Výsledky vyhledávání - "Simonetta Bernocco"

Functional Characterization of a Small-Molecule Inhibitor of the DKK1-LRP6 Interaction

Autor: Silvia Pileri, Rosaria Remelli, Daniela Diamanti, Barbara Lelli, Andrea Caricasole, Renza Roncarati, Luisa Bracci, Simonetta Bernocco, Sara Iozzi

Publikováno v: ISRN Molecular Biology

Background. DKK1 antagonizes canonical Wnt signalling through high-affinity binding to LRP5/6, an essential component of the Wnt receptor complex responsible for mediating downstream canonical Wnt signalling. DKK1 overexpression is known for its path

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddf933ab76dbf669d75dfca7dd878e9c
https://doi.org/10.5402/2012/823875

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Sequential detergent fractionation of primary neurons for proteomics studies

Autor: Letizia Magnoni, Roberto Raggiaschi, Georg C. Terstappen, Stefano Gotta, Simonetta Bernocco, Silvia Matteoni, Costanza Fondelli

Publikováno v: PROTEOMICS. 8:930-938

Proteomics studies employing primary neurons are difficult due to the neurons' characteristics. We have developed a detergent-based fractionation method which reduces complexity of the protein extracts, is sufficiently fast to allow differential prot

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5849161e2f53a671559ad3f1d02ea822
https://doi.org/10.1002/pmic.200700738

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Control of Heterotypic Fibril Formation by Collagen V Is Determined by Chain Stoichiometry

Autor: David J.S. Hulmes, Simonetta Bernocco, Robert Garrone, Hélène Chanut-Delalande, Agnès Fichard, Florence Ruggiero

Publikováno v: Journal of Biological Chemistry. 276:24352-24359

Although the collagen V heterotrimer is known to be involved in the control of fibril assembly, the role of the homotrimer in fibrillar organization has not yet been examined. Here, the production of substantial amounts of recombinant collagen V homo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89d85d30da7241217973548565d35a9d
https://doi.org/10.1074/jbc.m101182200

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Folding and activity of recombinant human procollagen C-proteinase enhancer

Autor: David J.S. Hulmes, Laura Moschcovich, Bernard Font, Denise Eichenberger, Efrat Kessler, Simonetta Bernocco, Nor Chejanovsky, Hadassah Rivkin

Publikováno v: European Journal of Biochemistry. 268:2991-2996

Recombinant human procollagen C-proteinase enhancer (rPCPE) was expressed using a baculovirus system and purified to homogeneity using a three-step procedure including heparin affinity chromatography. Heparin binding was dependent on the C-terminal n

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b742025f60eb2929cebcdb348a4b8c32
https://doi.org/10.1046/j.1432-1327.2001.02189.x

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Polymerization of Rod-Like Macromolecular Monomers Studied by Stopped-Flow, Multiangle Light Scattering: Set-Up, Data Processing, and Application to Fibrin Formation

Autor: Carla Cuniberti, Aldo Profumo, Federico Ferri, Simonetta Bernocco, Mattia Rocco

Publikováno v: Biophysical Journal. 79:561-583

Many biological supramolecular structures are formed by polymerization of macromolecular monomers. Light scattering techniques can provide structural information from such systems, if suitable procedures are used to collect the data and then to extra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9b1d4dff8636ef76563da18088f379a
https://doi.org/10.1016/s0006-3495(00)76317-x

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A homogeneous HTRF assay for the identification of inhibitors of the TWEAK-Fn14 protein interaction

Autor: Elisa Mori, Chiara Caramelli, Hanna Axelsson, Laura Maccari, Paola Fanti, Eva Genesio, Johan Schultz, Sara Iozzi, Simonetta Bernocco, Natalia Markova, Tiziana Benicchi, Andreas Svahn, Wolfgang Fecke, Valentina Porcari, Iolanda Micco, Federico Cappelli

Publikováno v: Journal of biomolecular screening. 17(7)

The TWEAK-Fn14 pathway is upregulated in models of inflammation, autoimmune diseases, and cancer. Both TWEAK and Fn14 show increased expression also in the CNS in response to different stimuli, particularly astrocytes, microglia, and neurons, leading

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2729cc80655d647a15e5bf07b29f4c1
https://pubmed.ncbi.nlm.nih.gov/22644269

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Low resolution structure determination shows procollagen C-proteinase enhancer to be an elongated multidomain glycoprotein

Autor: Christine Ebel, Denise Eichenberger, Gilbert Deléage, Sylvie Ricard-Blum, Maxim V. Petoukhov, Christophe Geourjon, Dmitri I. Svergun, Barry M. Steiglitz, Simonetta Bernocco, Florence Ruggiero, David J.S. Hulmes, Daniel S. Greenspan, Bernard Font

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2003, 278 (9), pp.7199-205. ⟨10.1074/jbc.M210857200⟩
Journal of Biological Chemistry, 2003, 278 (9), pp.7199-205. ⟨10.1074/jbc.M210857200⟩

International audience; Procollagen C-proteinase enhancer (PCPE) is an extracellular matrix glycoprotein that can stimulate the action of tolloid metalloproteinases, such as bone morphogenetic protein-1, on a procollagen substrate, by up to 20-fold.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41c5a11fef80792ae98b9380a5fb95a2
https://pubmed.ncbi.nlm.nih.gov/12486138

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Interaction properties of the procollagen C-proteinase enhancer protein shed light on the mechanism of stimulation of BMP-1

Autor: Catherine Moali, Elmar R. Burchardt, Efrat Kessler, David J.S. Hulmes, Michel van der Rest, Sylvie Ricard-Blum, Simonetta Bernocco, Bernard Font, Denise Eichenberger, Jean Farjanel

Procollagen C-proteinase enhancer (PCPE) is an extracellular matrix glycoprotein that binds to the C-propeptide of procollagen I and can enhance the activities of procollagen C-proteinases up to 20-fold. To determine the molecular mechanism of PCPE a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eef21c3722cd2a70fb7af2d47e4dfc44
https://hal.archives-ouvertes.fr/hal-00313822

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Biophysical characterization of the C-propeptide trimer from human procollagen III reveals a tri-lobed structure

Autor: Jean Farjanel, Christine Ebel, Denise Eichenberger, Marlène Mazzorana, Simonetta Bernocco, Stéphanie Finet, David J.S. Hulmes

Publikováno v: The Journal of biological chemistry. 276(52)

Procollagen C-propeptide domains direct chain association during intracellular assembly of procollagen molecules. In addition, they control collagen solubility during extracellular proteolytic processing and fibril formation and interact with cell su

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::103b525d104afd5c33b9b05a6db5a807
https://pubmed.ncbi.nlm.nih.gov/11684689

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Unhydroxylated triple helical collagen I produced in transgenic plants provides new clues on the role of hydroxyproline in collagen folding and fibril formation

Autor: Manfred Theisen, Christine Merle, David J.S. Hulmes, Robert Garrone, Simonetta Bernocco, Patricia Berland, Florence Ruggiero, Stephanie Perret

Publikováno v: The Journal of biological chemistry. 276(47)

Human unhydroxylated homotrimeric triple-helical collagen I produced in transgenic plants was used as an experimental model to provide insights into the role of hydroxyproline in molecular folding and fibril formation. By using chemically cross-linke

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1232d5354daba07a8afcdf7cde102aa
https://pubmed.ncbi.nlm.nih.gov/11557756

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