Zobrazeno 1 - 6
of 6
pro vyhledávání: '"M. Pilar Argente"'
Autor:
Christopher J. Day, Alvin W. Lo, Lauren E. Hartley-Tassell, M. Pilar Argente, Jessica Poole, Nathan P. King, Joe Tiralongo, Michael P. Jennings, Mark A. Schembri
Publikováno v:
mBio, Vol 12, Iss 1 (2021)
Understanding the tropism of pathogens for host and tissue requires a complete understanding of the host receptors targeted by fimbrial adhesins. Furthermore, blocking adhesion is a promising strategy to counter increasing antibiotic resistance and i
Externí odkaz:
https://doaj.org/article/093d6be022874964af90f81d63861f6b
Autor:
Joe Tiralongo, Jessica Poole, Lauren E. Hartley-Tassell, Alvin W. Lo, M. Pilar Argente, Michael P. Jennings, Mark A. Schembri, Nathan P. King, Christopher J. Day
Publikováno v:
mBio, Vol 12, Iss 1 (2021)
mBio
mBio
Chaperone-usher (CU) fimbriae are the most abundant Gram-negative bacterial fimbriae, with 38 distinct CU fimbria types described in Escherichia coli alone. Some E. coli CU fimbriae have been well characterized and bind to specific glycan targets to
Autor:
Samantha L. Taylor, Fabian Kurth, Mark J. Howard, Mark A. Schembri, Alastair G. McEwan, Nathan P. King, M. Pilar Argente, Begoña Heras, Gordon J. King, Maud E. S. Achard, Mark Shepherd
Publikováno v:
Antioxidants & Redox Signaling. 19:1494-1506
Aims: The prototypical protein disulfide bond (Dsb) formation and protein refolding pathways in the bacterial periplasm involving Dsb proteins have been most comprehensively defined in Escherichia coli. However, genomic analysis has revealed several
Autor:
Karrera Y. Djoko, M. Pilar Argente, JiaQi Ng, Stephen P. Kidd, Michael P. Jennings, Alastair G. McEwan
Publikováno v:
Metallomics : integrated biometal science. 3(10)
We have identified a novel regulator from the MerR family of transcription factors in the bacterial pathogen Haemophilus influenzae (HI1623; nickel-associated merR-like Regulator--NimR). NimR regulates the expression of a Ni(2+) uptake transporter (N
Autor:
Begoña Heras, Stephen R. Shouldice, Timothy J. Wells, Alastair G. McEwan, M. Pilar Argente, Gregor Gunčar, Makrina Totsika, Maud E. S. Achard, Mark A. Schembri, Russell Jarrott
Publikováno v:
The Journal of biological chemistry. 285(24)
In prototypic Escherichia coli K-12 the introduction of disulfide bonds into folding proteins is mediated by the Dsb family of enzymes, primarily through the actions of the highly oxidizing protein EcDsbA. Homologues of the Dsb catalysts are found in
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