Zobrazeno 1 - 10
of 56
pro vyhledávání: '"Scognamiglio, Pl"'
Publikováno v:
Chemical biology & drug design (Online) 77 (2011): 319–327. doi:10.1111/j.1747-0285.2011.01094
info:cnr-pdr/source/autori:Scognamiglio PL, Doti N, Grieco P, Pedone C, Ruvo M, Marasco D/titolo:Discovery ofsmall peptide antagonists of PED%2FPEA15-D4? interaction from simplifiedcombinatorial libraries/doi:10.1111%2Fj.1747-0285.2011.01094/rivista:Chemical biology & drug design (Online)/anno:2011/pagina_da:319/pagina_a:327/intervallo_pagine:319–327/volume:77
info:cnr-pdr/source/autori:Scognamiglio PL, Doti N, Grieco P, Pedone C, Ruvo M, Marasco D/titolo:Discovery ofsmall peptide antagonists of PED%2FPEA15-D4? interaction from simplifiedcombinatorial libraries/doi:10.1111%2Fj.1747-0285.2011.01094/rivista:Chemical biology & drug design (Online)/anno:2011/pagina_da:319/pagina_a:327/intervallo_pagine:319–327/volume:77
Most biological processes involve permanent and temporary interactions between different proteins: protein complexes often play key roles in human diseases and, as a consequence, molecules that prevent protein-protein interactions can be potential ne
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=cnr_________::affca48720f36ec7e5d8b873645d565f
Publikováno v:
info:cnr-pdr/source/autori:Scognamiglio PL, Doti N, Pedone C, Grieco P, Sabatella M, Ruvo M, Marasco D/congresso_nome:/congresso_luogo:/congresso_data:2009/anno:2009/pagina_da:/pagina_a:/intervallo_pagine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=cnr_________::1c4d3d763b496c3b9258d4779712ccfe
http://www.cnr.it/prodotto/i/77286
http://www.cnr.it/prodotto/i/77286
Autor:
Pasqualina Liana Scognamiglio, Daniela Marasco, Maurizio Pellecchia, Emilia Pedone, Marilisa Leone, Luciano Pirone, Flavia Anna Mercurio
Publikováno v:
ChemBioChem
14 (2013): 100–106. doi:10.1002/cbic.201200592
info:cnr-pdr/source/autori:Flavia Anna Mercurio, Daniela Marasco, Luciano Pirone, Pasqualina Liana Scognamiglio, Emilia Maria Pedone, Maurizio Pellecchia, Marilisa Leone/titolo:Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insights./doi:10.1002%2Fcbic.201200592/rivista:ChemBioChem (Print)/anno:2013/pagina_da:100/pagina_a:106/intervallo_pagine:100–106/volume:14
14 (2013): 100–106. doi:10.1002/cbic.201200592
info:cnr-pdr/source/autori:Flavia Anna Mercurio, Daniela Marasco, Luciano Pirone, Pasqualina Liana Scognamiglio, Emilia Maria Pedone, Maurizio Pellecchia, Marilisa Leone/titolo:Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insights./doi:10.1002%2Fcbic.201200592/rivista:ChemBioChem (Print)/anno:2013/pagina_da:100/pagina_a:106/intervallo_pagine:100–106/volume:14
Arap3 is a phosphatidylinositol 3 kinase effector protein that plays a role as GTPase activator (GAP) for Arf6 and RhoA. Arap3 contains a sterile alpha motif (Sam) domain that has high sequence homology with the Sam domain of the EphA2-receptor (EphA
A variety of peptides active in biological pathways have been identified e.g. receptor antagonists or inhibitors of protein-protein interactions and several peptide or peptide-derived compounds are on the drug market or in clinical trials. Through th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a09a3b7b52ef69b1e3a9271b1fcaaee
http://hdl.handle.net/11588/562905
http://hdl.handle.net/11588/562905
Autor:
Daniela Marasco, Gianluca Tell, Mattia Poletto, Luigi Vitagliano, Pasqualina Liana Scognamiglio, Carlo Vascotto, Alessia Ruggiero
Publikováno v:
Biochemical and biophysical research communications
430 (2013): 523–528. doi:10.1016/j.bbrc.2012.12.002
info:cnr-pdr/source/autori:Marasco, Daniela; Ruggiero, Alessia; Vascotto, Carlo; Poletto, Mattia; Scognamiglio, Pasqualina Liana; Tell, Gianluca; Vitagliano, Luigi/titolo:Role of mutual interactions in the chemical and thermal stability of nucleophosmin NPM1 domains/doi:10.1016%2Fj.bbrc.2012.12.002/rivista:Biochemical and biophysical research communications (Print)/anno:2013/pagina_da:523/pagina_a:528/intervallo_pagine:523–528/volume:430
430 (2013): 523–528. doi:10.1016/j.bbrc.2012.12.002
info:cnr-pdr/source/autori:Marasco, Daniela; Ruggiero, Alessia; Vascotto, Carlo; Poletto, Mattia; Scognamiglio, Pasqualina Liana; Tell, Gianluca; Vitagliano, Luigi/titolo:Role of mutual interactions in the chemical and thermal stability of nucleophosmin NPM1 domains/doi:10.1016%2Fj.bbrc.2012.12.002/rivista:Biochemical and biophysical research communications (Print)/anno:2013/pagina_da:523/pagina_a:528/intervallo_pagine:523–528/volume:430
Nucleophosmin (NPM1) is a key factor involved in fundamental biological processes. Mutations involving the NPM1 gene are the most frequent molecular alterations in acute myeloid leukemia. Here we report a biophysical characterization of NPM1 and of i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81c2acab02a74cef74309c6dd3ea01b7
http://hdl.handle.net/11588/530694
http://hdl.handle.net/11588/530694
Autor:
Pasqualina Liana Scognamiglio, Daniela Marasco, Carlo Vascotto, Mattia Poletto, Gianluca Tell, Lisa Lirussi
The hAPE1 (human apurinic/apyrimidinic endonuclease 1) is an essential enzyme, being the main abasic endonuclease in higher eukaryotes. However, there is strong evidence to show that hAPE1 can directly bind specific gene promoters, thus modulating th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26cba280fee23beb149d758098b965f4
http://hdl.handle.net/11588/562910
http://hdl.handle.net/11588/562910
Autor:
Monti A; Institute of Biostructures and Bioimaging (IBB)-CNR, Via P. Castellino 111, 80131, Napoli, Italy., Scognamiglio PL; Department of Sciences, University of Basilicata, Macchia Romana Campus 10, Viale dell'Ateneo Lucano, 85100, Potenza, Italy., Ruvo M; Institute of Biostructures and Bioimaging (IBB)-CNR, Via P. Castellino 111, 80131, Napoli, Italy., Vitagliano L; Institute of Biostructures and Bioimaging (IBB)-CNR, Via P. Castellino 111, 80131, Napoli, Italy., Doti N; Institute of Biostructures and Bioimaging (IBB)-CNR, Via P. Castellino 111, 80131, Napoli, Italy.
Publikováno v:
Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2024 Jun 20; Vol. 30 (35), pp. e202400846. Date of Electronic Publication: 2024 May 28.
Autor:
Simonyan H; Institute of Pharmacy, Yerevan State University, 1 Alex Manoogian Str., Yerevan 0025, Armenia., Palumbo R; Institute of Biostructures and Bioimaging, Italian National Council for Research (IBB-CNR), Area di Ricerca Site and Headquarters, Via Pietro Castellino 111, 80131 Naples, Italy., Petrosyan S; Institute of Pharmacy, Yerevan State University, 1 Alex Manoogian Str., Yerevan 0025, Armenia., Mkrtchyan A; Institute of Pharmacy, Yerevan State University, 1 Alex Manoogian Str., Yerevan 0025, Armenia., Galstyan A; Department of Chemistry, Yerevan State University, 1 Alex Manoogian Str., Yerevan 0025, Armenia., Saghyan A; Institute of Pharmacy, Yerevan State University, 1 Alex Manoogian Str., Yerevan 0025, Armenia., Scognamiglio PL; Department of Sciences, University of Basilicata, Via dell'Ateneo Lucano 10, 85100 Potenza, Italy., Vicidomini C; Institute of Biostructures and Bioimaging, Italian National Council for Research (IBB-CNR), Area di Ricerca Site and Headquarters, Via Pietro Castellino 111, 80131 Naples, Italy., Fik-Jaskólka M; Faculty of Chemistry, Adam Mickiewicz University in Poznań, Uniwersytetu Poznańskiego 8, 61-614 Poznań, Poland., Roviello GN; Institute of Biostructures and Bioimaging, Italian National Council for Research (IBB-CNR), Area di Ricerca Site and Headquarters, Via Pietro Castellino 111, 80131 Naples, Italy.
Publikováno v:
Biomolecules [Biomolecules] 2024 May 14; Vol. 14 (5). Date of Electronic Publication: 2024 May 14.