Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Angela Morrone"'
Autor:
Greta Hultqvist, Avinash S Punekar, Angela Morrone, Celestine N Chi, Ake Engström, Maria Selmer, Stefano Gianni, Per Jemth
Publikováno v:
PLoS ONE, Vol 7, Iss 11, p e50055 (2012)
Circular permutation is a common molecular mechanism for evolution of proteins. However, such re-arrangement of secondary structure connectivity may interfere with the folding mechanism causing accumulation of folding intermediates, which in turn can
Externí odkaz:
https://doaj.org/article/686f5d42279f47c3ae0bac20f3d94661
Autor:
Michele Vendruscolo, Stefano Gianni, Daniela Bonetti, Carlo Camilloni, Angela Morrone, Christopher M. Dobson, Maurizio Brunori, Rajanish Giri
Publikováno v:
Scientific Reports
The hydrophobic effect is a major driving force in protein folding. A complete understanding of this effect requires the description of the conformational states of water and protein molecules at different temperatures. Towards this goal, we characte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9d1e7271d18d093dc7d7778bbcd904d
http://hdl.handle.net/11573/867523
http://hdl.handle.net/11573/867523
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:
Annalisa Pastore, Angelo Toto, Angela Morrone, Stefano Gianni, Daniela Bonetti, Rajanish Giri, Maurizio Brunori, Pierandrea Temussi, Domenico Sanfelice
Publikováno v:
Physical Chemistry Chemical Physics
Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2014, 16 (14), pp.6391-7. <10.1039/c3cp54055c>
Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2014, 16 (14), pp.6391-7. ⟨10.1039/c3cp54055c⟩
Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2014, 16 (14), pp.6391-7. <10.1039/c3cp54055c>
Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2014, 16 (14), pp.6391-7. ⟨10.1039/c3cp54055c⟩
The role of the denatured state in protein folding represents a key issue for the proper evaluation of folding kinetics and mechanisms. The yeast ortholog of the human frataxin, a mitochondrial protein essential for iron homeostasis and responsible f
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2013, 110 (37), pp.14942-7. ⟨10.1073/pnas.1307337110⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2013, 110 (37), pp.14942-7. ⟨10.1073/pnas.1307337110⟩
International audience; A classical dogma of molecular biology dictates that the 3D structure of a protein is necessary for its function. However, a considerable fraction of the human proteome, although functional, does not adopt a defined folded sta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49bd7851bccfdedf9d3db17046b44b20
https://hal-riip.archives-ouvertes.fr/pasteur-01025444/document
https://hal-riip.archives-ouvertes.fr/pasteur-01025444/document
Publikováno v:
Biochemical and Biophysical Research Communications
Biochemical and Biophysical Research Communications, Elsevier, 2012, 428 (2), pp.205-9. ⟨10.1016/j.bbrc.2012.09.112⟩
Biochemical and Biophysical Research Communications, Elsevier, 2012, 428 (2), pp.205-9. ⟨10.1016/j.bbrc.2012.09.112⟩
International audience; A large body of evidence suggests that a considerable fraction of the human proteome may be at least in part intrinsically unstructured. While disordered, intrinsically unstructured proteins are nevertheless functional and med
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20bffb2aa4f12c1bae082c0f2756c5fe
https://hal-riip.archives-ouvertes.fr/pasteur-00960073
https://hal-riip.archives-ouvertes.fr/pasteur-00960073
Publikováno v:
Protein Science
Protein Science, Wiley, 2012, 21 (11), pp.1775-9. ⟨10.1002/pro.2159⟩
Protein Science, Wiley, 2012, 21 (11), pp.1775-9. ⟨10.1002/pro.2159⟩
International audience; The debate about the presence and role of intermediates in the folding of proteins has been a critical issue, especially for fast folders. One of the classical methodologies to identify such metastable species is the "burst-ph
Autor:
Angela Morrone, Stefano Gianni, Maurizio Brunori, Carlo Travaglini-Allocatelli, Rajanish Giri
Publikováno v:
Biochemical Society Transactions
Biochemical Society Transactions, Portland Press, 2012, 40 (2), pp.429-32. ⟨10.1042/BST20110683⟩
Biochemical Society Transactions, Portland Press, 2012, 40 (2), pp.429-32. ⟨10.1042/BST20110683⟩
International audience; Current knowledge on the reaction whereby a protein acquires its native three-dimensional structure was obtained by and large through characterization of the folding mechanism of simple systems. Given the multiplicity of amino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa56ddf203bfbe28ab004c8cd1bf7134
http://hdl.handle.net/11573/458690
http://hdl.handle.net/11573/458690