OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!
If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.
Requested Article:
Two β-Lactamase Variants with Reduced Clavulanic Acid Inhibition Display Different Millisecond Dynamics
Wouter Elings, Aleksandra Chikunova, Danny B. van Zanten, et al.
Antimicrobial Agents and Chemotherapy (2021) Vol. 65, Iss. 8
Open Access | Times Cited: 7
Wouter Elings, Aleksandra Chikunova, Danny B. van Zanten, et al.
Antimicrobial Agents and Chemotherapy (2021) Vol. 65, Iss. 8
Open Access | Times Cited: 7
Showing 7 citing articles:
Drug Discovery in the Field of β-Lactams: An Academic Perspective
Lian Jacobs, Patrick Consol, Yu Chen
Antibiotics (2024) Vol. 13, Iss. 1, pp. 59-59
Open Access | Times Cited: 10
Lian Jacobs, Patrick Consol, Yu Chen
Antibiotics (2024) Vol. 13, Iss. 1, pp. 59-59
Open Access | Times Cited: 10
Different Conformations Revealed by NMR Underlie Resistance to Ceftazidime/Avibactam and Susceptibility to Meropenem and Imipenem among D179Y Variants of KPC β-Lactamase
Magdalena A. Taracila, Christopher R. Bethel, Andrea M. Hujer, et al.
Antimicrobial Agents and Chemotherapy (2022) Vol. 66, Iss. 4
Open Access | Times Cited: 17
Magdalena A. Taracila, Christopher R. Bethel, Andrea M. Hujer, et al.
Antimicrobial Agents and Chemotherapy (2022) Vol. 66, Iss. 4
Open Access | Times Cited: 17
The roles of highly conserved, non‐catalytic residues in class A β‐lactamases
Aleksandra Chikunova, Marcellus Ubbink
Protein Science (2022) Vol. 31, Iss. 6
Open Access | Times Cited: 12
Aleksandra Chikunova, Marcellus Ubbink
Protein Science (2022) Vol. 31, Iss. 6
Open Access | Times Cited: 12
QM/MM Simulations Reveal the Determinants of Carbapenemase Activity in Class A β-Lactamases
Ewa I. Chudyk, Michael Beer, Michael A. L. Limb, et al.
ACS Infectious Diseases (2022) Vol. 8, Iss. 8, pp. 1521-1532
Open Access | Times Cited: 11
Ewa I. Chudyk, Michael Beer, Michael A. L. Limb, et al.
ACS Infectious Diseases (2022) Vol. 8, Iss. 8, pp. 1521-1532
Open Access | Times Cited: 11
Nordalbergin Synergizes with Novel β-Lactam Antibiotics against MRSA Infection
Haiting Wang, Sangyu Hu, Yuzhu Pei, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 14, pp. 7704-7704
Open Access | Times Cited: 1
Haiting Wang, Sangyu Hu, Yuzhu Pei, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 14, pp. 7704-7704
Open Access | Times Cited: 1
The G132S Mutation Enhances the Resistance of Mycobacterium tuberculosis β-Lactamase against Sulbactam
Ilona van Alen, Aleksandra Chikunova, Adil A. Safeer, et al.
Biochemistry (2021) Vol. 60, Iss. 28, pp. 2236-2245
Open Access | Times Cited: 13
Ilona van Alen, Aleksandra Chikunova, Adil A. Safeer, et al.
Biochemistry (2021) Vol. 60, Iss. 28, pp. 2236-2245
Open Access | Times Cited: 13
Mycobacterium tuberculosis β-lactamase variant reduces sensitivity to ampicillin/avibactam in a zebrafish-Mycobacterium marinum model of tuberculosis
Ilona van Alen, Mayra A. Aguirre García, Janneke J. Maaskant, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 2
Ilona van Alen, Mayra A. Aguirre García, Janneke J. Maaskant, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 2
