Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Igor Zelezetsky"'
Autor:
Chadi Dura Haddad, Ludovica Andreatti, Igor Zelezetsky, Davide Porrelli, Gianluca Turco, Lorenzo Bevilacqua, Michele Maglione
Publikováno v:
Bioengineering, Vol 11, Iss 4, p 383 (2024)
The approach employed for the site preparation of the dental implant is a variable factor that affects the implant’s primary stability and its ability to integrate with the surrounding bone. The main objective of this in vitro study is to evaluate
Externí odkaz:
https://doaj.org/article/5635f128abd94121becee65388f412c5
Autor:
Silvano Geremia, Lucio Randaccio, Alessandro Pesaresi, Igor Zelezetsky, Gianluca Tell, Alessia Bisca, Mara Campagnolo
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 24:429-441
Pax-8 is a member of the Pax family of transcription factors and is essential in the development of thyroid follicular cells. Pax-8 has two DNA-binding domains: the paired domain and the homeo domain. In this study, a preliminary X-ray diffraction an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f3e21963696473bc7def9414a700a8a
https://doi.org/10.1080/07391102.2007.10507131
https://doi.org/10.1080/07391102.2007.10507131
Autor:
Luca Puzzi, Sabrina Pacor, Ludovica Segat, Nikolinka Antcheva, Sergio Crovella, Igor Zelezetsky, Alessandro Tossi, Alessandra Pontillo
Publikováno v:
Journal of Biological Chemistry. 281:19861-19871
Cathelicidin genes homologous to the human CAMP gene, coding for the host defense peptide LL-37, have been sequenced and analyzed in 20 primate species, including Great Apes, hylobatidae, cercopithecidae, callithricidae, and cebidae. The region corre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4e528e110109b9f14712461aaad7e518
https://doi.org/10.1074/jbc.m511108200
https://doi.org/10.1074/jbc.m511108200
Autor:
Maria Vittoria Verga Falzacappa, Alessandro Tossi, Igor Zelezetsky, Sergio Crovella, Sabrina Pacor, Michele Boniotto, Nikolinka Antcheva
Publikováno v:
Current Protein & Peptide Science. 6:7-21
Host defense peptides (HDPs) are endogenous antibiotics that play a multifunctional role in the innate immunity of mammals. Among these, βdefensins contribute to mucosal and epithelial defense, also acting as signal molecules for cellular components
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e6003281dacb334cfacd395e84433676
https://doi.org/10.2174/1389203053027593
https://doi.org/10.2174/1389203053027593
Autor:
Igor Zelezetsky, Alessandro Tossi
An important class of cytolytic antimicrobial peptides (AMPs) assumes an amphipathic, α-helical conformation that permits efficient interaction with biological membranes. Host defence peptides of this type are widespread in nature, and numerous synt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6b590511bf5ead7ce60f69f8ee106f7
http://hdl.handle.net/11368/1702277
http://hdl.handle.net/11368/1702277
The term defensin relates different families of host defense peptides (HDPs) in vertebrates, invertebrates, plants, and molds that display structural similarities based on a cystine stabilized antiparallel β-sheet core, with an N-terminal α-helical
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08d87cc2f4c42bd494cc089c8ea4d714
https://doi.org/10.1016/b978-012369442-3/50014-3
https://doi.org/10.1016/b978-012369442-3/50014-3
Autor:
Renato Gennaro, Andrea Mazzoli, Igor Zelezetsky, Monica Benincasa, Marco Scocchi, Alessandro Tossi
Publikováno v:
The FEBS journal. 272(17)
PMAP-36 is a cathelicidin-derived host defence peptide originally deduced by a transcript from pig bone marrow RNA. The expression of the propeptide in leukocytes, and the structure, antimicrobial activity, and mechanism of action of the mature pepti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b88c273b740598cbda35a91f22ed715d
https://pubmed.ncbi.nlm.nih.gov/16128809
https://pubmed.ncbi.nlm.nih.gov/16128809
Autor:
Hans-Georg Sahl, Igor Zelezetsky, Ulrike Pag, Sabrina Pacor, Yechiel Shai, Niv Papo, Alessandro Tossi
A novel method, based on the rational and systematic modulation of macroscopic structural characteristics on a template originating from a large number of natural, cell-lytic, amphipathic α-helical peptides, was used to probe how the depths and shap
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d825d5de95163c2ff8e71742a989a4d
https://europepmc.org/articles/PMC1184573/
https://europepmc.org/articles/PMC1184573/
A template based on positional residue frequencies in the N-terminal stretch of natural alpha-helical antimicrobial peptides was used to prepare sequence patterns and to scan the Swiss-Prot Database, using the ScanProsite tool. This search identified
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62ea623e95eafb61f5179ed7cf670972
https://hdl.handle.net/11368/1702264
https://hdl.handle.net/11368/1702264
In nature, alpha-helical antimicrobial peptides present the small and flexible residue glycine at positions 7 or 14 with a significant frequency. Based on the sequence of the non-proteinogenic alpha-helical model peptide P1(Aib7), with a potent, broa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7eeb4eb96174c271c7c0631e0ac819ed
https://hdl.handle.net/11368/1702271
https://hdl.handle.net/11368/1702271