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pro vyhledávání: '"Giovanni Gotte"'
Autor:
Giovanni Gotte, Marta Menegazzi
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 13, p 10648 (2023)
Protein self-association is a biologically remarkable event that involves and affects the structural and functional properties of proteins [...]
Externí odkaz:
https://doaj.org/article/08479de861004f8cbc819f69cd83b0df
Autor:
Giovanni Gotte, Elena Butturini, Ilaria Bettin, Irene Noro, Alexander Mahmoud Helmy, Andrea Fagagnini, Barbara Cisterna, Manuela Malatesta
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 19, p 11192 (2022)
Natively monomeric RNase A can oligomerize upon lyophilization from 40% acetic acid solutions or when it is heated at high concentrations in various solvents. In this way, it produces many dimeric or oligomeric conformers through the three-dimensiona
Externí odkaz:
https://doaj.org/article/0656f1027a964094924110523282dabc
Autor:
Marta Menegazzi, Giovanni Gotte
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 12, p 6556 (2022)
The majority of transcribed RNAs do not codify for proteins, nevertheless they display crucial regulatory functions by affecting the cellular protein expression profile. MicroRNAs (miRNAs) and transfer RNA-derived small RNAs (tsRNAs) are effectors of
Externí odkaz:
https://doaj.org/article/efe8b50e4c3043b884be427f8f8ae66d
Autor:
Elisa De Tomi, Rachele Campagnari, Elisa Orlandi, Alessia Cardile, Valentina Zanrè, Marta Menegazzi, Macarena Gomez-Lira, Giovanni Gotte
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 3, p 1647 (2022)
Onconase (ONC) is an amphibian secretory ribonuclease displaying cytostatic and cytotoxic activities against many mammalian tumors, including melanoma. ONC principally damages tRNA species, but also other non-coding RNAs, although its precise targets
Externí odkaz:
https://doaj.org/article/9b3b6e4d438f468d90cf4ff858332fe3
Autor:
Giovanni Gotte, Marta Menegazzi
Publikováno v:
Frontiers in Immunology, Vol 10 (2019)
Ribonucleases (RNases) are a large number of enzymes gathered into different bacterial or eukaryotic superfamilies. Bovine pancreatic RNase A, bovine seminal BS-RNase, human pancreatic RNase 1, angiogenin (RNase 5), and amphibian onconase belong to t
Externí odkaz:
https://doaj.org/article/ee2e205fe80b4815877dec4bad1f043c
Autor:
Sabrina Fasoli, Ilaria Bettin, Riccardo Montioli, Andrea Fagagnini, Daniele Peterle, Douglas V. Laurents, Giovanni Gotte
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 18, p 10068 (2021)
Human Angiogenin (hANG, or ANG, 14.1 kDa) promotes vessel formation and is also called RNase 5 because it is included in the pancreatic-type ribonuclease (pt-RNase) super-family. Although low, its ribonucleolytic activity is crucial for angiogenesis
Externí odkaz:
https://doaj.org/article/fbdb8c86383f490e916310fa40a0a33e
Autor:
Andrea Fagagnini, Miguel Garavís, Irene Gómez-Pinto, Sabrina Fasoli, Giovanni Gotte, Douglas V. Laurents
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 3, p 1439 (2021)
Protein oligomerization is key to countless physiological processes, but also to abnormal amyloid conformations implicated in over 25 mortal human diseases. Human Angiogenin (h-ANG), a ribonuclease A family member, produces RNA fragments that regulat
Externí odkaz:
https://doaj.org/article/0671f20e6b0e41619ad56c0fa19f3bd5
Autor:
Riccardo Montioli, Rachele Campagnari, Sabrina Fasoli, Andrea Fagagnini, Andra Caloiu, Marcello Smania, Marta Menegazzi, Giovanni Gotte
Publikováno v:
Life, Vol 11, Iss 2, p 168 (2021)
Upon oligomerization, RNase A can acquire important properties, such as cytotoxicity against leukemic cells. When lyophilized from 40% acetic acid solutions, the enzyme self-associates through the so-called three-dimensional domain swapping (3D-DS) m
Externí odkaz:
https://doaj.org/article/728fafd679174371a2d75da9c25bd661
Autor:
Antonello Merlino, Giovanni Gotte, Rachele Campagnari, Domenico Loreto, Federica Calzetti, Ilaria Bettin, Marta Menegazzi
Publikováno v:
International Journal of Biological Macromolecules. 191:560-571
Onconase (ONC) is a monomeric amphibian "pancreatic-type" RNase endowed with remarkable anticancer activity. ONC spontaneously forms traces of a dimer (ONC-D) in solution, while larger amounts can be formed when ONC is lyophilized from mildly acidic
Autor:
Andrea Fagagnini, Douglas V. Laurents, Sabrina Fasoli, Giovanni Gotte, Ilaria Bettin, Daniele Peterle, Riccardo Montioli
Publikováno v:
International Journal of Molecular Sciences
Digital.CSIC. Repositorio Institucional del CSIC
instname
International Journal of Molecular Sciences, Vol 22, Iss 10068, p 10068 (2021)
Volume 22
Issue 18
Digital.CSIC. Repositorio Institucional del CSIC
instname
International Journal of Molecular Sciences, Vol 22, Iss 10068, p 10068 (2021)
Volume 22
Issue 18
18 pags., 6 figs., 1 tab.-- This article belongs to the Special Issue Protein Oligomerization
Human Angiogenin (hANG, or ANG, 14.1 kDa) promotes vessel formation and is also called RNase 5 because it is included in the pancreatic-type ribonuclea
Human Angiogenin (hANG, or ANG, 14.1 kDa) promotes vessel formation and is also called RNase 5 because it is included in the pancreatic-type ribonuclea