Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Eva di Silvio"'
Autor:
Célia Caillet-Saguy, Angelo Toto, Raphael Guerois, Pierre Maisonneuve, Eva di Silvio, Kristi Sawyer, Stefano Gianni, Nicolas Wolff
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
Abstract Human protein tyrosine phosphatase non-receptor type 4 (PTPN4) has been shown to prevent cell death. The active form of human PTPN4 consists of two globular domains, a PDZ (PSD-95/Dlg/ZO-1) domain and a phosphatase domain, tethered by a flex
Externí odkaz:
https://doaj.org/article/cee468f5e6294dbb87c0a2a532e72493
Autor:
Pallabi Sil, Carlo Travaglini-Allocatelli, Eva Di Silvio, Simanta Sarani Paul, Krishnananda Chattopadhyay
Publikováno v:
Physical Chemistry Chemical Physics. 18:24537-24548
In this paper, we have studied the equilibrium unfolding transitions of cytochrome c from Pseudomonas aeruginosa (cytc551), a small bacterial protein. Similar to eukaryotic cytochrome c, cytc551 folds sequentially, although significant differences ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2f3082cf667d73f8067e25340834e21
https://doi.org/10.1039/c6cp04819f
https://doi.org/10.1039/c6cp04819f
Publikováno v:
Journal of Proteins and Proteomics, Vol 3, Iss 1, Pp 1-7 (2012)
Cytochrome c contains heme covalently bound to the polypeptide chain through two thioether bonds between the heme vinyl groups and the two cysteines of the conserved heme- binding motif of the apoprotein. Surprisingly, the biochemical events leading
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doajarticles::2068c2d555e1f0ebe773621a0aeeaf42
http://jpp.org.in/index.php/jpp/article/view/27/26
http://jpp.org.in/index.php/jpp/article/view/27/26
Publikováno v:
Angewandte Chemie International Edition 54 (2015): 10867–10869. doi:10.1002/anie.201504835
info:cnr-pdr/source/autori:Di Silvio E.; Brunori M.; Gianni S./titolo:Frustration Sculpts the Early Stages of Protein Folding/doi:10.1002%2Fanie.201504835/rivista:Angewandte Chemie International Edition/anno:2015/pagina_da:10867/pagina_a:10869/intervallo_pagine:10867–10869/volume:54
info:cnr-pdr/source/autori:Di Silvio E.; Brunori M.; Gianni S./titolo:Frustration Sculpts the Early Stages of Protein Folding/doi:10.1002%2Fanie.201504835/rivista:Angewandte Chemie International Edition/anno:2015/pagina_da:10867/pagina_a:10869/intervallo_pagine:10867–10869/volume:54
The funneled energy landscape theory implies that protein structures are minimally frustrated. Yet, because of the divergent demands between folding and function, regions of frustrated patterns are present at the active site of proteins. To understan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76d75f88b556221256a92aa1d1727874
https://pubmed.ncbi.nlm.nih.gov/26212018
https://pubmed.ncbi.nlm.nih.gov/26212018
Autor:
Daniela Bonetti, Angela Morrone, Eva Di Silvio, Stefano Gianni, Marion Dosnon, Jenny Erales, Sonia Longhi
Publikováno v:
ACS Chemical Biology
ACS Chemical Biology, American Chemical Society, 2015, 10 (3), pp.795-802. ⟨10.1021/cb5008579⟩
ACS Chemical Biology, 2015, 10 (3), pp.795-802. ⟨10.1021/cb5008579⟩
ACS Chemical Biology, American Chemical Society, 2015, 10 (3), pp.795-802. ⟨10.1021/cb5008579⟩
ACS Chemical Biology, 2015, 10 (3), pp.795-802. ⟨10.1021/cb5008579⟩
In the past decade, a wealth of experimental data has demonstrated that a large fraction of proteins, while functional, are intrinsically disordered at physiological conditions. Many intrinsically disordered proteins (IDPs) undergo a disorder-to-orde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47178be42b7aa51440ca777bb6a1bca0
https://hal.archives-ouvertes.fr/hal-01439003
https://hal.archives-ouvertes.fr/hal-01439003
Publikováno v:
Scientific Reports
PDZ domains are the most prominent biological structural domains involved in protein-protein interactions in the human cell. The second PDZ domain of the protein tyrosine phosphatase BL (PDZ2) interacts and binds the C-termini of the tumour suppresso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe4ec6f27dfda3af5b4b97312d482975
http://hdl.handle.net/11573/782784
http://hdl.handle.net/11573/782784
Publikováno v:
Protein Engineering, Design and Selection
Protein Engineering, Design and Selection, Oxford University Press (OUP), 2014, 27 (8), pp.249-53. ⟨10.1093/protein/gzu022⟩
Protein Engineering, Design and Selection, Oxford University Press (OUP), 2014, 27 (8), pp.249-53. ⟨10.1093/protein/gzu022⟩
International audience; Many biological processes are regulated by the interaction between protein domains and their corresponding binding partners. The PDZ domain is one of the most common protein-protein interaction modules in mammalian cells, whos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e827a3f3ff3ffd19d62807e484683b8f
https://hal-riip.archives-ouvertes.fr/pasteur-01181359/document
https://hal-riip.archives-ouvertes.fr/pasteur-01181359/document
Autor:
Eva Di Silvio, Michele M. Bianchi, Giuseppe Damato, Hermann J. Heipieper, Chiara Micolonghi, Daniela Ottaviano
Publikováno v:
Microbiology (Reading, England). 158(Pt 7)
In the respiratory yeast Kluyveromyces lactis, little is known about the factors regulating the metabolic response to oxygen shortage. After searching for homologues of characterized Saccharomyces cerevisiae regulators of the hypoxic response, we ide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9841ae1220053177703246aa03d7afa9
https://pubmed.ncbi.nlm.nih.gov/22516223
https://pubmed.ncbi.nlm.nih.gov/22516223