Search Results - "Chikunova, Aleksandra"

The roles of highly conserved, non‐catalytic residues in class A β‐lactamases by Chikunova, Aleksandra, Ubbink, Marcellus

“…Evolution minimizes the number of highly conserved amino acid residues in proteins to ensure evolutionary robustness and adaptability. The roles of all highly…”
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Bimodal substrate binding in the active site of the glycosidase B c X by Saberi, Mahin, Chikunova, Aleksandra, Ben Bdira, Fredj, Cramer‐Blok, Anneloes, Timmer, Monika, Voskamp, Patrick, Ubbink, Marcellus

“…Bacillus circulans xylanase (BcX) from the glycoside hydrolase family 11 degrades xylan through a retaining, double‐displacement mechanism. The enzyme is…”
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Corrigendum to “Enhanced activity against a third-generation cephalosporin by destabilization of the active site of a class A beta-lactamase” [Int. J. Biol. Macromol. 250 (2023) 126160] by Sun, Jing, Chikunova, Aleksandra, Boyle, Aimee L., Voskamp, Patrick, Timmer, Monika, Ubbink, Marcellus

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Enhanced activity against a third-generation cephalosporin by destabilization of the active site of a class A beta-lactamase by Sun, Jing, Chikunova, Aleksandra, Boyle, Aimee L., Voskamp, Patrick, Timmer, Monika, Ubbink, Marcellus

“…The β-lactamase BlaC conveys resistance to a broad spectrum of β-lactam antibiotics to its host Mycobacterium tuberculosis but poorly hydrolyzes…”
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The G132S Mutation Enhances the Resistance of Mycobacterium tuberculosis β‑Lactamase against Sulbactam by van Alen, Ilona, Chikunova, Aleksandra, Safeer, Adil A, Ahmad, Misbha Ud Din, Perrakis, Anastassis, Ubbink, Marcellus

“…The current rise of antibiotic resistant forms of Mycobacterium tuberculosis is a global health threat that calls for new antibiotics. The β-lactamase BlaC of…”
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Bimodal substrate binding in the active site of the glycosidase BcX by Saberi, Mahin, Chikunova, Aleksandra, Ben Bdira, Fredj, Cramer‐Blok, Anneloes, Timmer, Monika, Voskamp, Patrick, Ubbink, Marcellus

“…Bacillus circulans xylanase (BcX) from the glycoside hydrolase family 11 degrades xylan through a retaining, double‐displacement mechanism. The enzyme is…”
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Conserved residues Glu37 and Trp229 play an essential role in protein folding of β‐lactamase by Chikunova, Aleksandra, Manley, Max P., Ud Din Ahmad, Misbha, Bilman, Tuğçe, Perrakis, Anastassis, Ubbink, Marcellus

“…Evolutionary robustness requires that the number of highly conserved amino acid residues in proteins is minimized. In enzymes, such conservation is observed…”
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Asp179 in the class A β-lactamase from Mycobacterium tuberculosis is a conserved yet not essential residue due to epistasis by van Alen, Ilona, Chikunova, Aleksandra, van Zanten, Danny B, de Block, Amber A, Timmer, Monika, Brünle, Steffen, Ubbink, Marcellus

“…Conserved residues are often considered essential for function, and substitutions in such residues are expected to have a negative influence on the properties…”
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Corrigendum to "Enhanced activity against a third-generation cephalosporin by destabilization of the active site of a class A beta-lactamase" Int. J. Biol. Macromol. 250 (2023) 126160 by Sun, Jing, Chikunova, Aleksandra, Boyle, Aimee L, Voskamp, Patrick, Timmer, Monika, Ubbink, Marcellus

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Two β-Lactamase Variants with Reduced Clavulanic Acid Inhibition Display Different Millisecond Dynamics by Elings, Wouter, Chikunova, Aleksandra, van Zanten, Danny B, Drenth, Ralphe, Ahmad, Misbha Ud Din, Blok, Anneloes J, Timmer, Monika, Perrakis, Anastassis, Ubbink, Marcellus

“…The β-lactamase of Mycobacterium tuberculosis, BlaC, is susceptible to inhibition by clavulanic acid. The ability of this enzyme to escape inhibition through…”
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