V. Bavro

发表

Structural and Functional Analysis of the Escherichia coli Acid-Sensing Histidine Kinase EvgS

Hrishiraj Sen, N. Aggarwal, Chibueze Ishionwu, 2017, Journal of bacteriology.

Structure of a KirBac potassium channel with an open bundle-crossing indicates a mechanism of channel gating

C. Venien-Bryan, M. Sansom, R. De Zorzi, 2011, Nature Structural &Molecular Biology.

Functional Complementation and Genetic Deletion Studies of KirBac Channels

M. Sansom, C. Nichols, V. Bavro, 2010, The Journal of Biological Chemistry.

Conformational changes during the gating of a potassium channel revealed by structural mass spectrometry.

M. Chance, C. Venien-Bryan, Sayan Gupta, 2010, Structure.

A role for the periplasmic adaptor protein AcrA in vetting substrate access to the RND efflux transporter AcrB

V. Bavro, Jessica M. A. Blair, Ilyas Alav, 2022, Scientific Reports.

Cefotaxime Exposure Selects Mutations within the CA-Domain of envZ Which Promote Antibiotic Resistance but Repress Biofilm Formation in Salmonella

G. Savva, V. Bavro, Eleftheria Trampari, 2022, Microbiology spectrum.

Interchangeability of periplasmic adaptor proteins AcrA and AcrE in forming functional efflux pumps with AcrD in Salmonella enterica serovar Typhimurium

V. Bavro, Vassiliy N. Bavro, Ilyas Alav, 2021, The Journal of antimicrobial chemotherapy.

Cryo-EM Structure and Molecular Dynamics Analysis of the Fluoroquinolone Resistant Mutant of the AcrB Transporter from Salmonella

Robert L. Marshall, P. Ruggerone, A. Vargiu, 2020, Microorganisms.

Antibiotics select for novel pathways of resistance in biofilms

M. Webber, G. Savva, V. Bavro, 2019, bioRxiv.

Identification of binding residues between periplasmic adapter protein (PAP) and RND efflux pumps explains PAP-pump promiscuity and roles in antimicrobial resistance

M. Davies, M. Webber, V. Bavro, 2019, PLoS pathogens.

Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation

I. Henderson, T. Lithgow, A. Cunningham, 2020, eLife.

Structure-function analyses of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation

I. Henderson, M. Overduin, T. Lithgow, 2020 .

Cytoplasmic Domains Gating at the Interface between Control of KirBac3.1 Potassium Channel Membrane Biology

C. Venien-Bryan, C. Nichols, V. Bavro, 2014 .

University of Birmingham Architecture and roles of periplasmic adaptor proteins in tripartite eux assemblies

Robert L. Marshall, V. Bavro, M. Symmons, 2015 .

MacB ABC Transporter Is a Dimer Whose ATPase Activity and Macrolide-binding Capacity Are Regulated by the Membrane Fusion Protein MacA*S⃞

C. Robinson, V. Bavro, H. V. van Veen, 2009, Journal of Biological Chemistry.

Cefotaxime Exposure Selects Mutations within the CA-Domain of envZ Which Promote Antibiotic Resistance but Repress Biofilm Formation in Salmonella

G. Savva, V. Bavro, Eleftheria Trampari, 2022, Microbiology spectrum.

RND pumps across the Acinetobacter genus; AdeIJK is the ancestral efflux system

V. Bavro, S. Dunn, A. McNally, 2022, bioRxiv.

Multidrug Resistance

Robert L. Marshall, V. Bavro, Vassiliy N. Bavro, 2019, Bacterial Resistance to Antibiotics – From Molecules to Man.

The role of bacterial transport systems in the removal of host antimicrobial peptides in Gram-negative bacteria

E. Sancho-Vaello, K. Zeth, V. Bavro, 2022, FEMS microbiology reviews.

The membrane-proximal domain of the periplasmic adapter protein plays a role in vetting substrates utilising channels 1 and 2 of RND efflux transporters

V. Bavro, Ilyas Alav, J. Blair, 2021, bioRxiv.

Ion mobility mass spectrometry of two tetrameric membrane protein complexes reveals compact structures and differences in stability and packing.

C. Robinson, P. Booth, V. Bavro, 2010, Journal of the American Chemical Society.

Outer membrane protein size and LPS O-antigen define protective antibody targeting to the Salmonella surface

I. Henderson, A. Cunningham, J. Gumbart, 2020, Nature Communications.

Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria

M. Picard, V. Bavro, K. M. Pos, 2021, Chemical reviews.

Mutations in the TolC Periplasmic Domain Affect Substrate Specificity of the AcrAB-TolC Pump

Robert L. Marshall, V. Bavro, Vassiliy N. Bavro, 2020, Frontiers in Molecular Biosciences.

Multidrug Efflux in the Context of Two-Membrane Cell Envelopes

Jon W. Weeks, H. Zgurskaya, V. Bavro, 2016 .

Architecture and roles of periplasmic adaptor proteins in tripartite eﬄux assemblies

Robert L. Marshall, V. Bavro, M. Symmons, 2015, Front. Microbiol..

Structure and mechanism of drug efflux machinery in Gram negative bacteria.

B. Luisi, Nicholas Furnham, E. Milner-White, 2008, Current drug targets.

ATP-Binding Cassette Transporter VcaM from Vibrio cholerae is Dependent on the Outer Membrane Factor Family for Its Function

V. Bavro, H. Lin, Wen-Jung Lu, 2018, International journal of molecular sciences.

Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions

Min Zhou, Ricardo Núñez Miguel, Christopher G Tate, 2009, Nature Methods.

Assembly and transport mechanism of tripartite drug efflux systems.

V. Bavro, R. Misra, Vassiliy N. Bavro, 2009, Biochimica et biophysica acta.

Assembly & Transport Mechanism of Tripartite Drug Efflux Systems

V. Bavro, R. Misra, Vassiliy N. Bavro, 2009 .

Quantitative real-time analysis of the efflux by the MacAB-TolC tripartite efflux pump clarifies the role of ATP hydrolysis within mechanotransmission mechanism

L. Catoire, M. Picard, V. Bavro, 2021, Communications biology.