Zobrazeno 1 - 10
of 46
pro vyhledávání: '"James G, Bann"'
Autor:
Fabiana Freire Mendes de Oliveira, Sireesha Mamillapalli, Srinivas Gonti, Robert N. Brey, Han Li, Jarad Schiffer, Arturo Casadevall, James G. Bann
Publikováno v:
mSphere, Vol 5, Iss 1 (2020)
ABSTRACT Protective antigen (PA) is a component of anthrax toxin that can elicit toxin-neutralizing antibody responses. PA is also the major antigen in the current vaccine to prevent anthrax, but stability problems with recombinant proteins have comp
Externí odkaz:
https://doaj.org/article/c5b08a3442284ba9b28cd6995fad9269
Autor:
David J. Evans, Alexa M. Wasinger, Robert N. Brey, James M. Dunleavey, Brad St. Croix, James G. Bann
Publikováno v:
Frontiers in Oncology, Vol 8 (2018)
Recent studies reveal that Seneca Valley Virus (SVV) exploits tumor endothelial marker 8 (TEM8) for cellular entry, the same surface receptor pirated by bacterial-derived anthrax toxin. This observation is particularly significant as SVV is a known o
Externí odkaz:
https://doaj.org/article/d6c13bb13a814536ad175b6016d94bce
Publikováno v:
Biochemistry
The anthrax toxin protective antigen (PA), the membrane binding and pore-forming component of the anthrax toxin, was studied using (19)F NMR. We site-specifically labeled PA with p-fluorophenylalanine (pF-Phe) at Phe427, a critically important residu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::447c4b841322f2a5b6128bdc2c8c8de3
https://europepmc.org/articles/PMC8991541/
https://europepmc.org/articles/PMC8991541/
Autor:
Harry Scott, Wei Huang, Kiran Andra, Sireesha Mamillapalli, Srinivas Gonti, Alexander Day, Kaiming Zhang, Nurjahan Mehzabeen, Kevin P. Battaile, Anjali Raju, Scott Lovell, James G. Bann, Derek J. Taylor
Publikováno v:
Journal of Molecular Biology. 434:167548
The tripartite protein complex produced by anthrax bacteria (Bacillus anthracis) is a member of the AB family of β-barrel pore-forming toxins. The protective antigen (PA) component forms an oligomeric prepore that assembles on the host cell surface
Autor:
Kevin P. Battaile, Kaiming Zhang, Scott Lovell, Wei Huang, Derek J. Taylor, Srinivas Gonti, James G. Bann, N. Mehzabeen, Alexander Day, Harry Scott
Anthrax is a severe bacterial infection caused by Bacillus anthracis, which produces a tripartite toxin that includes protective antigen (PA), lethal factor (LF) and edema factor (EF). A series of dominant-negative mutations have been previously iden
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::04f68dc84fe32c965eede9ab1b53a64f
https://doi.org/10.1101/2020.06.15.152231
https://doi.org/10.1101/2020.06.15.152231
Autor:
Sireesha Mamillapalli, James G. Bann, Jarad Schiffer, Srinivas Gonti, Han Li, Fabiana Freire Mendes de Oliveira, Arturo Casadevall, Robert N. Brey
Publikováno v:
mSphere
mSphere, Vol 5, Iss 1 (2020)
mSphere, Vol 5, Iss 1, p e00556-19 (2020)
mSphere, Vol 5, Iss 1 (2020)
mSphere, Vol 5, Iss 1, p e00556-19 (2020)
The anthrax toxin PA is the major immunogen in the current anthrax vaccine (anthrax vaccine adsorbed). Improving the anthrax vaccine for avoidance of a cold chain necessitates improvements in the thermodynamic stability of PA. We address how stabiliz
Publikováno v:
Protein Science. 27:1544-1556
The beta pore-forming proteins (β-PFPs) are a large class of polypeptides that are produced by all Kingdoms of life to contribute to their species' own survival. Pore assembly is a sophisticated multi-step process that includes receptor/membrane rec
Publikováno v:
Acta Crystallographica Section E, Vol 66, Iss 11, Pp o2713-o2713 (2010)
The title compound, C6H8FN3O2, an analog of histidine, shows a reduced side-chain pKa (ca 1). The title structure exhibits a shortening of the bond between the proximal ring N atom and the F-substituted ring C atom, indicating an increase in π-bond
Externí odkaz:
https://doaj.org/article/0815a4a300584fa099b45b68e0a04513
Publikováno v:
Protein Science. 26:355-364
The major immunogenic component of the current anthrax vaccine, anthrax vaccine adsorbed (AVA) is protective antigen (PA). We have shown recently that the thermodynamic stability of PA can be significantly improved by binding to the Von-Willebrand fa
Publikováno v:
Biochemistry. 60:1242-1242