Výsledky vyhledávání - "M. R. ARMENANTE"

Conformational Analysis of Peptides Derived from Feline Immunodeficiency Virus TM Glycoprotein

Autor: A. M. D'URSI, M. R. ARMENANTE, C. ESPOSITO, P. ROVERO, CAROTENUTO, ALFONSO, NOVELLINO, ETTORE

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3730::10aecce66c6d6fae14b98c41aaebee7f
http://hdl.handle.net/11588/422162

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STRUCTURE-ACTIVITY RELATIONSHIP STUDIES AND CONFORMATIONAL ANALYSIS OF NOVEL ANTIRETROVIRAL PEPTIDES DERIVED FROM FELINE IMMUNODEFICIENCY VIRUS GLYCOPROTEIN GP36

Autor: A. M. D'Ursi, M. R. Armenante, S. Giannecchini, C. Esposito, M. Bendinelli, P. Rovero, CAROTENUTO, ALFONSO, NOVELLINO, ETTORE

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::557bce25805b82d0d921e018b7d1181c
http://hdl.handle.net/11386/3842881

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Conformational features of Amyloid Beta-peptides in aqueous environment

Autor: TOMASELLI, SIMONA, PICONE, DELIA, M. R. Armenante, A. M. D'Ursi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3730::68ae44c439d6979fe6d2effb06d4122d
http://hdl.handle.net/11588/312478

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Physicochemical characterization of a peptide deriving from the glycoprotein gp36 of the feline immunodeficiency virus and its lipoylated analogue in micellar systems

Autor: Anna Maria D'Ursi, Simone Giannecchini, Paolo Rovero, Mauro Bendinelli, Gerardino D'Errico, Cinzia Esposito, Maria Rosaria Armenante

P59 is the Trp-rich 20-mer peptide ( 767 L–G 786 ), partial sequence of the membrane-proximal external region (MPER) of the FIV gp36. It has potent antiviral activity, possibly due to a mechanism that inhibits the fusion of the virus with the cell

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c66e59890da14ff8d78f8b22ce2f627a
http://hdl.handle.net/11588/304790

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Solution structure of amyloid beta-peptide (25-35) in different media

Autor: Anna Maria D'Ursi, Severo Salvadori, Remo Guerrini, Delia Picone, Maria Rosaria Armenante, Giuseppe Sorrentino

The design of molecules able to interact with the amyloid peptides either as inhibitors of fibril formation or as inhibitors of amyloid membrane pore formation represents one of the most relevant approaches in the development of anti-Alzheimer therap

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf37b87b142a01aa39b800134065e887
http://hdl.handle.net/11367/32965

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