Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Bronte A Johnstone"'
Autor:
Pantelis Poumbourios, Christine Langer, Irene Boo, Tasnim Zakir, Rob J Center, Anouschka Akerman, Vanessa Milogiannakis, Anupriya Aggarwal, Bronte A Johnstone, Jungmin Ha, Fasséli Coulibaly, Stuart G Turville, Heidi E Drummer
Publikováno v:
PLoS Pathogens, Vol 19, Iss 5, p e1010981 (2023)
The spike (S) glycoprotein of SARS CoV-2 is the target of neutralizing antibodies (NAbs) that are crucial for vaccine effectiveness. The S1 subunit binds ACE2 while the S2 subunit mediates virus-cell membrane fusion. S2 is a class I fusion glycoprote
Externí odkaz:
https://doaj.org/article/6d3cf0974e2e42daa96111a1d687d350
Autor:
Hunter L. Abrahamsen, Tristan C. Sanford, Casie E. Collamore, Bronte A. Johnstone, Michael J. Coyne, Leonor García-Bayona, Michelle P. Christie, Jordan C. Evans, Allison J. Farrand, Katia Flores, Craig J. Morton, Michael W. Parker, Laurie E. Comstock, Rodney K. Tweten
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract Cholesterol-dependent cytolysins (CDCs) comprise a large family of pore-forming toxins produced by Gram-positive bacteria, which are used to attack eukaryotic cells. Here, we functionally characterize a family of 2-component CDC-like (CDCL)
Externí odkaz:
https://doaj.org/article/fa81631103bf486aa966a456bbef1768
Autor:
Jordan C. Evans, Bronte A. Johnstone, Sara L. Lawrence, Craig J. Morton, Michelle P. Christie, Michael W. Parker, Rodney K. Tweten
Publikováno v:
mBio, Vol 11, Iss 5 (2020)
ABSTRACT The cholesterol-dependent cytolysins (CDCs) are bacterial, β-barrel, pore-forming toxins. A central enigma of the pore-forming mechanism is how completion of the prepore is sensed to initiate its conversion to the pore. We identified a moti
Externí odkaz:
https://doaj.org/article/c68956bf53bd4654a2ba9c2e4b08d948
Autor:
Bronte A. Johnstone, Riya Joseph, Michelle P. Christie, Craig J. Morton, Conall McGuiness, James C. Walsh, Till Böcking, Rodney K. Tweten, Michael W. Parker
Publikováno v:
IUBMB Life. 74:1169-1179
The cholesterol-dependent cytolysins (CDCs) are a major family of bacterial pore-forming proteins secreted as virulence factors by Gram-positive bacterial species. CDCs are produced as soluble, monomeric proteins that bind specifically to cholesterol
Publikováno v:
Methods in enzymology. 649
A common form of cellular attack by pathogenic bacteria is to secrete pore-forming toxins (PFTs). Capable of forming transmembrane pores in various biological membranes, PFTs have also been identified in a diverse range of other organisms such as sea
Publikováno v:
Methods in Enzymology ISBN: 9780128238585
A common form of cellular attack by pathogenic bacteria is to secrete pore-forming toxins (PFTs). Capable of forming transmembrane pores in various biological membranes, PFTs have also been identified in a diverse range of other organisms such as sea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cdfec538d72f97b3f1e0fdc74fc997a3
https://doi.org/10.1016/bs.mie.2021.01.001
https://doi.org/10.1016/bs.mie.2021.01.001
Autor:
Michelle P. Christie, Sara L. Lawrence, Bronte A Johnstone, Michael W. Parker, Rodney K. Tweten, Craig J. Morton, Jordan C Evans
Publikováno v:
mBio, Vol 11, Iss 5 (2020)
mBio
mBio
The cholesterol-dependent cytolysins’ pore-forming mechanism relies on the ability to sense the completion of the oligomeric prepore structure and initiate the insertion of the β-barrel pore from the assembled prepore structure. These studies show
Autor:
Bronte A. Johnstone, Sara L. Lawrence, Craig J. Morton, Jordan C. Evans, Michelle P. Christie, Rodney K. Tweten, Michael W. Parker
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 77:C482-C482
Autor:
Rodney K. Tweten, Michael W. Parker, Craig J. Morton, Bronte A Johnstone, Michelle P. Christie
Publikováno v:
Biophysical reviews. 10(5)
The cholesterol-dependent cytolysins (CDCs) are a family of bacterial toxins that are important virulence factors for a number of pathogenic Gram-positive bacterial species. CDCs are secreted as soluble, stable monomeric proteins that bind specifical