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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.
Biochemistry. 2016 May 3;55(17):2479-90. doi: 10.1021/acs.biochem.6b00056. Epub 2016 Apr 22.
Biochemistry. 2016.
PMID: 27073009
Free PMC article.
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.
Stojanoski V, Chow DC, Hu L, Sankaran B, Gilbert HF, Prasad BV, Palzkill T.
Stojanoski V, et al.
J Biol Chem. 2015 Apr 17;290(16):10382-94. doi: 10.1074/jbc.M114.633438. Epub 2015 Feb 20.
J Biol Chem. 2015.
PMID: 25713062
Free PMC article.
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Structural Basis for Different Substrate Profiles of Two Closely Related Class D β-Lactamases and Their Inhibition by Halogens.
Stojanoski V, Chow DC, Fryszczyn B, Hu L, Nordmann P, Poirel L, Sankaran B, Prasad BV, Palzkill T.
Stojanoski V, et al.
Biochemistry. 2015 Jun 2;54(21):3370-80. doi: 10.1021/acs.biochem.5b00298. Epub 2015 May 14.
Biochemistry. 2015.
PMID: 25938261
Free PMC article.
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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.
Patel MP, Hu L, Stojanoski V, Sankaran B, Prasad BVV, Palzkill T.
Patel MP, et al. Among authors: stojanoski v.
Biochemistry. 2017 Jul 11;56(27):3443-3453. doi: 10.1021/acs.biochem.7b00176. Epub 2017 Jun 27.
Biochemistry. 2017.
PMID: 28613873
Free PMC article.
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Synergistic effects of functionally distinct substitutions in β-lactamase variants shed light on the evolution of bacterial drug resistance.
Patel MP, Hu L, Brown CA, Sun Z, Adamski CJ, Stojanoski V, Sankaran B, Prasad BVV, Palzkill T.
Patel MP, et al. Among authors: stojanoski v.
J Biol Chem. 2018 Nov 16;293(46):17971-17984. doi: 10.1074/jbc.RA118.003792. Epub 2018 Oct 1.
J Biol Chem. 2018.
PMID: 30275013
Free PMC article.
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Mechanistic Basis of OXA-48-like β-Lactamases' Hydrolysis of Carbapenems.
Stojanoski V, Hu L, Sankaran B, Wang F, Tao P, Prasad BVV, Palzkill T.
Stojanoski V, et al.
ACS Infect Dis. 2021 Feb 12;7(2):445-460. doi: 10.1021/acsinfecdis.0c00798. Epub 2021 Jan 25.
ACS Infect Dis. 2021.
PMID: 33492952
Free PMC article.
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Structure of the catalytic domain of the colistin resistance enzyme MCR-1.
Stojanoski V, Sankaran B, Prasad BV, Poirel L, Nordmann P, Palzkill T.
Stojanoski V, et al.
BMC Biol. 2016 Sep 21;14(1):81. doi: 10.1186/s12915-016-0303-0.
BMC Biol. 2016.
PMID: 27655155
Free PMC article.
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