Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Alison L. Costello"'
Autor:
Kevin S. Boland, Alison L. Costello, Stosh A. Kozimor, Sean D. Reilly, Iain May, Andrew J. Gaunt, David D. Schnaars, Steven D. Conradson
Publikováno v:
Dalton Trans.. 41:2003-2010
We report the interaction between B-type tri-lacunary heteropolyoxotungstate anions and actinyl(V) cations in aqueous solution, yielding a greater understanding of the stability of the OAnO1+ linear dioxo actinide moiety. Previously we reported that
Autor:
Todd M. Alam, Alison L. Costello
Publikováno v:
Chemistry and Physics of Lipids. 163:506-513
The effect of cholesterol (5–40 mol%) on the magnetic induced orientation of sphingomyelin/cholesterol multilamellar vesicles (MLVs) was examined using static solid state 31P NMR spectroscopy. The orientation was modeled assuming an ellipsoidal def
Autor:
Katherine M. Bender, Michael W. Crowder, Brian Bennett, Christine E. Hajdin, David L. Tierney, Alison L. Costello, Zhenxin Hu, Megan J. Hawk, Robert M. Breece
Publikováno v:
Journal of the American Chemical Society. 131:10753-10762
In an effort to probe the structure, mechanism, and biochemical properties of metallo-beta-lactamase Bla2 from Bacillus anthracis, the enzyme was overexpressed, purified, and characterized. Metal analyses demonstrated that recombinant Bla2 tightly bi
Autor:
Todd M. Alam, Alison L. Costello
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1778:97-104
The impact of low cholesterol concentrations on an egg sphingomyelin bilayer is investigated using 31P magic angle spinning (MAS) NMR spectroscopy. The magnitude of the isotropic 31P MAS NMR line width is used to monitor the main gel to liquid crysta
Autor:
Alejandro J. Vila, Alison L. Costello, Francisco J. Medrano Martín, Javier M. González, David L. Tierney
Publikováno v:
Journal of Molecular Biology. 373:1141-1156
Metallo-beta-lactamases (MbetaLs) are bacterial Zn(II)-dependent hydrolases that confer broad-spectrum resistance to beta-lactam antibiotics. These enzymes can be subdivided into three subclasses (B1, B2 and B3) that differ in their metal binding sit
Autor:
Matteo Dal Peraro, Alison L. Costello, Javier M. González, María-Natalia Lisa, Alejandro J. Vila, Adriana S. Limansky, Alejandro M. Viale, David L. Tierney, Brian Bennett, Jorgelina Morán-Barrio, Paolo Carloni
Publikováno v:
Journal of Biological Chemistry. 282:18286-18293
Metallo-beta-lactamases (MbetaLs) are zinc-dependent enzymes able to hydrolyze and inactivate most beta-lactam antibiotics. The large diversity of active site structures and metal content among MbetaLs from different sources has limited the design of
Autor:
John C. Gordon, Timothy J. Boyle, Sherrika D. Daniel-Taylor, Louis J. Tribby, Scott D. Bunge, Alison L. Costello, T. Mark McCleskey, Leigh Anna M. Ottley, Todd M. Alam
Publikováno v:
Inorganic Chemistry. 46:3705-3713
The synthesis and characterization of a series of neo-pentoxide (OCH2C(CH3)3 or ONep) derivatives of group 3 and the lanthanide (Ln) series' metals were undertaken via an amide/alcohol exchange route. Surprisingly, the products isolated and character
Publikováno v:
Biochemistry. 45:13650-13658
X-ray absorption spectroscopy was used to investigate the metal-binding sites of ImiS from Aeromonas veronii bv. sobria in catalytically active (1-Zn), product-inhibited (1-Zn plus imipenem), and inactive (2-Zn) forms. The first equivalent of zinc(II
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 11:351-358
Extended X-ray absorption fine structure studies of the metallo-beta-lactamase L1 from Stenotrophomonas maltophilia containing 1 and 2 equiv of Zn(II) and containing 2 equiv of Zn(II) plus hydrolyzed nitrocefin are presented. The data indicate that t
Autor:
Ke-Wu Yang, Gopal R. Periyannan, Brian Bennett, Michael W. Crowder, David L. Tierney, Alison L. Costello
Publikováno v:
Biochemistry. 45:1313-1320
In an effort to probe Co(II) binding to metallo-beta-lactamase CcrA, EPR, EXAFS, and (1)H NMR studies were conducted on CcrA containing 1 equiv (1-Co(II)-CcrA) and 2 equiv (Co(II)Co(II)-CcrA) of Co(II). The EPR spectra of 1-Co(II)-CcrA and Co(II)Co(I