Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Francesca Collu"'
Autor:
Morena Pappalardo, Francesca Collu, James Macpherson, Martin Michaelis, Franca Fraternali, Mark N. Wass
Publikováno v:
BMC Genomics, Vol 18, Iss S5, Pp 35-45 (2017)
Abstract Background Ebolaviruses have been known to cause deadly disease in humans for 40 years and have recently been demonstrated in West Africa to be able to cause large outbreaks. Four Ebolavirus species cause severe disease associated with high
Externí odkaz:
https://doaj.org/article/49a7942b6ddf4322a922edadc924a74d
Autor:
Jeroen Claus, Gargi Patel, Flavia Autore, Audrey Colomba, Gregory Weitsman, Tanya N Soliman, Selene Roberts, Laura C Zanetti-Domingues, Michael Hirsch, Francesca Collu, Roger George, Elena Ortiz-Zapater, Paul R Barber, Boris Vojnovic, Yosef Yarden, Marisa L Martin-Fernandez, Angus Cameron, Franca Fraternali, Tony Ng, Peter J Parker
Publikováno v:
eLife, Vol 7 (2018)
While targeted therapy against HER2 is an effective first-line treatment in HER2+ breast cancer, acquired resistance remains a clinical challenge. The pseudokinase HER3, heterodimerisation partner of HER2, is widely implicated in the resistance to HE
Externí odkaz:
https://doaj.org/article/05bdc0b657ae488494f7ad21996d47c6
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 5, Iss 6, p e201302008 (2013)
Over-expression of multidrug efflux pumps of the Resistance Nodulation Division (RND) protein super family counts among the main causes for microbial resistance against pharmaceuticals. Understanding the molecular basis of this process is one of the
Externí odkaz:
https://doaj.org/article/8bf2ae7179c84cfba3465c605cfd2925
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e52633 (2012)
Ligand-receptor interactions are at the basis of the mediation of our physiological responses to a large variety of ligands, such as hormones, neurotransmitters and environmental stimulants, and their tuning represents the goal of a large variety of
Externí odkaz:
https://doaj.org/article/c5d8ea647e584af3a48546edae06ef38
Publikováno v:
PLoS Computational Biology, Vol 6, Iss 6, p e1000806 (2010)
The tripartite complex AcrAB-TolC is the major efflux system in Escherichia coli. It extrudes a wide spectrum of noxious compounds out of the bacterium, including many antibiotics. Its active part, the homotrimeric transporter AcrB, is responsible fo
Externí odkaz:
https://doaj.org/article/f09fe10093e74a379063b2e3610e2371
Autor:
Giuseppe Compagnini, Antonio Raudino, Martina Pannuzzo, Carmelo La Rosa, Danilo Milardi, Franca Fraternali, Fabio Lolicato, Birgit Strodel, Human Rezaei, Francesca Collu, Marcello Condorelli, Trang Nhu Do, Ayyalusamy Ramamoorthy, Mikko Karttunen
Publikováno v:
European biophysics journal 49 (2020): 175–191. doi:10.1007/s00249-020-01424-1
info:cnr-pdr/source/autori:La Rosa, Carmelo; Condorelli, Marcello; Compagnini, Giuseppe; Lolicato, Fabio; Milardi, Danilo; Do, Trang Nhu; Karttunen, Mikko; Pannuzzo, Martina; Ramamoorthy, Ayyalusamy; Fraternali, Franca; Collu, Francesca; Rezaei, Human; Strodel, Birgit; Raudino, Antonio/titolo:Symmetry-breaking transitions in the early steps of protein self-assembly/doi:10.1007%2Fs00249-020-01424-1/rivista:European biophysics journal/anno:2020/pagina_da:175/pagina_a:191/intervallo_pagine:175–191/volume:49
European Biophysics Journal
European Biophysics Journal, Springer Verlag (Germany), 2020, 49 (2), pp.175-191. ⟨10.1007/s00249-020-01424-1⟩
European biophysics journal 49(2), 175-191 (2020). doi:10.1007/s00249-020-01424-1
info:cnr-pdr/source/autori:La Rosa, Carmelo; Condorelli, Marcello; Compagnini, Giuseppe; Lolicato, Fabio; Milardi, Danilo; Do, Trang Nhu; Karttunen, Mikko; Pannuzzo, Martina; Ramamoorthy, Ayyalusamy; Fraternali, Franca; Collu, Francesca; Rezaei, Human; Strodel, Birgit; Raudino, Antonio/titolo:Symmetry-breaking transitions in the early steps of protein self-assembly/doi:10.1007%2Fs00249-020-01424-1/rivista:European biophysics journal/anno:2020/pagina_da:175/pagina_a:191/intervallo_pagine:175–191/volume:49
European Biophysics Journal
European Biophysics Journal, Springer Verlag (Germany), 2020, 49 (2), pp.175-191. ⟨10.1007/s00249-020-01424-1⟩
European biophysics journal 49(2), 175-191 (2020). doi:10.1007/s00249-020-01424-1
International audience; Protein misfolding and subsequent self-association are complex, intertwined processes, resulting in development of a heterogeneous population of aggregates closely related to many chronic pathological conditions including Type
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b546abc0f3961d52c5d84d20de2758c9
https://doi.org/10.1007/s00249-020-01424-1
https://doi.org/10.1007/s00249-020-01424-1
Autor:
Franca Fraternali, Ritu Garg, Bárbara Borda D’Agua, Audrey Colomba, Anne J. Ridley, Sofia T. Menéndez, Raquel B. Haga, Francesca Collu
Publikováno v:
Haga, R B, Garg, R, Collu, F, D’Agua, B B, Menéndez, S T, Colomba, A, Fraternali, F & Ridley, A J 2019, ' RhoBTB1 interacts with ROCKs and inhibits invasion ', Biochemical Journal, vol. 476, no. 17, pp. 2499-2514 . https://doi.org/10.1042/BCJ20190203, https://doi.org/10.1042/BCJ20190203
Biochemical Journal
Biochemical Journal
RhoBTB1 is an atypical Rho GTPase with two BTB domains in addition to its Rho domain. Although most Rho GTPases regulate actin cytoskeletal dynamics, RhoBTB1 is not known to affect cell shape or motility. We report that RhoBTB1 depletion increases pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70f70e51419822cdeed2109b6bca21c8
https://hdl.handle.net/1983/0ce5e1c3-ad97-49f7-ad5b-ac02293f6d35
https://hdl.handle.net/1983/0ce5e1c3-ad97-49f7-ad5b-ac02293f6d35
Publikováno v:
Chemical Communications
Chemical Communications, Royal Society of Chemistry, 2018, 54 (57), pp.8007-8010. ⟨10.1039/c8cc04089c⟩
Chemical Communications, Royal Society of Chemistry, 2018, 54 (57), pp.8007-8010. ⟨10.1039/c8cc04089c⟩
International audience; Prions are self-replicating infectious proteinaceous agents whose conformations are capable of forming amyloid-like aggregate fibrils. Here we present molecular dynamics simulations aimed at investigating the aggregation proce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3d43cefd7b5498c05bcffbc83cdd298
https://pubmed.ncbi.nlm.nih.gov/29967919
https://pubmed.ncbi.nlm.nih.gov/29967919
Autor:
Paul R. Barber, Yosef Yarden, Roger George, Gargi Patel, Flavia Autore, Boris Vojnovic, Gregory Weitsman, Audrey Colomba, Marisa L. Martin-Fernandez, Selene K. Roberts, Peter J. Parker, Laura C. Zanetti-Domingues, Tony Ng, Michael Hirsch, Francesca Collu, Angus J.M. Cameron, Franca Fraternali, Tanya N. Soliman, Elena Ortiz-Zapater, Jeroen Claus
Publikováno v:
Claus, J, Patel, G, Autore, F, Colomba, A, Weitsman, G, Soliman, T N, Roberts, S, Zanetti Domingues, L C, Hirsch, M, Collu, F, George, R, Ortiz-Zapater, E, Barber, P R, Vojnovic, B, Yarden, Y, Martin-Fernandez, M L, Cameron, A, Fraternali, F, Ng, T & Parker, P J 2018, ' Inhibitor-induced HER2-HER3 heterodimerisation promotes proliferation through a novel dimer interface ', eLife, vol. 7, e32271 . https://doi.org/10.7554/eLife.32271
eLife
eLife, Vol 7 (2018)
eLife
eLife, Vol 7 (2018)
While targeted therapy against HER2 is an effective first-line treatment in HER2+ breast cancer, acquired resistance remains a clinical challenge. The pseudokinase HER3, heterodimerisation partner of HER2, is widely implicated in the resistance to HE
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::710cfdc7ac40e5df3cb72c57279b1b1a
https://doi.org/10.7554/elife.32271
https://doi.org/10.7554/elife.32271
Autor:
Francesca Collu, Tony Ng, Paul R. Barber, Jeroen Claus, Gargi Patel, Franca Fraternali, Gregory Weitsman, Angus J.M. Cameron, Michael Hirsch, Peter J. Parker, Roger George, Flavia Autore, Marisa L. Martin-Fernandez, Laura C. Zanetti-Domingues, Boris Vojnovic, Yosef Yarden, Tanya N. Soliman, Elena Ortiz-Zapater, Selene K. Roberts, Audrey Colomba
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ec3894b79dd4cc103426160cb78a6061
https://doi.org/10.7554/elife.32271.037
https://doi.org/10.7554/elife.32271.037