Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Peter Brzovic"'
Autor:
Atanas Radkov, Anne L Sapiro, Sebastian Flores, Corey Henderson, Hayden Saunders, Rachel Kim, Steven Massa, Samuel Thompson, Chase Mateusiak, Jacob Biboy, Ziyi Zhao, Lea M Starita, William L Hatleberg, Waldemar Vollmer, Alistair B Russell, Jean-Pierre Simorre, Spencer Anthony-Cahill, Peter Brzovic, Beth Hayes, Seemay Chou
Publikováno v:
eLife, Vol 11 (2022)
Members of the bacterial T6SS amidase effector (Tae) superfamily of toxins are delivered between competing bacteria to degrade cell wall peptidoglycan. Although Taes share a common substrate, they exhibit distinct antimicrobial potency across differe
Externí odkaz:
https://doaj.org/article/e8b6e88e62cc4ba1b7e72be730157666
Autor:
W. Ryan Will, Peter Brzovic, Isolde Le Trong, Ronald E. Stenkamp, Matthew B. Lawrenz, Joyce E. Karlinsey, William W. Navarre, Kara Main-Hester, Virginia L. Miller, Stephen J. Libby, Ferric C. Fang
Publikováno v:
mBio, Vol 10, Iss 2 (2019)
ABSTRACT Gene duplication and subsequent evolutionary divergence have allowed conserved proteins to develop unique roles. The MarR family of transcription factors (TFs) has undergone extensive duplication and diversification in bacteria, where they a
Externí odkaz:
https://doaj.org/article/6e89773f3ee944aa996a1cf09ab4bf04
Publikováno v:
Trends Biochem Sci
Mutations in BRCA1 and BARD1 predispose carriers to breast and ovarian cancers. The BRCA1 and BARD1 proteins form a heterodimeric complex (BRCA1/BARD1) that regulates many biological processes, including transcription and DNA double-stranded break re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da9b9b857817711fe30eb445cac9b1f7
https://doi.org/10.1016/j.tibs.2022.03.001
https://doi.org/10.1016/j.tibs.2022.03.001
Autor:
Atanas Radkov, Anne L Sapiro, Sebastian Flores, Corey Henderson, Hayden Saunders, Rachel Kim, Steven Massa, Samuel Thompson, Chase Mateusiak, Jacob Biboy, Ziyi Zhao, Lea M Starita, William L Hatleberg, Waldemar Vollmer, Alistair B Russell, Jean-Pierre Simorre, Spencer Anthony-Cahill, Peter Brzovic, Beth Hayes, Seemay Chou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fd88b616c4ea743437b1ec2a1bdc0740
https://doi.org/10.7554/elife.79796.sa2
https://doi.org/10.7554/elife.79796.sa2
Autor:
Seemay Chou, Beth Hayes, Peter Brzovic, Spencer Anthony-Cahill, Jean-Pierre Simorre, Alistair B. Russell, Waldemar Vollmer, William Hatleberg, Lea M. Starita, Ziyi Zhao, Jacob Biboy, Chase Mateusiak, Samuel Thompson, Steven Massa, Rachel Kim, Hayden Saunders, Corey Henderson, Sebastian Flores, Anne L Sapiro, Atanas Radkov
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5d6c765e70ce06757a90569176e22dbd
https://doi.org/10.15252/rc.2022933120
https://doi.org/10.15252/rc.2022933120
Publikováno v:
Cellular microbiology. 17(1)
Shigella species are the aetiological agents of shigellosis, a severe diarrhoeal disease that is a significant cause of morbidity and mortality worldwide. Shigellosis causes massive colonic destruction, high fever and bloody diarrhoea. Shigella patho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1cc1bca6f8dc80d7e4ad255e620394eb
https://pubmed.ncbi.nlm.nih.gov/25355173
https://pubmed.ncbi.nlm.nih.gov/25355173
Autor:
Peter Brzovic, Ilme Schlichting, M.F. Dunn, Dimitri Niks, Lars Blumenstein, Thomas R. M. Barends, Patricia Casino, Huu Ngo, Peng Pan
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Biochemistry
instname
Biochemistry
12 pages, 4 tables, 3 schemes.-- PMID: 17559231 [PubMed].-- Printed version published Jul 3, 2007.
Substrate channeling in the tryptophan synthase bienzyme complex from Salmonella typhimurium is regulated by allosteric interactions triggered by
Substrate channeling in the tryptophan synthase bienzyme complex from Salmonella typhimurium is regulated by allosteric interactions triggered by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ad70c70b6f3389ddc5f3c1d3451311e
http://hdl.handle.net/10261/17417
http://hdl.handle.net/10261/17417
Publikováno v:
Scopus-Elsevier
Lysine 269 in Escherichia coli tryptophan indole-lyase (tryptophanase) has been changed to arginine by site-directed mutagenesis. The resultant K269R mutant enzyme exhibits kcat values about 10% those of the wild-type enzyme with S-(o-nitrophenyl)-L-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::961f2fd3fbff840d2a2c430244964e77
http://www.scopus.com/inward/record.url?eid=2-s2.0-0026044676&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0026044676&partnerID=MN8TOARS