Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Marian Vincenzi"'
Publikováno v:
Molecules, Vol 29, Iss 5, p 1024 (2024)
The lipid phosphatase Ship2 interacts with the EphA2 receptor by forming a heterotypic Sam (sterile alpha motif)–Sam complex. Ship2 works as a negative regulator of receptor endocytosis and consequent degradation, and anti-oncogenic effects in canc
Externí odkaz:
https://doaj.org/article/ec9ca8ac40024d119eca2f3a6a207315
Publikováno v:
Molecules, Vol 23, Iss 8, p 1846 (2018)
Adenosine receptors are involved in many physiological processes and pathological conditions and are therefore attractive therapeutic targets. To identify new types of effective ligands for these receptors, a library of adenosine derivatives bearing
Externí odkaz:
https://doaj.org/article/104f9d328c1b4900a5dda2a53d2d9dfb
Autor:
Marian Vincenzi, Marilisa Leone
Publikováno v:
Current Medicinal Chemistry. 28:4380-4453
Background: COVID-19 has brought the world to its knees, and there is an urgent need for new strategies to identify molecules capable of fighting the pandemic. During the last few decades, NMR (Nuclear Magnetic Resonance) spectroscopy has emerged as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91984e576a085cfcf2d9d8bb747d61f3
https://doi.org/10.2174/0929867328666201228123748
https://doi.org/10.2174/0929867328666201228123748
Publikováno v:
International journal of molecular sciences. 23(18)
Among the diverse protein binding modules, Sam (Sterile alpha motif) domains attract attention due to their versatility. They are present in different organisms and play many functions in physiological and pathological processes by binding multiple p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8832899118612c780e9c84ee1192b1f
https://pubmed.ncbi.nlm.nih.gov/36142306
https://pubmed.ncbi.nlm.nih.gov/36142306
Publikováno v:
Current medicinal chemistry (2020). doi:10.2174/0929867327666200702131032
info:cnr-pdr/source/autori:Vincenzi M, Mercurio FA, Leone M./titolo:NMR spectroscopy in the conformational analysis of peptides: an overview./doi:10.2174%2F0929867327666200702131032/rivista:Current medicinal chemistry/anno:2020/pagina_da:/pagina_a:/intervallo_pagine:/volume
info:cnr-pdr/source/autori:Vincenzi M, Mercurio FA, Leone M./titolo:NMR spectroscopy in the conformational analysis of peptides: an overview./doi:10.2174%2F0929867327666200702131032/rivista:Current medicinal chemistry/anno:2020/pagina_da:/pagina_a:/intervallo_pagine:/volume
Background: NMR spectroscopy is one of the most powerful tools to study the structure and interaction properties of peptides and proteins from a dynamic perspective. Knowing the bioactive conformations of peptides is crucial in the drug discovery fie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01a90bafd056a645b18799c39d2aecb2
https://doi.org/10.2174/0929867327666200702131032
https://doi.org/10.2174/0929867327666200702131032
Publikováno v:
Current medicinal chemistry.
Background: In the last few years, in silico tools, including drug repurposing coupled with structure-based virtual screening, have been extensively employed to look for anti-COVID-19 agents. Objective: The present review aims to provide readers with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e19fcea1b0afd774ba6a6a580833385b
https://pubmed.ncbi.nlm.nih.gov/36200217
https://pubmed.ncbi.nlm.nih.gov/36200217
Publikováno v:
Current medicinal chemistry (2019). doi:10.2174/0929867326666190620101637
info:cnr-pdr/source/autori:Marian Vincenzi, Flavia Anna Mercurio, Marilisa Leone/titolo:Protein Interaction Domains and post-translational modifications: structural features and drug discovery applications./doi:10.2174%2F0929867326666190620101637/rivista:Current medicinal chemistry/anno:2019/pagina_da:/pagina_a:/intervallo_pagine:/volume
info:cnr-pdr/source/autori:Marian Vincenzi, Flavia Anna Mercurio, Marilisa Leone/titolo:Protein Interaction Domains and post-translational modifications: structural features and drug discovery applications./doi:10.2174%2F0929867326666190620101637/rivista:Current medicinal chemistry/anno:2019/pagina_da:/pagina_a:/intervallo_pagine:/volume
Background:Many pathways regarding healthy cells and/or linked to diseases onset and progression depend on large assemblies including multi-protein complexes. Protein-protein interactions may occur through a vast array of modules known as protein int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26253dea7c66d55939f8ad7bbee1fe6b
https://doi.org/10.2174/0929867326666190620101637
https://doi.org/10.2174/0929867326666190620101637
Publikováno v:
Current medicinal chemistry 27 (2020): 450–476. doi:10.2174/0929867325666181009114445
info:cnr-pdr/source/autori:Vincenzi, Marian; Mercurio, Flavia Anna; Leone, Marilisa/titolo:Sam Domains in Multiple Diseases/doi:10.2174%2F0929867325666181009114445/rivista:Current medicinal chemistry/anno:2020/pagina_da:450/pagina_a:476/intervallo_pagine:450–476/volume:27
info:cnr-pdr/source/autori:Vincenzi, Marian; Mercurio, Flavia Anna; Leone, Marilisa/titolo:Sam Domains in Multiple Diseases/doi:10.2174%2F0929867325666181009114445/rivista:Current medicinal chemistry/anno:2020/pagina_da:450/pagina_a:476/intervallo_pagine:450–476/volume:27
Background:The sterile alpha motif (Sam) domain is a small helical protein module, able to undergo homo- and hetero-oligomerization, as well as polymerization, thus forming different types of protein architectures. A few Sam domains are involved in p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1731608b2a3411696022d18268e431f
https://doi.org/10.2174/0929867325666181009114445
https://doi.org/10.2174/0929867325666181009114445
Autor:
Marilisa Leone, Emilia Pedone, Flavia Anna Mercurio, Marian Vincenzi, Luciano Pirone, Daniela Marasco, Stefania De Luca, Concetta Di Natale
Publikováno v:
ChemBioChem. 21:702-711
Sterile alpha motif (SAM) domains are protein interaction modules with a helical fold. SAM-SAM interactions often adopt the mid-loop (ML)/end-helix (EH) model, in which the C-terminal helix and adjacent loops of one SAM unit (EH site) bind the centra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3337cc797122220ff09a7b38daffac04
https://doi.org/10.1002/cbic.201900444
https://doi.org/10.1002/cbic.201900444
Autor:
Marian Vincenzi, Flavia Anna Mercurio, Concetta Di Natale, Rosanna Palumbo, Luciano Pirone, Sara La Manna, Daniela Marasco, Emilia Maria Pedone, Marilisa Leone
Publikováno v:
Bioorganic Chemistry. 122:105680
The lipid phosphatase Ship2 binds the EphA2 receptor through a heterotypic Sam-Sam (Sterile alpha motif) interaction. Inhibitors of the Ship2-Sam/EphA2-Sam complex hold a certain potential as novel anticancer agents. The previously reported “KRI3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a56c5382e4e88bea30cd4d71aa39dd72
https://doi.org/10.1016/j.bioorg.2022.105680
https://doi.org/10.1016/j.bioorg.2022.105680