5 results on '"Maura Garofalo"'
Search Results
2. Management of transthyretin amyloidosis
- Author
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Adalgisa Condoluci, Marie Théaudin, Rahel Schwotzer, Aju P. Pazhenkottil, Paolo Arosio, Manuela Averaimo, Ulrike Bacher, Peter Bode, Andrea Cavalli, Stefan Dirnhofer, Nadia Djerbi, Stephan Dobner, Thomas Fehr, Maura Garofalo, Ariana Gaspert, Sabine Gerull, Raphael Heimgartner, Annemarie Hübers, Hans H. Jung, Chiara Kessler, Raphael Knöpfel, Natallia Laptseva, Giulia Magini, Robert Manka, Luca Mazzucchelli, Martin Meyer, Violeta Mihaylova, Pierre Monney, Alessio Mylonas, René Nkoulou, Thomas Pabst, Otmar Pfister, Axel Rüfer, Adrian Schmidt, Harald Seeger, Simon F. Stämpfli, Guido Stirnimann, Thomas Suter, Giorgio Treglia, Alexandar Tzankov, Friederike Vetter, Markus Zweier, Andreas J. Flammer, and Bernhard Gerber
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Medicine - Abstract
This article was corrected and republished online on November 4, 2021. Please see Erratum (Swiss Med Wkly. 2021;151:w30104)
- Published
- 2021
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3. Oxidation State Dependent Conformational Changes of HMGB1 Regulate the Formation of the CXCL12/HMGB1 Heterocomplex
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Enrico M.A. Fassi, Jacopo Sgrignani, Gianluca D'Agostino, Valentina Cecchinato, Maura Garofalo, Giovanni Grazioso, Mariagrazia Uguccioni, and Andrea Cavalli
- Subjects
Biotechnology ,TP248.13-248.65 - Abstract
High-mobility Group Box 1 (HMGB1) is an abundant protein present in all mammalian cells and involved in several processes. During inflammation or tissue damage, HMGB1 is released in the extracellular space and, depending on its redox state, can form a heterocomplex with CXCL12. The heterocomplex acts exclusively via the chemokine receptor CXCR4 enhancing leukocyte recruitment.Here, we used multi-microsecond molecular dynamics (MD) simulations to elucidate the effect of the disulfide bond on the structure and dynamics of HMGB1.The results of the MD simulations show that the presence or lack of the disulfide bond between Cys23 and Cys45 modulates the conformational space explored by HMGB1, making the reduced protein more suitable to form a complex with CXCL12. Keywords: HMGB1, CXCL12, Molecular dynamics, Protein-protein docking, Conformational ensemble
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- 2019
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4. Expert recommendation from the Swiss Amyloidosis Network (SAN) for systemic AL-amyloidosis
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Rahel Schwotzer, Andreas J. Flammer, Sabine Gerull, Thomas Pabst, Paolo Arosio, Manuela Averaimo, Ulrike Bacher, Peter Bode, Andrea Cavalli, Adalgisa Condoluci, Stefan Dirnhofer, Nadia Djerbi, Stephan W. Dobner, Thomas Fehr, Maura Garofalo, Ariana Gaspert, Raphael Heimgartner, Annemarie Hübers, Hans H. Jung, Chiara Kessler, Raphael Knöpfel, Natallia Laptseva, Robert Manka, Luca Mazzucchelli, Martin Meyer, Violeta Mihaylova, Pierre Monney, Alessio Mylonas, René Nkoulou, Aju P. Pazhenkottil, Otmar Pfister, Axel Rüfer, Adrian Schmidt, Harald Seeger, Simon F. Stämpfli, Guido Stirnimann, Thomas Suter, Marie Théaudin, Giorgio Treglia, Alexandar Tzankov, Friederike Vetter, Markus Zweier, and Bernhard Gerber
- Subjects
AL amyloidosis ,Swiss Amyloidosis Network ,expert recommendation ,diagnostic work-up and treatment ,Medicine - Abstract
Systemic amyloidosis is a heterogeneous group of diseases associated with protein misfolding into insoluble beta-sheet rich structures that deposit extracellularly in different organs, eventually compromising their function. There are more than 30 different proteins, known to be amyloidogenic with “light chain” (AL)-amyloidosis being the most common type, followed by transthyretin (ATTR)-, and amyloid protein A (AA)-amyloidosis. Systemic amyloidosis is a rare disease with an incidence of around 10 patients in 1 million inhabitants. Recently several new therapeutic options have been developed for subgroups of amyloidosis patients, and the introduction of novel therapies for plasma cell myeloma has led to an increase in the therapeutic armamentarium for plasma cell disorders, including AL amyloidosis. Among them, proteasome inhibitors, immunomodulatory agents (-imids), and monoclonal antibodies have been successfully introduced into clinical practice. Still, high-quality data from randomised controlled trials regarding the benefit of these cost-intensive drugs in AL amyloidosis are widely lacking, and due to the rarity of the disease many physicians will not gain routine experience in the management of these frail patients. The diagnosis of AL amyloidosis relies on a close collaboration between clinicians, pathologists, imaging experts, and sometimes geneticists. Diagnosis and treatment options in this complex disorder should be discussed in dedicated multidisciplinary boards. In January 2020, the first meeting of the Swiss Amyloidosis Network took place in Zurich, Switzerland. One aim of this meeting was to establish a consensus guideline regarding the diagnostic work-up and the treatment recommendations for systemic amyloidosis tailored to the Swiss health care system. Forty-five participants from different fields in medicine discussed many aspects of amyloidosis. These are the Swiss Amyloidosis Network recommendations which focus on diagnostic work-up and treatment of AL-amyloidosis.
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- 2020
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5. Structural Biology of STAT3 and Its Implications for Anticancer Therapies Development
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Jacopo Sgrignani, Maura Garofalo, Milos Matkovic, Jessica Merulla, Carlo V. Catapano, and Andrea Cavalli
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STAT3 ,cancer ,molecular modeling ,drug design ,structural biology ,Biology (General) ,QH301-705.5 ,Chemistry ,QD1-999 - Abstract
Transcription factors are proteins able to bind DNA and induce the transcription of specific genes. Consequently, they play a pivotal role in multiple cellular pathways and are frequently over-expressed or dysregulated in cancer. Here, we will focus on a specific “signal transducer and activator of transcription” (STAT3) factor that is involved in several pathologies, including cancer. For long time, the mechanism by which STAT3 exerts its cellular functions has been summarized by a three steps process: (1) Protein phosphorylation by specific kinases, (2) dimerization promoted by phosphorylation, (3) activation of gene expression by the phosphorylated dimer. Consequently, most of the inhibitors reported in literature aimed at blocking phosphorylation and dimerization. However, recent observations reopened the debate and the entire functional mechanism has been revisited stimulating the scientific community to pursue new inhibition strategies. In particular, the dimerization of the unphosphorylated species has been experimentally demonstrated and specific roles proposed also for these dimers. Despite difficulties in the expression and purification of the full length STAT3, structural biology investigations allowed the determination of atomistic structures of STAT3 dimers and several protein domains. Starting from this information, computational methods have been used both to improve the understanding of the STAT3 functional mechanism and to design new inhibitors to be used as anticancer drugs. In this review, we will focus on the contribution of structural biology to understand the roles of STAT3, to design new inhibitors and to suggest new strategies of pharmacological intervention.
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- 2018
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