Palma Mangione

Scopus Publications

Role of extracellular space and matrix remodeling in cardiac amyloidosis
Francesca Lavatelli, Loredana Marchese, Palma Patrizia Mangione, Sara Raimondi, Diana Canetti, et al.
Matrix Biology, 2025
Design and Mechanistic Analysis of a Potent Bivalent Inhibitor of Transthyretin Amyloid Fibrillogenesis
P. Patrizia Mangione, Guglielmo Verona, Cristina Cantarutti, Paola Nocerino, Maria Chiara Mimmi, et al.
Journal of Medicinal Chemistry, 2025
Transthyretin amyloidosis (ATTR) is a systemic disease that primarily affects the heart and the peripheral nervous system. Despite available therapeutic options, advanced ATTR amyloidosis still presents unmet medical needs. We have therefore focused on the design of bivalent small molecules starting from our prototype palindromic ligand mds84, whose binding by transthyretin (TTR) greatly improves stability of the native structure by overcoming the negative cooperativity which is typical of monovalent stabilizers. Among the newly designed compounds here, we present B26, which is pseudoirreversibly bound by native TTR with faster entry kinetics into the protein molecule compared to mds84. It retains the ability to inhibit fibril formation in vitro, together with improved solubility. Using solution NMR, we show that B26 occupies both TTR binding sites simultaneously, leading to conformational effects distant from the binding site, including the proteolytic cleavage site involved in fibril formation by the mechano-enzymatic mechanism.
Truncation of the constant domain drives amyloid formation by immunoglobulin light chains
Francesca Lavatelli, Antonino Natalello, Loredana Marchese, Diletta Ami, Alessandra Corazza, et al.
Journal of Biological Chemistry, 2024
Degradation versus fibrillogenesis, two alternative pathways modulated by seeds and glycosaminoglycans
Guglielmo Verona, Sara Raimondi, Diana Canetti, P. Patrizia Mangione, Loredana Marchese, et al.
Protein Science, 2024
The mechanism that converts native human transthyretin into amyloid fibrils in vivo is still a debated and controversial issue. Commonly, non‐physiological conditions of pH, temperature, or organic solvents are used in in vitro models of fibrillogenesis of globular proteins. Transthyretin amyloid formation can be achieved under physiological conditions through a mechano‐enzymatic mechanism involving specific serine proteases such as trypsin or plasmin. Here, we investigate S52P and L111M transthyretin variants, both causing a severe form of systemic amyloidosis mostly targeting the heart at a relatively young age with heterogeneous phenotype among patients. Our studies on thermodynamics show that both proteins are significantly less stable than other amyloidogenic variants. However, despite a similar thermodynamic stability, L111M variant seems to have enhanced susceptibility to cleavage and a lower tendency to form fibrils than S52P in the presence of specific proteases and biomechanical forces. Heparin strongly enhances the fibrillogenic capacity of L111M transthyretin, but has no effect on the S52P variant. Fibrillar seeds similarly affect the fibrillogenesis of both proteins, with a stronger effect on the L111M variant. According to our model of mechano‐enzymatic fibrillogenesis, both full‐length and truncated monomers, released after the first cleavage, can enter into fibrillogenesis or degradation pathways. Our findings show that the kinetics of the two processes can be affected by several factors, such as intrinsic amyloidogenicity due to the specific mutations, environmental factors including heparin and fibrillar seeds that significantly accelerate the fibrillogenic pathway.
Human wild-type and D76N β2-microglobulin variants are significant proteotoxic and metabolic stressors for transgenic C. elegans
Sara Raimondi, Giulia Faravelli, Paola Nocerino, Valentina Mondani, Alma Baruffaldi, et al.
FASEB Bioadvances, 2023
β2‐microglobulin (β2‐m) is a plasma protein derived from physiological shedding of the class I major histocompatibility complex (MHCI), causing human systemic amyloidosis either due to persistently high concentrations of the wild‐type (WT) protein in hemodialyzed patients, or in presence of mutations, such as D76N β2‐m, which favor protein deposition in the adulthood, despite normal plasma levels. Here we describe a new transgenic Caenorhabditis elegans (C. elegans) strain expressing human WT β2‐m at high concentrations, mimicking the condition that underlies dialysis‐related amyloidosis (DRA) and we compare it to a previously established strain expressing the highly amyloidogenic D76N β2‐m at lower concentrations. Both strains exhibit behavioral defects, the severity of which correlates with β2‐m levels rather than with the presence of mutations, being more pronounced in WT β2‐m worms. β2‐m expression also has a deep impact on the nematodes' proteomic and metabolic profiles. Most significantly affected processes include protein degradation and stress response, amino acids metabolism, and bioenergetics. Molecular alterations are more pronounced in worms expressing WT β2‐m at high concentration compared to D76N β2‐m worms. Altogether, these data show that β2‐m is a proteotoxic protein in vivo also in its wild‐type form, and that concentration plays a key role in modulating pathogenicity. Our transgenic nematodes recapitulate the distinctive features subtending DRA compared to hereditary β2‐m amyloidosis (high levels of non‐mutated β2‐m vs. normal levels of variant β2‐m) and provide important clues on the molecular bases of these human diseases.
Calcium Binds to Transthyretin with Low Affinity
Cristina Cantarutti, Maria Chiara Mimmi, Guglielmo Verona, Walter Mandaliti, Graham W. Taylor, et al.
Biomolecules, 2022
The plasma protein transthyretin (TTR), a transporter for thyroid hormones and retinol in plasma and cerebrospinal fluid, is responsible for the second most common type of systemic (ATTR) amyloidosis either in its wild type form or as a result of destabilizing genetic mutations that increase its aggregation propensity. The association between free calcium ions (Ca2+) and TTR is still debated, although recent work seems to suggest that calcium induces structural destabilization of TTR and promotes its aggregation at non-physiological low pH in vitro. We apply high-resolution NMR spectroscopy to investigate calcium binding to TTR showing the formation of labile interactions, which leave the native structure of TTR substantially unaltered. The effect of calcium binding on TTR-enhanced aggregation is also assessed at physiological pH through the mechano-enzymatic mechanism. Our results indicate that, even if the binding is weak, about 7% of TTR is likely to be Ca2+-bound in vivo and therefore more aggregation prone as we have shown that this interaction is able to increase the protein susceptibility to the proteolytic cleavage that leads to aggregation at physiological pH. These events, even if involving a minority of circulating TTR, may be relevant for ATTR, a pathology that takes several decades to develop.
Amyloid Formation by Globular Proteins: The Need to Narrow the Gap Between in Vitro and in Vivo Mechanisms
Giulia Faravelli, Valentina Mondani, P. Patrizia Mangione, Sara Raimondi, Loredana Marchese, et al.
Frontiers in Molecular Biosciences, 2022
The globular to fibrillar transition of proteins represents a key pathogenic event in the development of amyloid diseases. Although systemic amyloidoses share the common characteristic of amyloid deposition in the extracellular matrix, they are clinically heterogeneous as the affected organs may vary. The observation that precursors of amyloid fibrils derived from circulating globular plasma proteins led to huge efforts in trying to elucidate the structural events determining the protein metamorphosis from their globular to fibrillar state. Whereas the process of metamorphosis has inspired poets and writers from Ovid to Kafka, protein metamorphism is a more recent concept. It is an ideal metaphor in biochemistry for studying the protein folding paradigm and investigating determinants of folding dynamics. Although we have learned how to transform both normal and pathogenic globular proteins into fibrillar polymers in vitro, the events occurring in vivo, are far more complex and yet to be explained. A major gap still exists between in vivo and in vitro models of fibrillogenesis as the biological complexity of the disease in living organisms cannot be reproduced at the same extent in the test tube. Reviewing the major scientific attempts to monitor the amyloidogenic metamorphosis of globular proteins in systems of increasing complexity, from cell culture to human tissues, may help to bridge the gap between the experimental models and the actual pathological events in patients.
Plasmin activity promotes amyloid deposition in a transgenic model of human transthyretin amyloidosis
Ivana Slamova, Rozita Adib, Stephan Ellmerich, Michal R. Golos, Janet A. Gilbertson, et al.
Nature Communications, 2021
Cardiac ATTR amyloidosis, a serious but much under-diagnosed form of cardiomyopathy, is caused by deposition of amyloid fibrils derived from the plasma protein transthyretin (TTR), but its pathogenesis is poorly understood and informative in vivo models have proved elusive. Here we report the generation of a mouse model of cardiac ATTR amyloidosis with transgenic expression of human TTRS52P. The model is characterised by substantial ATTR amyloid deposits in the heart and tongue. The amyloid fibrils contain both full-length human TTR protomers and the residue 49-127 cleavage fragment which are present in ATTR amyloidosis patients. Urokinase-type plasminogen activator (uPA) and plasmin are abundant within the cardiac and lingual amyloid deposits, which contain marked serine protease activity; knockout of α2-antiplasmin, the physiological inhibitor of plasmin, enhances amyloid formation. Together, these findings indicate that cardiac ATTR amyloid deposition involves local uPA-mediated generation of plasmin and cleavage of TTR, consistent with the previously described mechano-enzymatic hypothesis for cardiac ATTR amyloid formation. This experimental model of ATTR cardiomyopathy has potential to allow further investigations of the factors that influence human ATTR amyloid deposition and the development of new treatments.
Clinical ApoA-IV amyloid is associated with fibrillogenic signal sequence
Diana Canetti, Paola Nocerino, Nigel B Rendell, Nicola Botcher, Janet A Gilbertson, et al.
Journal of Pathology, 2021
Apolipoprotein A‐IV amyloidosis is an uncommon form of the disease normally resulting in renal and cardiac dysfunction. ApoA‐IV amyloidosis was identified in 16 patients attending the National Amyloidosis Centre and in eight clinical samples received for histology review. Unexpectedly, proteomics identified the presence of ApoA‐IV signal sequence residues (p.18‐43 to p.20‐43) in 16/24 trypsin‐digested amyloid deposits but in only 1/266 non‐ApoA‐IV amyloid samples examined. These additional signal residues were also detected in the cardiac sample from the Swedish patient in which ApoA‐IV amyloid was first described, and in plasma from a single cardiac ApoA‐IV amyloidosis patient. The most common signal‐containing peptide observed in ApoA‐IV amyloid, p.20‐43, and to a far lesser extent the N‐terminal peptide, p.21‐43, were fibrillogenic in vitro at physiological pH, generating Congo red‐positive fibrils. The addition of a single signal‐derived alanine residue to the N‐terminus has resulted in markedly increased fibrillogenesis. If this effect translates to the mature circulating protein in vivo, then the presence of signal may result in preferential deposition as amyloid, perhaps acting as seed for the main circulating native form of the protein; it may also influence other ApoA‐IV‐associated pathologies. © 2021 The Authors. The Journal of Pathology published by John Wiley & Sons, Ltd. on behalf of The Pathological Society of Great Britain and Ireland.
Comparative study of the stabilities of synthetic in vitro and natural ex vivo transthyretin amyloid fibrils
Sara Raimondi, P. Patrizia Mangione, Guglielmo Verona, Diana Canetti, Paola Nocerino, et al.
Journal of Biological Chemistry, 2020
Systemic amyloidosis caused by extracellular deposition of insoluble fibrils derived from the pathological aggregation of circulating proteins, such as transthyretin, is a severe and usually fatal condition. Elucidation of the molecular pathogenic mechanism of the disease and discovery of effective therapies still represents a challenging medical issue. The in vitro preparation of amyloid fibrils that exhibit structural and biochemical properties closely similar to those of natural fibrils is central to improving our understanding of the biophysical basis of amyloid formation in vivo and may offer an important tool for drug discovery. Here, we compared the morphology and thermodynamic stability of natural transthyretin fibrils with those of fibrils generated in vitro either using the common acidification procedure or primed by limited selective cleavage by plasmin. The free energies for fibril formation were −12.36, −8.10, and −10.61 kcal mol−1, respectively. The fibrils generated via plasmin cleavage were more stable than those prepared at low pH and were thermodynamically and morphologically similar to natural fibrils extracted from human amyloidotic tissue. Determination of thermodynamic stability is an important tool that is complementary to other methods of structural comparison between ex vivo fibrils and fibrils generated in vitro. Our finding that fibrils created via an in vitro amyloidogenic pathway are structurally similar to ex vivo human amyloid fibrils does not necessarily establish that the fibrillogenic pathway is the same for both, but it narrows the current knowledge gap between in vitro models and in vivo pathophysiology.
Lysozyme amyloid: evidence for the W64R variant by proteomics in the absence of the wild type protein
Alexandra Moura, Paola Nocerino, Janet A. Gilbertson, Nigel B. Rendell, P. Patrizia Mangione, et al.
Amyloid, 2020
Diagnostic amyloid proteomics: Experience of the UK National Amyloidosis Centre
Diana Canetti, Nigel B. Rendell, Janet A. Gilbertson, Nicola Botcher, Paola Nocerino, et al.
Clinical Chemistry and Laboratory Medicine, 2020
C. elegans expressing D76N β2-microglobulin: a model for in vivo screening of drug candidates targeting amyloidosis
Giulia Faravelli, Sara Raimondi, Loredana Marchese, Frederick A. Partridge, Cristina Soria, et al.
Scientific Reports, 2019
Binding of Monovalent and Bivalent Ligands by Transthyretin Causes Different Short- And Long-Distance Conformational Changes
Alessandra Corazza, Guglielmo Verona, Christopher A. Waudby, P. Patrizia Mangione, Ryan Bingham, et al.
Journal of Medicinal Chemistry, 2019
Proteomic Analysis for the Diagnosis of Fibrinogen Aα-chain Amyloidosis
Graham W. Taylor, Janet A. Gilbertson, Rabya Sayed, Angel Blanco, Nigel B. Rendell, et al.
Kidney International Reports, 2019
The complementary role of histology and proteomics for diagnosis and typing of systemic amyloidosis
Tamer Rezk, Janet A Gilbertson, P Patrizia Mangione, Dorota Rowczenio, Nigel B Rendell, et al.
Journal of Pathology Clinical Research, 2019
Plasminogen activation triggers transthyretin amyloidogenesis in vitro
P. Patrizia Mangione, Guglielmo Verona, Alessandra Corazza, Julien Marcoux, Diana Canetti, et al.
Journal of Biological Chemistry, 2018
Short-chain alkanethiol coating for small-size gold nanoparticles supporting protein stability
Cristina Cantarutti, Paolo Bertoncin, Alessandra Corazza, Sofia Giorgetti, P. Mangione, et al.
Magnetochemistry, 2017
Misidentification of transthyretin and immunoglobulin variants by proteomics due to methyl lysine formation in formalin-fixed paraffin-embedded amyloid tissue
Diana Canetti, Nigel Brian Rendell, Lucia Di Vagno, Janet A. Gilbertson, Dorota Rowczenio, et al.
Amyloid, 2017
Increasing the accuracy of proteomic typing by decellularisation of amyloid tissue biopsies
P. Patrizia Mangione, Giuseppe Mazza, Janet A. Gilbertson, Nigel B. Rendell, Diana Canetti, et al.
Journal of Proteomics, 2017
Citrate-stabilized gold nanoparticles hinder fibrillogenesis of a pathological variant of β2-microglobulin
Cristina Cantarutti, Sara Raimondi, Giorgia Brancolini, Alessandra Corazza, Sofia Giorgetti, et al.
Nanoscale, 2017
Antiamyloidogenic and proamyloidogenic chaperone effects of C-reactive protein and serum amyloid P component
Daisaku Ozawa, Ryo Nomura, P. Patrizia Mangione, Kazuhiro Hasegawa, Tadakazu Okoshi, et al.
Amyloid, 2017
Inhibition of the mechano-enzymatic amyloidogenesis of transthyretin: Role of ligand affinity, binding cooperativity and occupancy of the inner channel
Guglielmo Verona, P. Patrizia Mangione, Sara Raimondi, Sofia Giorgetti, Giulia Faravelli, et al.
Scientific Reports, 2017
A specific nanobody prevents amyloidogenesis of D76N β2- microglobulin in vitro and modifies its tissue distribution in vivo
Sara Raimondi, Riccardo Porcari, P. Patrizia Mangione, Guglielmo Verona, Julien Marcoux, et al.
Scientific Reports, 2017
Multifaceted anti-amyloidogenic and pro-amyloidogenic effects of C-reactive protein and serum amyloid P component in vitro
Daisaku Ozawa, Ryo Nomura, P. Patrizia Mangione, Kazuhiro Hasegawa, Tadakazu Okoshi, et al.
Scientific Reports, 2016
Co-fibrillogenesis of wild-type and D76N β2-microglobulin: The crucial role of fibrillar seeds
Antonino Natalello, P. Patrizia Mangione, Sofia Giorgetti, Riccardo Porcari, Loredana Marchese, et al.
Journal of Biological Chemistry, 2016
D25V apolipoprotein C-III variant causes dominant hereditary systemic amyloidosis and confers cardiovascular protective lipoprotein profile
Sophie Valleix, Guglielmo Verona, Noémie Jourde-Chiche, Brigitte Nédelec, P. Patrizia Mangione, et al.
Nature Communications, 2016
Amyloid persistence in decellularized liver: Biochemical and histopathological characterization
Giuseppe Mazza, J. Paul Simons, Raya Al-Shawi, Stephan Ellmerich, Luca Urbani, et al.
Amyloid, 2016
Decoding the structural bases of D76N β2-microglobulin high amyloidogenicity through crystallography and asn-scan mutagenesis
Matteo de Rosa, Alberto Barbiroli, Sofia Giorgetti, Patrizia P. Mangione, Martino Bolognesi, et al.
Plos One, 2015
Enhanced toxicity of silver nanoparticles in transgenic Caenorhabditis elegans expressing amyloidogenic proteins
Cristina Soria, Teresa Coccini, Uliana De Simone, Loredana Marchese, Irene Zorzoli, et al.
Amyloid, 2015
Capillary electrophoresis analysis of different variants of the amyloidogenic protein β2-microglobulin as a simple tool for misfolding and stability studies
Laura Bertoletti, Federica Bisceglia, Raffaella Colombo, Sofia Giorgetti, Sara Raimondi, et al.
Electrophoresis, 2015
A novel mechano-enzymatic cleavage mechanism underlies transthyretin amyloidogenesis
Julien Marcoux, P Patrizia Mangione, Riccardo Porcari, Matteo T Degiacomi, Guglielmo Verona, et al.
EMBO Molecular Medicine, 2015
Bifunctional crosslinking ligands for transthyretin
P. Patrizia Mangione, Stéphanie Deroo, Stephan Ellmerich, Vittorio Bellotti, Simon Kolstoe, et al.
Open Biology, 2015
The H50Q mutation induces a 10-fold decrease in the solubility of α-synuclein
Riccardo Porcari, Christos Proukakis, Christopher A. Waudby, Benedetta Bolognesi, P. Patrizia Mangione, et al.
Journal of Biological Chemistry, 2015
Class I major histocompatibility complex, the Trojan Horse for secretion of Amyloidogenic β2-Microglobulin
Levon Halabelian, Stefano Ricagno, Sofia Giorgetti, Carlo Santambrogio, Alberto Barbiroli, et al.
Journal of Biological Chemistry, 2014
Proteolytic cleavage of Ser52Pro variant transthyretin triggers its amyloid fibrillogenesis
P. Patrizia Mangione, Riccardo Porcari, Julian D. Gillmore, Piero Pucci, Maria Monti, et al.
Proceedings of the National Academy of Sciences of the United States of America, 2014
Structure, folding dynamics, and amyloidogenesis of D76N β2-microglobulin roles of shear flow, hydrophobic surfaces, and α-crystallin
P. Patrizia Mangione, Gennaro Esposito, Annalisa Relini, Sara Raimondi, Riccardo Porcari, et al.
Journal of Biological Chemistry, 2013
Pathogenetic mechanisms of amyloid A amyloidosis
J. Paul Simons, Raya Al-Shawi, Stephan Ellmerich, Ivana Speck, Samrina Aslam, et al.
Proceedings of the National Academy of Sciences of the United States of America, 2013
Benefit of doxycycline treatment on articular disability caused by dialysis related amyloidosis
Giovanni Montagna, Benedetta Cazzulani, Laura Obici, Carla Uggetti, Sofia Giorgetti, et al.
Amyloid, 2013
Monitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers
Gennaro Esposito, Megan Garvey, Vera Alverdi, Fabio Pettirossi, Alessandra Corazza, et al.
Journal of Biological Chemistry, 2013
Distribution and determinants of circulating complement factor H concentration determined by a high-throughput immunonephelometric assay
Reecha Sofat, P. Patrizia Mangione, J. Ruth Gallimore, Svetlana Hakobyan, Timothy R. Hughes, et al.
Journal of Immunological Methods, 2013
C. elegans Expressing Human β2-Microglobulin: A Novel Model for Studying the Relationship between the Molecular Assembly and the Toxic Phenotype
Luisa Diomede, Cristina Soria, Margherita Romeo, Sofia Giorgetti, Loredana Marchese, et al.
Plos One, 2012
Isolation and characterization of pharmaceutical grade human pentraxins, serum amyloid P component and C-reactive protein, for clinical use
Mark B. Pepys, J. Ruth Gallimore, Joanne Lloyd, Zhanhong Li, David Graham, et al.
Journal of Immunological Methods, 2012
Hereditary systemic amyloidosis due to Asp76Asn variant β2-microglobulin
Sophie Valleix, Julian D. Gillmore, Frank Bridoux, Palma P. Mangione, Ahmet Dogan, et al.
New England Journal of Medicine, 2012
Effects of the known pathogenic mutations on the aggregation pathway of the amyloidogenic peptide of apolipoprotein A-I
Sara Raimondi, Fulvio Guglielmi, Sofia Giorgetti, Sonia Di Gaetano, Angela Arciello, et al.
Journal of Molecular Biology, 2011
Effect of tetracyclines on the dynamics of formation and destructuration of β2-microglobulin amyloid fibrils
Sofia Giorgetti, Sara Raimondi, Katiuscia Pagano, Annalisa Relini, Monica Bucciantini, et al.
Journal of Biological Chemistry, 2011
Structural basis of ligand specificity in the human pentraxins, C-reactive protein and serum amyloid P component
Halina Mikolajek, Simon E. Kolstoe, Valerie E. Pye, Palma Mangione, Mark B. Pepys, et al.
Journal of Molecular Recognition, 2011
The intracellular quality control system down-regulates the secretion of amyloidogenic apolipoprotein A-I variants: A possible impact on the natural history of the disease
Marta Marchesi, Cinzia Parolini, Caterina Valetti, Palma Mangione, Laura Obici, et al.
Biochimica Et Biophysica Acta Molecular Basis of Disease, 2011
The two tryptophans of 2-microglobulin have distinct roles in function and folding and might represent two independent responses to evolutionary pressure
Sara Raimondi, Nicola Barbarini, Palma Mangione, Gennaro Esposito, Stefano Ricagno, et al.
BMC Evolutionary Biology, 2011
Trapping of palindromic ligands within native transthyretin prevents amyloid formation
Simon E. Kolstoe, Palma P. Mangione, Vittorio Bellotti, Graham W. Taylor, Glenys A. Tennent, et al.
Proceedings of the National Academy of Sciences of the United States of America, 2010
Antibodies to human serum amyloid P component eliminate visceral amyloid deposits
Karl Bodin, Stephan Ellmerich, Melvyn C. Kahan, Glenys A. Tennent, Andrzej Loesch, et al.
Nature, 2010
Complement factor H binds to denatured rather than to native pentameric C-reactive protein
Svetlana Hakobyan, Claire L. Harris, Carmen W. van den Berg, Maria Carmen Fernandez-Alonso, Elena Goicoechea de Jorge, et al.
Journal of Biological Chemistry, 2008
Sulfonated molecules that bind a partially structured species of β2-microglobulin also influence refolding and fibrillogenesis
Chiara Carazzone, Raffaella Colombo, Milena Quaglia, Palma Mangione, Sara Raimondi, et al.
Electrophoresis, 2008
Recombinant amyloidogenic domain of ApoA-I: Analysis of its fibrillogenic potential
Sonia Di Gaetano, Fulvio Guglielmi, Angela Arciello, Palma Mangione, Maria Monti, et al.
Biochemical and Biophysical Research Communications, 2006
Micro-heterogeneity and aggregation in β2-microglobulin solutions: Effects of temperature, pH, and conformational variant addition
Roberto Piazza, Matteo Pierno, Sara Iacopini, Palma Mangione, Gennaro Esposito, et al.
European Biophysics Journal, 2006
Solution structure of β2-microglobulin and insights into fibrillogenesis
Gennaro Esposito, Alessandra Corazza, Paolo Viglino, Giuliana Verdone, Fabio Pettirossi, et al.
Biochimica Et Biophysica Acta Proteins and Proteomics, 2005
Proteomics of β2-microglobulin amyloid fibrils
Monica Stoppini, Palma Mangione, Maria Monti, Sofia Giorgetti, Loredana Marchese, et al.
Biochimica Et Biophysica Acta Proteins and Proteomics, 2005
β2-Microglobulin isoforms display an heterogeneous affinity for type I collagen
Sofia Giorgetti, Antonio Rossi, Palma Mangione, Sara Raimondi, Sara Marini, et al.
Protein Science, 2005
Properties of Some Variants of Human β2- Microglobulin and Amyloidogenesis
Alessandra Corazza, Fabio Pettirossi, Paolo Viglino, Giuliana Verdone, Julian Garcia, et al.
Journal of Biological Chemistry, 2004
β2-Microglobulin H31Y Variant 3D Structure Highlights the Protein Natural Propensity Towards Intermolecular Aggregation
C Rosano, S Zuccotti, P Mangione, S Giorgetti, V Bellotti, et al.
Journal of Molecular Biology, 2004
Structural and folding dynamic properties of the T70N variant of human lysozyme
Gennaro Esposito, Julian Garcia, Palma Mangione, Sofia Giorgetti, Alessandra Corazza, et al.
Journal of Biological Chemistry, 2003
Preliminary crystallographic characterization of the human β2 microglobulin His31Tyr mutant in a tetrameric assembly
Simone Zuccotti, Camillo Rosano, Palma Mangione, Vittorio Bellotti, Martino Bolognesi
Acta Crystallographica Section D Biological Crystallography, 2003
Conformational switching and fibrillogenesis in the amyloidogenic fragment of apolipoprotein A-I
Alessia Andreola, Vittorio Bellotti, Sofia Giorgetti, Palma Mangione, Laura Obici, et al.
Journal of Biological Chemistry, 2003
Topological investigation of amyloid fibrils obtained from β2-microglobulin
Maria Monti, Serena Principe, Sofia Giorgetti, Palma Mangione, Gianpaolo Merlini, et al.
Protein Science, 2002
The solution structure of human β2-microglobulin reveals the prodromes of its amyloid transition
Giuliana Verdone, Alessandra Corazza, Paolo Viglino, Fabio Pettirossi, Sofia Giorgetti, et al.
Protein Science, 2002
Capillary electrophoresis investigation of a partially unfolded conformation of β2-microglobulin
Ersilia De Lorenzi, Silvia Grossi, Gabriella Massolini, Sofia Giorgetti, Palma Mangione, et al.
Electrophoresis, 2002
A Partially Structured Species of β2-Microglobulin Is Significantly Populated under Physiological Conditions and Involved in Fibrillogenesis
Fabrizio Chiti, Ersilia De Lorenzi, Silvia Grossi, Palma Mangione, Sofia Giorgetti, et al.
Journal of Biological Chemistry, 2001
Amyloid fibrils derived from the apolipoprotein A1 Leu174Ser variant contain elements of ordered helical structure
Palma Mangione, Margaret Sunde, Sofia Giorgetti, Monica Stoppini, Gennaro Esposito, et al.
Protein Science, 2001
Detection of two partially structured species in the folding process of the amyloidogenic protein β2-microglobulin
Fabrizio Chiti, Palma Mangione, Alessia Andreola, Sofia Giorgetti, Massimo Stefani, et al.
Journal of Molecular Biology, 2001
Hepatitis C virus-associated cryoglobulinaemic glomerulonephritis with delayed appearance of monoclonal cryoglobulinaemia [4]
Giovanni Montagna, Valter Piazza, Giovanni Banfi, Vittorio Bellotti, Siro Segagni, et al.
Nephrology Dialysis Transplantation, 2001
Review: Immunoglobulin light chain amyloidosis - The archetype of structural and pathogenic variability
Vittorio Bellotti, Palma Mangione, Giampaolo Merlini
Journal of Structural Biology, 2000
Detection of fragments of β2-microglobulin in amyloid fibrils [5]
Monica Stoppini, Patrizia Arcidiaco, Palma Mangione, Sofia Giorgetti, Diego Brancaccio, et al.
Kidney International, 2000
Affinity capillary electrophoresis is a powerful tool to identify transthyretin binding drugs for potential therapeutic use in amyloidosis
Ersilia De Lorenzi, Chiara Galbusera, Vittorio Bellotti, Palma Mangione, Gabriella Massolini, et al.
Electrophoresis, 2000
Conformational dynamics of the β2-microglobulin C terminal in the cell-membrane-anchored major histocompatibility complex type I
M. Massa, P. Mangione, P. Pignatti, M. Stoppini, G. Zanotti, et al.
Cellular and Molecular Life Sciences, 2000
Removal of the N-terminal hexapeptide from human β2-microglobulin facilities protein aggregation and fibril formation
G. Esposito, R. Michelutti, G. Verdone, P. Viglino, H. Hern ÁNdez, et al.
Protein Science, 2000
Effects of a vitamin E-modified dialyzer (excebrane®) on beta-2-microglobulin structure and removal
Contributions to Nephrology, 1999
Biological activity and pathological implications of misfolded proteins
V. Bellotti, P. Mangione, M. Stoppini
Cellular and Molecular Life Sciences, 1999
The new apolipoprotein A-I variant Leu174 → Ser causes hereditary cardiac amyloidosis, and the amyloid fibrils are constituted by the 93- residue N-terminal polypeptide
Laura Obici, Vittorio Bellotti, Palma Mangione, Monica Stoppini, Eloisa Arbustini, et al.
American Journal of Pathology, 1999
β2-Microglobulin can be refolded into a native state from ex vivo amyloid fibrils
Vittorio Bellotti, Monica Stoppini, Palma Mangione, Margaret Sunde, Carol Robinson, et al.
European Journal of Biochemistry, 1998
Evidence that amyloidogenic light chains undergo antigen-driven selection
Vittorio Perfetti, Paola Ubbiali, Maurizio Colli Vignarelli, Marta Diegoli, Roberta Fasani, et al.
Blood, 1998
Use of anti-(β2 microglobulin) mAb to study formation of amyloid fibrils
Monica Stoppini, Vittorio Bellotti, Palma Mangione, Giampaolo Merlini, Giuseppina Ferri
European Journal of Biochemistry, 1997
Structural and functional characterization of three human immunoglobulin κ light chains with different pathological implications
Vittorio Bellotti, Monica Stoppini, Palma P. Mangione, Alessandro Fornasieri, Li Min, et al.
Biochimica Et Biophysica Acta Molecular Basis of Disease, 1996