نتائج البحث - "Veronica Di Antonio"

المساهمون: Alvisi Gualtiero, Paolini Lucia, Contarini Andrea, Zambarda Chiara, Di Antonio Veronica, Colosini Antonella, Mercandelli Nicole, Timmoneri Martina, Palu', Giorgio, Caimi Luigi, Ricotta Dori, Radeghieri Annalisa

مصطلحات موضوعية: Intersectin 1-s, nucleocytoplasmic shuttling, Nuclear envelope, Importin, CMR1

وصف الملف: STAMPA

Relation: info:eu-repo/semantics/altIdentifier/pmid/29599122; info:eu-repo/semantics/altIdentifier/wos/WOS:000432444200005; volume:475; issue:8; firstpage:1455; journal:BIOCHEMICAL JOURNAL; http://hdl.handle.net/11379/505519; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85046896517

الاتاحة: http://hdl.handle.net/11379/505519
https://doi.org/10.1042/BCJ20170897

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9

Molecular requirements for self-interaction of the respiratory syncytial virus matrix protein in living mammalian cells

المؤلفون: Giorgio Palù, Veronica Di Antonio, Reena Ghildyal, Gualtiero Alvisi, Marta Trevisan, Annalisa Radeghieri

المصدر: Viruses; Volume 10; Issue 3; Pages: 109
Viruses
Viruses, Vol 10, Iss 3, p 109 (2018)

مصطلحات موضوعية: Models, Molecular, 0301 basic medicine, Protein Conformation, viruses, Viral budding, 030106 microbiology, lcsh:QR1-502, Intracellular Space, Respiratory Syncytial Virus Infections, Matrix (biology), Virus Replication, lcsh:Microbiology, Article, Virus, Cell Line, law.invention, Viral Matrix Proteins, 03 medical and health sciences, Confocal microscopy, law, Virology, medicine, Animals, Humans, Protein Interaction Domains and Motifs, Respiratory system, Bioluminescence resonance energy transfer (BRET), Sequence Deletion, RSV M protein, virus assembly, confocal microscopy, Viral matrix protein, Chemistry, Virus assembly, Infectious Diseases, medicine.disease, Respiratory Syncytial Viruses, 3. Good health, Protein Transport, 030104 developmental biology, medicine.anatomical_structure, Bronchiolitis, Protein Multimerization, Protein Binding, Respiratory tract

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::301a3359388b2505f99760deb19e79a4
http://hdl.handle.net/11577/3266239

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10

Contribution of the residue at position 4 within classical nuclear localization signals to modulating interaction with importins and nuclear targeting

المؤلفون: Hanieh Ghassabian, Luca Bellucci, Jade K. Forwood, Kate Smith, David A. Jans, Gualtiero Alvisi, Kylie M. Wagstaff, Veronica Di Antonio, Francesco Ciccarese, Giorgio Palù, David R. Thomas, Fabiana Caporuscio

المصدر: Biochimica et biophysica acta. Molecular cell research 1865 (2018): 1114–1129. doi:10.1016/j.bbamcr.2018.05.006
info:cnr-pdr/source/autori:Smith K.M.; Di Antonio V.; Bellucci L.; Thomas D.R.; Caporuscio F.; Ciccarese F.; Ghassabian H.; Wagstaff K.M.; Forwood J.K.; Jans D.A.; Palu G.; Alvisi G./titolo:Contribution of the residue at position 4 within classical nuclear localization signals to modulating interaction with importins and nuclear targeting/doi:10.1016%2Fj.bbamcr.2018.05.006/rivista:Biochimica et biophysica acta. Molecular cell research/anno:2018/pagina_da:1114/pagina_a:1129/intervallo_pagine:1114–1129/volume:1865