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Items: 1 to 20 of 97


Twelve positions in a β-lactamase that can expand its substrate spectrum with a single amino acid substitution.

Yi H, Cho KH, Cho YS, Kim K, Nierman WC, Kim HS.

PLoS One. 2012;7(5):e37585. doi: 10.1371/journal.pone.0037585.


Substrate spectrum extension of PenA in Burkholderia thailandensis with a single amino acid deletion, Glu168del.

Yi H, Kim K, Cho KH, Jung O, Kim HS.

Antimicrob Agents Chemother. 2012 Jul;56(7):4005-8. doi: 10.1128/AAC.00598-12.


Systematic mutagenesis of the active site omega loop of TEM-1 beta-lactamase.

Petrosino JF, Palzkill T.

J Bacteriol. 1996 Apr;178(7):1821-8.


A novel ceftazidime-hydrolysing extended-spectrum beta-lactamase, CTX-M-54, with a single amino acid substitution at position 167 in the omega loop.

Bae IK, Lee BH, Hwang HY, Jeong SH, Hong SG, Chang CL, Kwak HS, Kim HJ, Youn H.

J Antimicrob Chemother. 2006 Aug;58(2):315-9.


Exploring the role of the Ω-loop in the evolution of ceftazidime resistance in the PenA β-lactamase from Burkholderia multivorans, an important Cystic Fibrosis pathogen.

Papp-Wallace KM, Becka SA, Taracila MA, Zeiser ET, Gatta JA, LiPuma JJ, Bonomo RA.

Antimicrob Agents Chemother. 2016 Nov 21. pii: AAC.01941-16. [Epub ahead of print]


Roles of amino acids 161 to 179 in the PSE-4 omega loop in substrate specificity and in resistance to ceftazidime.

Therrien C, Sanschagrin F, Palzkill T, Levesque RC.

Antimicrob Agents Chemother. 1998 Oct;42(10):2576-83.


Characterization of TEM-1 beta-lactamase mutants from positions 238 to 241 with increased catalytic efficiency for ceftazidime.

Venkatachalam KV, Huang W, LaRocco M, Palzkill T.

J Biol Chem. 1994 Sep 23;269(38):23444-50.


Amino acid sequence determinants of extended spectrum cephalosporin hydrolysis by the class C P99 beta-lactamase.

Zhang Z, Yu Y, Musser JM, Palzkill T.

J Biol Chem. 2001 Dec 7;276(49):46568-74.


Amino acid substitutions in a variant of IMP-1 metallo-beta-lactamase.

Iyobe S, Kusadokoro H, Ozaki J, Matsumura N, Minami S, Haruta S, Sawai T, O'Hara K.

Antimicrob Agents Chemother. 2000 Aug;44(8):2023-7.


SHV-type beta-lactamases.

Tzouvelekis LS, Bonomo RA.

Curr Pharm Des. 1999 Nov;5(11):847-64. Review.


Unexpected advanced generation cephalosporinase activity of the M69F variant of SHV beta-lactamase.

Helfand MS, Hujer AM, Sönnichsen FD, Bonomo RA.

J Biol Chem. 2002 Dec 6;277(49):47719-23.


Effects on substrate profile by mutational substitutions at positions 164 and 179 of the class A TEM(pUC19) beta-lactamase from Escherichia coli.

Vakulenko SB, Taibi-Tronche P, Tóth M, Massova I, Lerner SA, Mobashery S.

J Biol Chem. 1999 Aug 13;274(33):23052-60.


SHV-16, a beta-lactamase with a pentapeptide duplication in the omega loop.

Arpin C, Labia R, Andre C, Frigo C, El Harrif Z, Quentin C.

Antimicrob Agents Chemother. 2001 Sep;45(9):2480-5.


A secondary drug resistance mutation of TEM-1 beta-lactamase that suppresses misfolding and aggregation.

Sideraki V, Huang W, Palzkill T, Gilbert HF.

Proc Natl Acad Sci U S A. 2001 Jan 2;98(1):283-8.

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