Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Katia, Maso"'
Autor:
Marino Bellini, Katia Maso, Ilaria Marigo, Antonella Grigoletto, Hiroki Yoshioka, Vincenzo Ingangi, Kamiya Masaki, Midori Hirai, Lucia Raccagni, Akira Suzuki, Gianfranco Pasut
Publikováno v:
Journal of Controlled Release. 324:228-237
Poly(L-glutamic acid)-co-poly(ethylene glycol) block copolymers (PLE-PEG) are here investigated as polymers for conjugation to therapeutic proteins such as granulocyte colony stimulating factor (G-CSF) and human growth hormone (hGH). PLE-PEG block co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2a92e016224131b8a36df32a187b5d3
https://doi.org/10.1016/j.jconrel.2020.05.015
https://doi.org/10.1016/j.jconrel.2020.05.015
Autor:
Isabella Monia Montagner, Katia Maso, Antonella Grigoletto, Oddone Schiavon, Gianfranco Pasut, Antonio Rosato
Publikováno v:
European Journal of Pharmaceutics and Biopharmaceutics. 142:49-60
Antibody drug conjugates (ADCs), which are obtained by coupling a potent cytotoxic agent to a monoclonal antibody (mAb), are traditionally bound in a random way to lysine or cysteine residues, with the final product’s heterogeneity having an import
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e61d82c03243ba634962b9445f357b5d
https://doi.org/10.1016/j.ejpb.2019.06.012
https://doi.org/10.1016/j.ejpb.2019.06.012
Autor:
Amr S. Abu Lila, Rosalía Agusti, Sahar Awwad, Carsten Behrens, Mary J. Bossard, Gunda Brandenburg, Steve Brocchini, Jens Buchardt, Chris Caster, Victor R. de la Rosa, Rosa M. de Lederkremer, Celine Derunes, Nehal E. Elsadek, Elaine L. Ferguson, Marc A. Gauthier, M. Eugenia Giorgi, Kenneth Grabstein, Andrea A. Greschner, Antonella Grigoletto, Richard Hoogenboom, Tatsuhiro Ishida, Waliul Islam, Nandini V. Katre, Hanieh Khalili, Ralf Krähmer, Michael J. LaBarre, Frank Leenders, Gary Li, Kenneth W. Locke, Hiroshi Maeda, Daniel C. Maneval, Katia Maso, Mann Muhsin, Natalie Winblade Nairn, Steffen Nock, Gianfranco Pasut, Christina Picken, Sabine Poppenborg, Christoph Radcke, Sybille Sauter, Ondrej Sedlacek, Rose E. Sekulovich, Kurt D. Shanebeck, Jürgen Siekmann, Joana Stokniene, David W. Thomas, Curtis B. Thompson, Peter L. Turecek, Mathieu Varache, María J. Vicent, Aijun Wang, Julia Wittmann, Ahlem Zaghmi, Samuel Zalipsky, Mire Zloh, Linglong Zou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a5499b541259ce8ea55013fa36b35449
https://doi.org/10.1016/b978-0-444-64081-9.01002-0
https://doi.org/10.1016/b978-0-444-64081-9.01002-0
Until recently, polymer–protein PEGylation has for the most part been characterized by chemical approaches to conjugation, and, in fact, the majority of conjugates approved for human use are based on these protocols. The growing demand for site-sel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::249a6d5a034f7c940aa9e848fa1e62c5
http://hdl.handle.net/11577/3344116
http://hdl.handle.net/11577/3344116
Publikováno v:
International Review of Cell and Molecular Biology
International Review of Cell and Molecular Biology volume 346
International Review of Cell and Molecular Biology volume 346
The targeted delivery of bioactive molecules to the appropriate site of action, one of the critical focuses of pharmaceutical research, improves therapeutic outcomes and increases safety at the same time; a concept envisaged by Ehrlich over 100 years
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b12f0106488b86e4d6ee4f83a5607c6
https://doi.org/10.1016/bs.ircmb.2019.03.001
https://doi.org/10.1016/bs.ircmb.2019.03.001
Autor:
Hiroki Yoshioka, Antonella Grigoletto, Gianfranco Pasut, Antonio Rosato, Katia Maso, Anna Mero
Publikováno v:
Polymer Chemistry. 7:6545-6553
Microbial transglutaminase (mTGase) is an enzyme that catalyzes site-specific protein derivatization at specific glutamines. mTGase-mediated conjugation with PEG-NH2 to granulocyte colony stimulating factor (G-CSF) yields a site selective mono-deriva
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f4d296e9422098f8c3e3324e7c0f4a7
https://doi.org/10.1039/c6py01616b
https://doi.org/10.1039/c6py01616b
Publikováno v:
Advances in protein chemistry and structural biology. 112
Proteins hold a central role in medicine and biology, also confirmed by the several therapeutic applications based on biologic drugs. Such therapies are of great relevance thanks to high potency and safety of proteins. Nevertheless, many proteins as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3560d9c7a5871903bb8ddf20ec7bf694
https://pubmed.ncbi.nlm.nih.gov/29680235
https://pubmed.ncbi.nlm.nih.gov/29680235
Proteins hold a central role in medicine and biology, also confirmed by the several therapeutic applications based on biologic drugs. Such therapies are of great relevance thanks to high potency and safety of proteins. Nevertheless, many proteins as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dae219e994fb8f9254fb64f5e73ed9dd
https://doi.org/10.1016/bs.apcsb.2018.01.003
https://doi.org/10.1016/bs.apcsb.2018.01.003
Publikováno v:
Methods in enzymology. 590
PEGylation, the covalent attachment of polyethylene glycol to bioactive molecules, is one of the leading approaches used to prolong pharmacokinetics, to improve the stability, and to reduce the immunogenicity of therapeutic proteins. PEG-conjugated p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6f14cd02ee7a41835cdba9354a6687a5
https://pubmed.ncbi.nlm.nih.gov/28411643
https://pubmed.ncbi.nlm.nih.gov/28411643
PEGylation, the covalent attachment of polyethylene glycol to bioactive molecules, is one of the leading approaches used to prolong pharmacokinetics, to improve the stability, and to reduce the immunogenicity of therapeutic proteins. PEG-conjugated p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d556089de43496a07ff2bcc59bd1c8b0
http://hdl.handle.net/11577/3226289
http://hdl.handle.net/11577/3226289