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    • Plusieurs versions

    A peptide extension dictates IgM assembly

    Pasalic, Dzana, Weber, Benedikt, Giannone, Chiara, Anelli, Tiziana, Müller, Roger, Fagioli, Claudio, Felkl, Manuel, John, Christine, Mossuto, Maria Francesca, Becker, Christian F W, Sitia, Roberto, Buchner, Johannes
    Proceedings of the National Academy of Sciences of the United States of America, 10 October 2017, Vol.114(41), pp.E8575-E8584 [Revue évaluée par les pairs]

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    Variation in employment rates of provisionally admitted foreigners across Swiss cantons and a comparison of their individual experiences

    Giannone, Chiara
    Neuchâtel : [éditeur non identifié]
    2019
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    Titre: Variation in employment rates of provisionally admitted foreigners across Swiss cantons and a comparison of their individual experiences / Chiara Giannone
    Auteur: Giannone, Chiara
    Editeur: Neuchâtel : [éditeur non identifié]
    Date: 2019
    Collation: 92 f. : ill
    Note: Mémoire de master Université de Neuchâtel, 2019
    Classification: neu-sfm Switzerland
    neu-sfm Access to employment
    neu-sfm F Permit
    neu-sfm Comparative analysis
    No RERO: R008930668
    Permalien:
    http://data.rero.ch/01-R008930668/html?view=NJ_V1

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    Roles of N-glycans in the polymerization-dependent aggregation of mutant Ig-μ chains in the early secretory pathway

    Giannone, Chiara, Fagioli, Claudio, Valetti, Caterina, Sitia, Roberto, Anelli, Tiziana
    Scientific reports, 03 February 2017, Vol.7, pp.41815 [Revue évaluée par les pairs]
    MEDLINE/PubMed (U.S. National Library of Medicine)
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    Titre: Roles of N-glycans in the polymerization-dependent aggregation of mutant Ig-μ chains in the early secretory pathway
    Auteur: Giannone, Chiara; Fagioli, Claudio; Valetti, Caterina; Sitia, Roberto; Anelli, Tiziana
    Sujet: Protein Aggregates ; Protein Multimerization ; Secretory Pathway ; Immunoglobulin M -- Metabolism ; Immunoglobulin Mu-Chains -- Metabolism ; Polysaccharides -- Metabolism
    Description: The polymeric structure of secretory IgM allows efficient antigen binding and complement fixation. The available structural models place the N-glycans bound to asparagines 402 and 563 of Ig-μ chains within a densely packed core of native IgM. These glycans are found in the high mannose state also in secreted IgM, suggesting that polymerization hinders them to Golgi processing enzymes. Their absence alters polymerization. Here we investigate their role following the fate of aggregation-prone mutant μ chains lacking the Cμ1 domain (μ∆). Our data reveal that μ∆ lacking 563 glycans (μ∆5) form larger intracellular aggregates than μ∆ and are not secreted. Like μ∆, they sequester ERGIC-53, a lectin previously shown to promote polymerization. In contrast, μ∆ lacking 402 glycans (μ∆4) remain detergent soluble and accumulate in the ER, as does a double mutant devoid of both (μ∆4-5). These results suggest that the two C-terminal Ig-μ glycans shape the polymerization-dependent aggregation by engaging...
    Fait partie de: Scientific reports, 03 February 2017, Vol.7, pp.41815
    Identifiant: 2045-2322 (E-ISSN); 28157181 Version (PMID); 10.1038/srep41815 (DOI)

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    Atypical IgM on T cells predict relapse and steroid dependence in idiopathic nephrotic syndrome

    Colucci, Manuela, Carsetti, Rita, Rosado, Maria Manuela, Cascioli, Simona, Bruschi, Maurizio, Candiano, Giovanni, Corpetti, Giorgia, Giardino, Laura, Serafinelli, Jessica, Giannone, Chiara, Ghiggeri, Gian Marco, Rastaldi, Maria Pia, Sitia, Roberto, Emma, Francesco, Vivarelli, Marina
    Kidney International, October 2019, Vol.96(4), pp.971-982 [Revue évaluée par les pairs]