Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Rasem J. Fattah"'
Autor:
Christopher Bachran, Thomas Morley, Suzanne Abdelazim, Rasem J. Fattah, Shihui Liu, Stephen H. Leppla
Publikováno v:
mBio, Vol 4, Iss 3 (2013)
ABSTRACT Anthrax toxin proteins from Bacillus anthracis constitute a highly efficient system for delivering cytotoxic enzymes to the cytosol of tumor cells. However, exogenous proteins delivered to the cytosol of cells are subject to ubiquitination o
Externí odkaz:
https://doaj.org/article/bf0f3719e73844cda27ef4d099143852
Autor:
Megan A. Mendenhall, Makayla K. Portley, Shihui Liu, Rasem J. Fattah, Mahtab Moayeri, Jaspal S. Khillan, Danielle O'Mard, Stephen H. Leppla, Roman Szabo, Thomas H. Bugge
Publikováno v:
Nature Microbiology. 5:1464-1471
Anthrax lethal toxin (LT), produced by Bacillus anthracis, comprises a receptor-binding moiety, protective antigen and the lethal factor (LF) protease1,2. Although LF is known to cleave mitogen-activated protein kinase kinases (MEKs/MKKs) and some va
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0dd70570cdbb89816b977fdee0bc9136
https://doi.org/10.1038/s41564-020-0782-1
https://doi.org/10.1038/s41564-020-0782-1
Autor:
Carly Merritt, Elizabeth M. Chun, Rasem J. Fattah, Lakmali M. Silva, Quinn Q. Ma, Mahtab Moayeri, Dennis Paliga, Sebastian Neumann, Rolf Heumann, Stephen H. Leppla, Thomas H. Bugge
Publikováno v:
The Journal of Biological Chemistry
Bacillus anthracis lethal toxin and edema toxin are binary toxins that consist of a common cell-binding moiety, protective antigen (PA), and the enzymatic moieties, lethal factor (LF) and edema factor (EF). PA binds to either of two receptors, capill
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b8e85493ae8fb0793c10733cb1de80e
https://pubmed.ncbi.nlm.nih.gov/34871548
https://pubmed.ncbi.nlm.nih.gov/34871548
Autor:
Carly Merritt, Stephen H. Leppla, Dennis Paliga, Rasem J. Fattah, Sebastian Neumann, Mahtab Moayeri, Rolf Heumann, Thomas H. Bugge, Elizabeth M. Chun
SUMMARYThe virulence of Bacillus anthracis is linked to the secretion of anthrax lethal toxin and anthrax edema toxin. These binary toxins consist of a common cell-binding moiety, protective antigen (PA), and the enzymatic moieties, lethal factor (LF
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4850fdfb0dbca3cea5aad13b71137380
https://doi.org/10.1101/2021.01.22.427304
https://doi.org/10.1101/2021.01.22.427304
Autor:
Clinton E Leysath, Damilola D Phillips, Devorah Crown, Rasem J Fattah, Mahtab Moayeri, Stephen H Leppla
Publikováno v:
PLoS ONE, Vol 8, Iss 8, p e74474 (2013)
Anthrax edema factor (EF) is a calmodulin-dependent adenylate cyclase that converts adenosine triphosphate (ATP) into 3'-5'-cyclic adenosine monophosphate (cAMP), contributing to the establishment of Bacillus anthracis infections and the resulting pa
Externí odkaz:
https://doaj.org/article/d701bb7f450b4a3abdf78239ed8bf81f
Publikováno v:
PLoS ONE, Vol 3, Iss 9, p e3130 (2008)
Anthrax lethal factor (LF) is a Zn(+2)-dependent metalloprotease that cleaves several MAPK kinases and is responsible for the lethality of anthrax lethal toxin (LT). We observed that a recombinant LF (LF-HMA) which differs from wild type LF (LF-A) by
Externí odkaz:
https://doaj.org/article/ee71ed6670784ed09734e9851a61131b
Publikováno v:
Oncotarget
// Shihui Liu 1, 2 , Qian Ma 2 , Rasem Fattah 2 , Thomas H. Bugge 1 and Stephen H. Leppla 2 1 Proteases and Tissue Remodeling Section, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892, USA 2 Mi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::773165993526bcb2e347728714b0548c
https://doi.org/10.18632/oncotarget.17729
https://doi.org/10.18632/oncotarget.17729
Autor:
Margaret Chahoud, Andrei P. Pomerantsev, Rita M. McCall, Rasem J. Fattah, Stephen H. Leppla, Nathan K. Hepler
Publikováno v:
PLoS ONE, Vol 12, Iss 8, p e0183346 (2017)
PLoS ONE
PLoS ONE
Tyrosine site-specific recombinases (T-SSR) are polynucleotidyltransferases that catalyze cutting and joining reactions between short specific DNA sequences. We developed three systems for performing genetic modifications in Bacillus anthracis that u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6c75149d64156c7e2625f82486eac52
http://europepmc.org/articles/PMC5567495?pdf=render
http://europepmc.org/articles/PMC5567495?pdf=render
Autor:
Shihui Liu, Elizabeth R. Fischer, Rodolfo Ghirlando, Clinton E. Leysath, Ekaterina M. Nestorovich, Rasem J. Fattah, Damilola D. Phillips, Yi Zhang, Lacy Simons, Stephen H. Leppla, Mahtab Moayeri, Bryan Hansen, Alexander N. Wein, Devorah Crown
Publikováno v:
Journal of Biological Chemistry. 288:9058-9065
Anthrax toxin protective antigen (PA) delivers its effector proteins into the host cell cytosol through formation of an oligomeric pore, which can assume heptameric or octameric states. By screening a highly directed library of PA mutants, we identif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c945f66c6ec16e69ec481a23b3e053a9
https://doi.org/10.1074/jbc.m113.452110
https://doi.org/10.1074/jbc.m113.452110
Publikováno v:
Biochemical and Biophysical Research Communications. 430:150-155
Many recombinant therapeutic proteins are purified from Escherichia coli. While expression in E. coli is easily achieved, some disadvantages such as protein aggregation, formation of inclusion bodies, and contamination of purified proteins with the l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b5bfc2a3076dd11696ba43303927b42
https://doi.org/10.1016/j.bbrc.2012.11.055
https://doi.org/10.1016/j.bbrc.2012.11.055