Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Augusto Bellomio"'
Autor:
Koldo Morante, Augusto Bellomio, Ana Rosa Viguera, Juan Manuel González-Mañas, Kouhei Tsumoto, Jose M. M. Caaveiro
Publikováno v:
Toxins, Vol 11, Iss 7, p 401 (2019)
Random mutations and selective pressure drive protein adaptation to the changing demands of the environment. As a consequence, nature favors the evolution of protein diversity. A group of proteins subject to exceptional environmental stress and known
Externí odkaz:
https://doaj.org/article/f1c44771913946f1a4b329d3891bea35
Publikováno v:
Applied Microbiology and Biotechnology. 104:6067-6077
Bacteriocins are peptides of ribosomal synthesis that are active against bacteria related to the producing strain. They have been widely used in the food industry as biopreservatives. The generation of hybrid peptides by combining the genes that enco
Autor:
Augusto Bellomio, Natalia Soledad Ríos Colombo, Silvia Adriana Navarro, Miriam Carolina Chalon
Publikováno v:
Current Genetics. 64:345-351
This review attempts to analyze the mechanism of action and immunity of class IIa bacteriocins. These peptides are promising alternative food preservatives and they have a great potential application in medical sciences. Class IIa bacteriocins act on
Autor:
Miriam Carolina Chalon, Carlos Minahk, Daniela Estefanía Barraza, Natalia Soledad Ríos Colombo, Leonardo Acuña, Adriana Galván, Augusto Bellomio
Publikováno v:
Molecular Microbiology. 105:922-933
The role of the class IIa bacteriocin membrane receptor protein remains unclear, and the following two different mechanisms have been proposed: the bacteriocin could interact with the receptor changing it to an open conformation or the receptor might
Autor:
N. S. Ríos Colombo, Miriam Carolina Chalon, Leonardo Acuña, Silvia Adriana Navarro, M. Fernandez de Ullivarri, L. Lanza, Augusto Bellomio, B. Sosa-Padilla, Gianluca Picariello
Publikováno v:
Applied microbiology and biotechnology 103 (2019): 9607–9618. doi:10.1007/s00253-019-10187-5
info:cnr-pdr/source/autori:Navarro S.A.; Lanza L.; Colombo N.S.R.; de Ullivarri M.F.; Acuna L.; Sosa-Padilla B.; Picariello G.; Bellomio A.; Chalon M.C./titolo:Obtaining an Ent35-MccV derivative with mutated hinge region that exhibits increased activity against Listeria monocytogenes and Escherichia coli/doi:10.1007%2Fs00253-019-10187-5/rivista:Applied microbiology and biotechnology/anno:2019/pagina_da:9607/pagina_a:9618/intervallo_pagine:9607–9618/volume:103
info:cnr-pdr/source/autori:Navarro S.A.; Lanza L.; Colombo N.S.R.; de Ullivarri M.F.; Acuna L.; Sosa-Padilla B.; Picariello G.; Bellomio A.; Chalon M.C./titolo:Obtaining an Ent35-MccV derivative with mutated hinge region that exhibits increased activity against Listeria monocytogenes and Escherichia coli/doi:10.1007%2Fs00253-019-10187-5/rivista:Applied microbiology and biotechnology/anno:2019/pagina_da:9607/pagina_a:9618/intervallo_pagine:9607–9618/volume:103
The present paper describes the generation of derivatives from the hybrid peptide called Ent35-MccV, active against Gram-positive and Gram-negative bacteria. This peptide has a triple glycine hinge region between enterocin CRL35 and microcin V. In or
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fc4199fcc3ba4943c13abe2db35d76d
https://link.springer.com/article/10.1007/s00253-019-10187-5
https://link.springer.com/article/10.1007/s00253-019-10187-5
Autor:
Augusto Bellomio, Katia Gianni de Carvalho, Nora Ines Perotti, Romina Belén Parada, Marisol Vallejo, Johana Stefani Gomez, Emilio Rogelio Marguet
Publikováno v:
Archives of microbiology. 203(4)
Lactic acid bacteria can be considered as natural biopreservative and good biotechnological alternative to food safety. In this study, the antilisterial compounds produced by Enterococcus isolates from the Patagonian environment and their effectivene
Autor:
F.G. Dupuy, N. S. Ríos Colombo, Augusto Bellomio, Miriam Carolina Chalon, Claudio F. Gonzalez
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Class II bacteriocins are unmodified membrane-active peptides that act over a narrow spectrum of target bacteria. They bind a specific receptor protein on the membrane to form a pore, leading to membrane permeabilization and cell death. However, litt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14ffbf4995dff008ce5da3d2a74702e8
https://www.sciencedirect.com/science/article/pii/S030090841930224X
https://www.sciencedirect.com/science/article/pii/S030090841930224X
Autor:
Jose M. M. Caaveiro, Augusto Bellomio, Ana Rosa Viguera, Juan Manuel González-Mañas, Koldo Morante, Kouhei Tsumoto
Publikováno v:
Toxins, Vol 11, Iss 7, p 401 (2019)
Toxins
Volume 11
Issue 7
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Toxins
Volume 11
Issue 7
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Random mutations and selective pressure drive protein adaptation to the changing demands of the environment. As a consequence, nature favors the evolution of protein diversity. A group of proteins subject to exceptional environmental stress and known
Identification of a Membrane-bound Prepore Species Clarifies the Lytic Mechanism of Actinoporins * ♦
Autor:
Juan Manuel González-Mañas, Mikel Valle, Augusto Bellomio, Kouhei Tsumoto, David Gil-Carton, Koldo Morante, Jose M. M. Caaveiro, Jesús Sot, Simon Scheuring, Lorena Redondo-Morata
Publikováno v:
The Journal of Biological Chemistry
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2016, ⟨10.1074/jbc.M116.734053⟩
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2016, ⟨10.1074/jbc.M116.734053⟩
Pore-forming toxins (PFTs) are cytolytic proteins belonging to the molecular warfare apparatus of living organisms. The assembly of the functional transmembrane pore requires several intermediate steps ranging from a water-soluble monomeric species t
Autor:
Natalia S Corbalán, Augusto Bellomio, Jorge Barros-Velázquez, Leonardo Acuña, Marcos Quintela-Baluja
Publikováno v:
International Dairy Journal. 104:104650
Bacteriocins are antimicrobial peptides synthesised ribosomally. One of the main drawbacks of bacteriocins as food biopreservative agents is their restricted action spectrum. To obtain a broad-spectrum bacteriocin-producing lactic acid bacterium, we