Systematic substitutions at BLIP position 50 result in changes in binding specificity for class A β-lactamases

Por Adamski, Carolyn J., Palzkill, Timothy
Publicado no BMC Biochem (2017)

Deep Sequencing of Random Mutant Libraries Reveals the Active Site of the Narrow Specificity CphA Metallo-β-Lactamase is Fragile to Mutations

Por Sun, Zhizeng, Mehta, Shrenik C., Adamski, Carolyn J., Gibbs, Richard A., Palzkill, Timothy
Publicado no Sci Rep (2016)

Role of β-lactamase residues in a common interface for binding the structurally unrelated inhibitory proteins BLIP and BLIP-II

Por Fryszczyn, Bartlomiej G, Adamski, Carolyn J, Brown, Nicholas G, Rice, Kacie, Huang, Wanzhi, Palzkill, Timothy
Publicado no Protein Sci (2014)

Removal of the Side Chain at the Active-Site Serine by a Glycine Substitution Increases the Stability of a Wide Range of Serine β-Lactamases by Relieving Steric Strain

Por Stojanoski, Vlatko, Adamski, Carolyn J., Hu, Liya, Mehta, Shrenik C., Sankaran, Banumathi, Zwart, Peter, Prasad, B.V. Venkataram, Palzkill, Timothy
Publicado no Biochemistry (2016)

Deep Sequencing of Systematic Combinatorial Libraries Reveals β-lactamase Sequence Constraints at High Resolution

Por Deng, Zhifeng, Huang, Wanzhi, Bakkalbasi, Erol, Brown, Nicholas G., Adamski, Carolyn J., Rice, Kacie, Muzny, Donna, Gibbs, Richard A., Palzkill, Timothy
Publicado em 2012

Molecular Basis for the Catalytic Specificity of the CTX-M Extended-Spectrum β-Lactamases

Por Adamski, Carolyn J., Cardenas, Ana Maria, Brown, Nicholas G., Horton, Lori B., Sankaran, Banumathi, Prasad, B. V. Venkataram, Gilbert, Hiram F., Palzkill, Timothy
Publicado no Biochemistry (2014)