other factors: hydrophobicity, propensity secondary structure, and net charge polypeptide chain. We propose evaluate relative importance charge, as opposed factors, on amyloidogenicity. For this aim, we have used two homologous proteins that were previously shown able fibrils in vitro, N-terminal domain HypF from Escherichia...
The HypF N-terminal domain has been found to convert readily from its native globular conformation into protein aggregates with the characteristics of amyloid fibrils associated a variety human diseases. This conversion was achieved by incubation at acidic pH or in presence moderate concentrations trifluoroethanol. Electron microscopy showed that grown trifluoroethanol were predominantly 3-5 nm and 7-9 width, whereas 12-20 width prevailed samples incubated pH. These results indicate assembly...