V. Stojanoski

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Structure of the catalytic domain of the colistin resistance enzyme MCR-1

B. Sankaran, B. Prasad, T. Palzkill, 2016, BMC Biology.

The Drug-Resistant Variant P167S Expands the Substrate Profile of CTX-M β-Lactamases for Oxyimino-Cephalosporin Antibiotics by Enlarging the Active Site upon Acylation.

B. Sankaran, B. Prasad, T. Palzkill, 2017, Biochemistry.

Mechanistic Basis of OXA-48-like β-Lactamases' Hydrolysis of Carbapenems.

B. Sankaran, B. Prasad, T. Palzkill, 2021, ACS infectious diseases.

Lawrence Berkeley National Laboratory Recent Work Title Structure of the catalytic domain of the colistin resistance enzyme MCR-1 Permalink

B. Sankaran, B. Prasad, T. Palzkill, 2016 .

A Triple Mutant in the (cid:2) -loop of TEM-1 (cid:3) -Lactamase Changes the Substrate Profile via a Large Conformational Change and an Altered General Base for Catalysis *

B. Sankaran, T. Palzkill, D. Chow, 2020 .

A Triple Mutant in the Ω -loop of TEM-1 β -lactamase Changes the Substrate Profile via a Large Conformational Change and an Altered General Base for Catalysis

B. Sankaran, T. Palzkill, D. Chow, 2015 .

Structural Basis for Different Substrate Profiles of Two Closely Related Class D β-Lactamases and Their Inhibition by Halogens.

B. Sankaran, B. Prasad, T. Palzkill, 2015, Biochemistry.

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.

P. Zwart, B. Sankaran, B. Prasad, 2016, Biochemistry.

A Triple Mutant in the Ω-loop of TEM-1 β-Lactamase Changes the Substrate Profile via a Large Conformational Change and an Altered General Base for Catalysis*

B. Sankaran, B. Prasad, T. Palzkill, 2015, The Journal of Biological Chemistry.

Synergistic effects of functionally distinct substitutions in β-lactamase variants shed light on the evolution of bacterial drug resistance

B. Sankaran, B. Prasad, T. Palzkill, 2018, The Journal of Biological Chemistry.