Items where Author is "Blair, Jessica MA"
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Blair, Jessica MA and Zeth, Kornelius and Bavro, Vassiliy N and Sancho-Vaello, Enea (2022) The role of bacterial transport systems in the removal of host antimicrobial peptides in Gram-negative bacteria. FEMS Microbiology Reviews, 46 (6). fuac032-fuac032. DOI https://doi.org/10.1093/femsre/fuac032
Alav, Ilyas and Bavro, Vassiliy N and Blair, Jessica MA (2022) A role for the periplasmic adaptor protein AcrA in vetting substrate access to the RND efflux transporter AcrB. Scientific Reports, 12 (1). 4752-. DOI https://doi.org/10.1038/s41598-022-08903-9
Alav, Ilyas and Bavro, Vassiliy N and Blair, Jessica MA (2021) Interchangeability of periplasmic adaptor proteins AcrA and AcrE in forming functional efflux pumps with AcrD in Salmonella enterica serovar Typhimurium. Journal of Antimicrobial Chemotherapy, 76 (10). pp. 2558-2564. DOI https://doi.org/10.1093/jac/dkab237
Alav, Ilyas and Kobylka, Jessica and Kuth, Miriam S and Pos, Klaas M and Picard, Martin and Blair, Jessica MA and Bavro, Vassiliy N (2021) Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria. Chemical Reviews, 121 (9). pp. 5479-5596. DOI https://doi.org/10.1021/acs.chemrev.1c00055
McNeil, Helen E and Alav, Ilyas and Corona Torres, Ricardo and Rossiter, Amanda E and Laycock, Eve and Legood, Simon and Kaur, Inderpreet and Davies, Matthew and Wand, Matthew and Webber, Mark A and Bavro, Vassiliy N and Blair, Jessica MA (2019) Identification of binding residues between periplasmic adapter protein (PAP) and RND efflux pumps explains PAP-pump promiscuity and roles in antimicrobial resistance. PLoS Pathogens, 15 (12). e1008101-e1008101. DOI https://doi.org/10.1371/journal.ppat.1008101
Blair, Jessica MA and Bavro, Vassiliy N and Ricci, Vito and Modi, Niraj and Cacciotto, Pierpaolo and Kleinekathӧfer, Ulrich and Ruggerone, Paolo and Vargiu, Attilio V and Baylay, Alison J and Smith, Helen E and Brandon, Yvonne and Galloway, David and Piddock, Laura JV (2015) AcrB drug-binding pocket substitution confers clinically relevant resistance and altered substrate specificity. Proceedings of the National Academy of Sciences, 112 (11). pp. 3511-3516. DOI https://doi.org/10.1073/pnas.1419939112