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of 3
pro vyhledávání: '"Adrià Mayo"'
Autor:
Daniel Yero, Mireia Díaz-Lobo, Lionel Costenaro, Oscar Conchillo-Solé, Adrià Mayo, Mario Ferrer-Navarro, Marta Vilaseca, Isidre Gibert, Xavier Daura
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-16 (2021)
Yero et al. elucidate the function of Ttg2D, a Pseudomonas aeruginosa periplasmic protein, in maintaining phospholipid asymmetry between the outer and inner membrane. Gram negative bacteria have inner and outer membranes that differ in phospholipd co
Externí odkaz:
https://doaj.org/article/50977891a64d4ef6a08754ef5a6e7656
Autor:
Oscar Conchillo-Solé, Mario Ferrer-Navarro, Marta Vilaseca, Isidre Gibert, Lionel Costenaro, Mireia Díaz-Lobo, Adrià Mayo, Daniel Yero, Xavier Daura
In Pseudomonas aeruginosa, Ttg2D is the soluble periplasmic phospholipid-binding component of an ABC transport system thought to be involved in maintaining the asymmetry of the outer membrane. The crystallographic structure of Ttg2D at 2.5 Å resolut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0da4d370277706a517c64a90cd3cbb2e
https://doi.org/10.21203/rs.3.rs-89298/v1
https://doi.org/10.21203/rs.3.rs-89298/v1
Autor:
Isidre Gibert, Daniel Yero, Adrià Mayo, Oscar Conchillo-Solé, Lionel Costenaro, Xavier Daura, Mireia Díaz-Lobo, Marta Vilaseca, Mario Ferrer-Navarro
InPseudomonas aeruginosa, Ttg2D is the soluble periplasmic phospholipid-binding component of an ABC transport system thought to be involved in maintaining the asymmetry of the outer membrane. The crystallographic structure of Ttg2D at 2.5Å resolutio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88105916803eaaa4072a5ec16933bbb0