Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Bradley J. Wallar"'
Autor:
Maria Luisa Introvigne, Trevor J. Beardsley, Micah C. Fernando, David A. Leonard, Bradley J. Wallar, Susan D. Rudin, Magdalena A. Taracila, Philip N. Rather, Jennifer M. Colquhoun, Shaina Song, Francesco Fini, Kristine M. Hujer, Andrea M. Hujer, Fabio Prati, Rachel A. Powers, Robert A. Bonomo, Emilia Caselli
Publikováno v:
Antibiotics, Vol 12, Iss 4, p 644 (2023)
Acinetobacter baumannii is a Gram-negative organism listed as an urgent threat pathogen by the World Health Organization (WHO). Carbapenem-resistant A. baumannii (CRAB), especially, present therapeutic challenges due to complex mechanisms of resistan
Externí odkaz:
https://doaj.org/article/0bf39937c44f473185677dc4d7075b7e
Autor:
Sara J. Barlow, Robert A. Bonomo, Rachel A. Powers, Fabio Prati, Kali A. Smolen, Magdalena A. Taracila, Bradley J. Wallar, Emilia Caselli, Brandy N. Curtis
Publikováno v:
Antimicrob Agents Chemother
Extended-spectrum class C β-lactamases have evolved to rapidly inactivate expanded-spectrum cephalosporins, a class of antibiotics designed to be resistant to hydrolysis by β-lactamase enzymes. To better understand the mechanism by which A cinetoba
Autor:
Emilia, Caselli, Francesco, Fini, Maria Luisa, Introvigne, Mattia, Stucchi, Magdalena A, Taracila, Erin R, Fish, Kali A, Smolen, Philip N, Rather, Rachel A, Powers, Bradley J, Wallar, Robert A, Bonomo, Fabio, Prati
Publikováno v:
ACS Infectious Diseases
Boronic acid transition state inhibitors (BATSIs) are known reversible covalent inhibitors of serine β-lactamases. The selectivity and high potency of specific BATSIs bearing an amide side chain mimicking the β-lactam’s amide side chain are an es
Autor:
Bradley J. Wallar, Rachel A. Powers, Francesco Fini, Philip N. Rather, Fabio Prati, Erin R. Fish, Maria Luisa Introvigne, Robert A. Bonomo, Mattia Stucchi, Kali A. Smolen, Magdalena A. Taracila, Emilia Caselli
Boronic acid transition state inhibitors (BATSIs) are known reversible covalent inhibitors of serine β-lactamases. The selectivity and high potency of specific BATSIs bearing an amide side chain mimicking the β-lactam's amide side chain are an esta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::216e83087d08f3162ebae8cbb64b0670
https://hdl.handle.net/11380/1208053
https://hdl.handle.net/11380/1208053
Autor:
Thomas H. Clarke, Derrick E. Fouts, Magdalena A. Taracila, Pratap Venepally, David A. Leonard, Bradley J. Wallar, Paul G. Higgins, Rachel A. Powers, Philip N. Rather, Lauren Brinkac, Robert A. Bonomo, Steven H. Marshall, Andrew R Mack, Kristine M. Hujer, Barry N. Kreiswirth, Fabio Prati, Christopher Greco, Emilia Caselli, Andrea M. Hujer
Publikováno v:
Diagnostic Microbiology and Infectious Disease
Successful treatment of Acinetobacter baumannii infections require early and appropriate antimicrobial therapy. One of the first steps in this process is understanding which β-lactamase (bla) alleles are present and in what combinations. Thus, we pe
Autor:
Rachel A. Powers, Kali A. Smolen, Fabio Prati, Alexandra A. Bouza, Magdalena A. Taracila, Emilia Caselli, Robert A. Bonomo, Francesco Fini, Hollister C. Swanson, Bradley J. Wallar, Chiara Romagnoli
Boronic acids are attracting a lot of attention as β-lactamase inhibitors, and in particular, compound S02030 (Ki = 44 nM) proved to be a good lead compound against ADC-7 (Acinetobacter-derived cephalosporinase), one of the most significant resistan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f75682e8ee3ed7686321fca1b7b6a5ad
https://europepmc.org/articles/PMC5987196/
https://europepmc.org/articles/PMC5987196/
Autor:
Rachel A. Powers, Chiara Romagnoli, Kali A. Smolen, Magdalena A. Taracila, Fabio Prati, Hollister C. Swanson, Emilia Caselli, Robert A. Bonomo, Alison L. VanDine, Alexandra A. Bouza, Bradley J. Wallar
Publikováno v:
ACS infectious diseases. 4(3)
Acinetobacter baumannii is a multidrug resistant pathogen that infects more than 12 000 patients each year in the US. Much of the resistance to β-lactam antibiotics in Acinetobacter spp. is mediated by class C β-lactamases known as Acinetobacter-de
Autor:
Nicholas W. Florek, Emilia Caselli, Hollister C. Swanson, Robert A. Bonomo, Bradley J. Wallar, Fabio Prati, Magdalena A. Taracila, Rachel A. Powers, Chiara Romagnoli
Publikováno v:
Biochemistry
β-Lactam resistance in Acinetobacter baumannii presents one of the greatest challenges to contemporary antimicrobial chemotherapy. Much of this resistance to cephalosporins derives from the expression of the class C β-lactamase enzymes, known as Ac
Autor:
Jessica A. Schoenherr, Susan M. Kitchen, Brittany N. Stropich, Holly A. Holman, Arthur S. Alberts, Bradley J. Wallar
Publikováno v:
Journal of Biological Chemistry. 281:4300-4307
Mammalian diaphanous-related (mDia) formins act as Rho GTPase effectors during cytoskeletal remodeling. Rho binding to mDia amino-terminal GTPase-binding domains (GBDs) causes the adjacent Dia-inhibitory domain (DID) to release the carboxyl-terminal
Autor:
Philippe Chavrier, Jun Peng, Florence Niedergang, Bradley J. Wallar, Emma Colucci-Guyon, Arthur S. Alberts
Publikováno v:
Current Biology. 15:2007-2012
SummaryMacrophages, dendritic cells, and neutrophils use phagocytosis to capture and clear off invading pathogens. The process is triggered by the interaction of ligands on the pathogens’ surface with specific phagocytic receptors, including immuno