Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Eamonn, Reading"'
Autor:
Benjamin Russell Lewis, Muhammad R. Uddin, Mohammad Moniruzzaman, Katie M. Kuo, Anna J. Higgins, Laila M. N. Shah, Frank Sobott, Jerry M. Parks, Dietmar Hammerschmid, James C. Gumbart, Helen I. Zgurskaya, Eamonn Reading
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
Abstract Membrane efflux pumps play a major role in bacterial multidrug resistance. The tripartite multidrug efflux pump system from Escherichia coli, AcrAB-TolC, is a target for inhibition to lessen resistance development and restore antibiotic effi
Externí odkaz:
https://doaj.org/article/db36206389534e89aa35837123b7295a
Autor:
Valeria Calvaresi, Antoni G. Wrobel, Joanna Toporowska, Dietmar Hammerschmid, Katie J. Doores, Richard T. Bradshaw, Ricardo B. Parsons, Donald J. Benton, Chloë Roustan, Eamonn Reading, Michael H. Malim, Steve J. Gamblin, Argyris Politis
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
In this paper, the authors use hydrogen-deuterium exchange mass spectrometry to describe how the SARS-CoV-2 spike glycoprotein has evolved its structural dynamics features and receptor binding capability from the emergence of the original Wuhan isola
Externí odkaz:
https://doaj.org/article/97f9efb389ef48dfa07633acc7b2d899
Autor:
Eamonn Reading, Zainab Ahdash, Chiara Fais, Vito Ricci, Xuan Wang-Kan, Elizabeth Grimsey, Jack Stone, Giuliano Malloci, Andy M. Lau, Heather Findlay, Albert Konijnenberg, Paula J. Booth, Paolo Ruggerone, Attilio V. Vargiu, Laura J. V. Piddock, Argyris Politis
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
AcrB is a prototypical resistance–nodulation–division (RND) bacterial transporter, conferring resistance to a variety of antibiotics. HDX-MS and other, complementary approaches offer insight into AcrB structural dynamics and suggest the molecular
Externí odkaz:
https://doaj.org/article/f67d2dabeba6419d899fd8c49aa914be
Autor:
Chloe Martens, Mrinal Shekhar, Antoni J. Borysik, Andy M. Lau, Eamonn Reading, Emad Tajkhorshid, Paula J. Booth, Argyris Politis
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Secondary transporters catalyse substrate translocation across the cell membrane but the role of lipids during the transport cycle remains unclear. Here authors used hydrogen-deuterium exchange mass spectrometry and molecular dynamics simulations to
Externí odkaz:
https://doaj.org/article/3878486fe69c4a06a829c58c6f048e54
Autor:
Nicola J. Harris, Eamonn Reading, Kenichi Ataka, Lucjan Grzegorzewski, Kalypso Charalambous, Xia Liu, Ramona Schlesinger, Joachim Heberle, Paula J. Booth
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-15 (2017)
Abstract Correctly folded membrane proteins underlie a plethora of cellular processes, but little is known about how they fold. Knowledge of folding mechanisms centres on reversible folding of chemically denatured membrane proteins. However, this can
Externí odkaz:
https://doaj.org/article/8f8480ca6af2428ea155c29546970aae
Autor:
Dietmar Hammerschmid, Valeria Calvaresi, Chloe Bailey, Benjamin Russell Lewis, Argyris Politis, Michael Morris, Laetitia Denbigh, Malcolm Anderson, Eamonn Reading
Lipid interactions modulate the function, folding, structure, and organization of membrane proteins. Hydrogen/deuterium exchange mass spectrometry (HDX-MS) has emerged as a useful tool to understand the structural dynamics of these proteins within li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0b7feeaff864ee0f469c13579af8a8c
https://eprints.soton.ac.uk/478873/
https://eprints.soton.ac.uk/478873/
Autor:
Benjamin Russell Lewis, Muhammad R. Uddin, Mohammad Moniruzzaman, Katie M. Kuo, Anna J. Higgins, Laila M. N. Shah, Frank Sobott, Jerry M. Parks, Dietmar Hammerschmid, James C. Gumbart, Helen I. Zgurskaya, Eamonn Reading
Membrane efflux pumps play a major role in bacterial multidrug resistance. The tripartite multidrug efflux pump system fromEscherichia coli, AcrAB-TolC, is a target for inhibition to lessen resistance development and restore antibiotic efficacy, with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4585e9969a8c7f87dfeb44bb38352d67
https://doi.org/10.1101/2022.12.09.519754
https://doi.org/10.1101/2022.12.09.519754
Autor:
Dietmar Hammerschmid, Valeria Calvaresi, Chloe Bailey, Benjamin Russell Lewis, Argyris Politis, Mike Morris, Laetitia Denbigh, Malcolm Anderson, Eamonn Reading
Lipid interactions modulate the function, folding, structure, and organization of membrane proteins. Hydrogen/deuterium exchange mass spectrometry (HDX-MS) has emerged as a useful tool to understand the structural dynamics of these proteins within li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a15a98c479bd304728e9688be6000ef8
https://doi.org/10.26434/chemrxiv-2022-8j01g
https://doi.org/10.26434/chemrxiv-2022-8j01g
Publikováno v:
Russell Lewis, B, Lawrence, R, Hammerschmid, D & Reading, E 2022, ' Structural mass spectrometry approaches to understand multidrug efflux systems ', Essays in Biochemistry . https://doi.org/10.1042/EBC20220190
Multidrug efflux pumps are ubiquitous across both eukaryotes and prokaryotes, and have major implications in antimicrobial and multidrug resistance. They reside within cellular membranes and have proven difficult to study owing to their hydrophobic c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b158172614c597b8824d1750a31d9517
https://pubmed.ncbi.nlm.nih.gov/36504255
https://pubmed.ncbi.nlm.nih.gov/36504255
Autor:
Valeria Calvaresi, Antoni Wrobel, Joanna Toporowska, Dietmar Hammerschmid, Katie Doores, Richard Bradshaw, Ricardo Parsons, Donald Benton, Chloe Roustan, Eamonn Reading, Michael Malim, Steve Gamblin, Argyris Politis
SARS-CoV-2 spike glycoprotein mediates receptor binding and subsequent membrane fusion. It exists in a range of conformations, including a closed state unable to bind the ACE2 receptor, and an open state that does so but displays more exposed antigen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ccedfd6d61b6fbc85543d97dc1f51192
https://doi.org/10.21203/rs.3.rs-2049401/v1
https://doi.org/10.21203/rs.3.rs-2049401/v1