Výsledky vyhledávání - "Alessio, Prunotto"

Akademický článek

Structure Based Modeling of Small Molecules Binding to the TLR7 by Atomistic Level Simulations

Autor: Francesco Gentile, Marco A. Deriu, Ginevra Licandro, Alessio Prunotto, Andrea Danani, Jack A. Tuszynski

Publikováno v: Molecules, Vol 20, Iss 5, Pp 8316-8340 (2015)

Toll-Like Receptors (TLR) are a large family of proteins involved in the immune system response. Both the activation and the inhibition of these receptors can have positive effects on several diseases, including viral pathologies and cancer, therefor

Externí odkaz: https://doaj.org/article/0809d6115fe146a58ec21128248dec82

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Molecular Bases of the Membrane Association Mechanism Potentiating Antibiotic Resistance by New Delhi Metallo-β-lactamase 1

Autor: Lisandro J González, Alessio Prunotto, Matteo Dal Peraro, Guillermo Bahr, Alejandro J. Vila

Publikováno v: ACS Infect Dis

Resistance to last-resort carbapenem antibiotics is an increasing threat to human health, as it critically limits therapeutic options. Metallo-β-lactamases (MBLs) are the largest family of carbapenemases, enzymes that inactivate these drugs. Among M

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ca33c9f1425d0c07efefe52f7dcf55e
https://doi.org/10.1021/acsinfecdis.0c00341

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Specific Protein-Membrane Interactions Promote Packaging of Metallo-β-Lactamases into Outer Membrane Vesicles

Autor: Guillermo Bahr, Lisandro J González, Alessio Prunotto, Carolina Lopez, Matteo Dal Peraro, Alejandro J Vila, Robert A. Bonomo

Publikováno v: Antimicrob Agents Chemother

Outer membrane vesicles (OMVs) act as carriers of bacterial products such as plasmids and resistance determinants, including metallo-β-lactamases. The lipidated, membrane-anchored metallo-β-lactamase NDM-1 can be detected in Gram-negative OMVs. The

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73728934c993201dcdc5963f92b245fd
https://doi.org/10.1128/aac.00507-21

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Specific protein-membrane interactions promote the export of metallo-β-lactamases via outer membrane vesicles

Autor: Bahr G, Dal Peraro M, Alessio Prunotto, Lisandro J González, Carolina López, Alejandro J. Vila, Robert A. Bonomo

Outer membrane vesicles (OMVs) act as carriers of resistance determinants such as metallo-β-lactamases. The metallo-β-lactamase NDM-1 is present in OMVs produced by Gram-negative bacteria since it is a lipidated, membrane-anchored protein. The solu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2338dee4810d8f3866328e0240fb62c7
https://doi.org/10.1101/2021.03.18.436108

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Structural basis for recognition of bacterial cell wall teichoic acid by pseudo-symmetric SH3b-like repeats of a viral peptidoglycan hydrolase

Autor: Benjamin Gerber, Martin J. Loessner, Francisco Javier Cañada, Matthew Dunne, Matteo Dal Peraro, Ioanna Kalograiaki, Alicia Julian-Rodero, Yang Shen, Eric T. Sumrall, Rebecca Martin, Samy Boulos, Margarita Menéndez, Marcel R. Eugster, Petr G. Leiman, Alessio Prunotto, Nicholas M.I. Taylor

Publikováno v: Chemical Science, 12 (2)
Chemical Science
Digital.CSIC. Repositorio Institucional del CSIC
instname

14 p.-6 fig.-1 tab.
Endolysins are bacteriophage-encoded peptidoglycan hydrolases targeting the cell wall of host bacteria via their cell wall-binding domains (CBDs). The molecular basis for selective recognition of surface carbohydrate ligands

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa3a29961afd89f2314ecb5655e6e476
https://hdl.handle.net/20.500.11850/459659

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Molecular basis for recognition of Listeria cell wall teichoic acid by the pseudo-symmetric SH3b-like repeats of a bacteriophage endolysin

Autor: Benjamin Gerber, Ioanna Kalograiaki, Alessio Prunotto, Eric T. Sumrall, Yang Shen, Matthew Dunne, Francisco Javier Cañada, Nicholas M.I. Taylor, Loessner J. Martin, Margarita Menéndez, Alicia Julian Rodero, Petr G. Leiman, Samy Boulos, Rebecca Martin, Marcel R. Eugster, Matteo Dal Peraro

Endolysins are bacteriophage-encoded peptidoglycan hydrolases targeting the cell wall of host bacteria via their cell wall-binding domains (CBDs). The molecular basis for selective recognition of surface carbohydrate ligands by CBDs remains elusive.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::677faeb205215b310242f1322bf61f59
https://doi.org/10.1101/2020.06.05.136911

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Salt Enhances the Thermostability of Enteroviruses by Stabilizing Capsid Protein Interfaces

Autor: Matteo Dal Peraro, Simon Meister, Alessio Prunotto, Tamar Kohn

Publikováno v: J Virol

Enteroviruses are common agents of infectious disease that are spread by the fecal-oral route. They are readily inactivated by mild heat, which causes the viral capsid to disintegrate or undergo conformational change. While beneficial for the thermal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8e1f696e9fbfe110e76c0726ae08676
https://doi.org/10.1128/jvi.02176-19

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Extensive tissue-specific expression variation and novel regulators underlying circadian behavior

Autor: Maria, Litovchenko, Antonio C A, Meireles-Filho, Michael V, Frochaux, Roel P J, Bevers, Alessio, Prunotto, Ane Martin, Anduaga, Brian, Hollis, Vincent, Gardeux, Virginie S, Braman, Julie M C, Russeil, Sebastian, Kadener, Matteo, Dal Peraro, Bart, Deplancke

Publikováno v: Science Advances

A dataset of >700 tissue-specific transcriptomes of D. melanogaster reveals population-level molecular circadian clock variation.
Natural genetic variation affects circadian rhythms across the evolutionary tree, but the underlying molecular mech

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d3b9dc68fd64d6cc028a944aec234a0a
https://pubmed.ncbi.nlm.nih.gov/33514540

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