Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Caroline M. Peneff"'
Publikováno v:
European Biophysics Journal. 41:259-271
NanC is an Escherichia coli outer membrane protein involved in sialic acid (Neu5Ac, i.e., N-acetylneuraminic acid) uptake. Expression of the NanC gene is induced and controlled by Neu5Ac. The transport mechanism of Neu5Ac is not known. The structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4e5d910db4e4898896eaba566b40668
https://doi.org/10.1007/s00249-011-0781-5
https://doi.org/10.1007/s00249-011-0781-5
Autor:
Simon Bernèche, Tilman Schirmer, Christophe Wirth, Céline Boiteux, Caroline M. Peneff, Guy Condemine
Publikováno v:
J Mol Biol
Sialic acids are acidic sugars present mostly on vertebrate cell surfaces, which can be metabolized by bacteria and act as an inflammation signal. N-Acetylneuraminic acid, the most abundant sialic acid, can enter into Escherichia coli K12 through Nan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cf809cc89bffc5b656ebedd00c9da42
Autor:
Miichael J. E. Hewlins, Michaela Markova, Caroline M. Peneff, Tilman Schirmer, Robert A. John
Publikováno v:
Journal of Biological Chemistry. 280:36409-36416
Ornithine aminotransferase and 4-aminobutyrate aminotransferase are related pyridoxal phosphate-dependent enzymes having different substrate specificities. The atomic structures of these enzymes have shown (i) that active site differences are limited
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30c0dc3b8c179fa22f1ff77e2622d5d4
https://doi.org/10.1074/jbc.m506977200
https://doi.org/10.1074/jbc.m506977200
Autor:
Daniela De Biase, Andrea Mozzarelli, Stefano Bruno, Richard B. Silverman, Paola Storici, Francesco Bossa, Caroline M. Peneff, Tilman Schirmer
Publikováno v:
Journal of Biological Chemistry. 279:363-373
Gamma-aminobutyric acid aminotransferase (GABA-AT) is a pyridoxal 5'-phosphate-dependent enzyme responsible for the degradation of the inhibitory neurotransmitter GABA. GABA-AT is a validated target for antiepilepsy drugs because its selective inhibi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0eb6586b2f2d53441be212fd74573676
https://doi.org/10.1074/jbc.m305884200
https://doi.org/10.1074/jbc.m305884200
Autor:
Caroline M. Peneff, Ch. Wirth, Roman Lehner, Guy Condemine, Cedric A. J. Hutter, Tilman Schirmer
Publikováno v:
Acta Crystallogr D Biol Crystallogr
Acta Crystallogr D Biol Crystallogr, 2014, 70 (Pt 6), pp.1770-8
Acta Crystallogr D Biol Crystallogr, 2014, 70 (Pt 6), pp.1770-8
The phytopathogenic Gram-negative bacteriumDickeya dadantii(Erwinia chrysanthemi) feeds on plant cell walls by secreting pectinases and utilizing the oligogalacturanate products. An outer membrane porin, KdgM, is indispensable for the uptake of these
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b442e6d3db3b15af244cb717a4d7ed87
https://hal.archives-ouvertes.fr/hal-02001306
https://hal.archives-ouvertes.fr/hal-02001306
Autor:
Bob Eisenberg, Christophe Wirth, J. M. Tang, Janhavi Giri, Tilman Schirmer, Caroline M. Peneff
Publikováno v:
Biophysical Journal. 100(3)
Sialic acid is a nutrient of bacteria important in host-pathogen interactions. The mechanism of transport of sialic acid from outer membrane to periplasmic space of Escherichia coli is not known. N-acetylneuraminic acid (Neu5Ac) - the most abundant f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3478dcd45e3e1d9d4510308a170a8088
Autor:
Janhavi Giri, Christophe Wirth, Bob Eisenberg, Caroline M. Peneff, J. M. Tang, Tilman Schirmer
Publikováno v:
Biophysical Journal. 100:579a
Escherichia coli can use N-acetylneuraminic acid (Neu5Ac) as its sole carbon source even if the general outer membrane proteins OmpF and OmpC are not expressed: NanC - a monomeric outer membrane channel - allows Neu5Ac to move into the bacterial peri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::787e525f2d8f40b23b685e0ae27b0867
https://doi.org/10.1016/j.bpj.2010.12.3348
https://doi.org/10.1016/j.bpj.2010.12.3348