OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Dynamic Profiling of β-Coronavirus 3CL Mpro Protease Ligand-Binding Sites
Eunice Cho, Margarida Rosa, Ruhi Anjum, et al.
Journal of Chemical Information and Modeling (2021) Vol. 61, Iss. 6, pp. 3058-3073
Open Access | Times Cited: 48

Showing 26-50 of 48 citing articles:

Analyzing 3D structures of the SARS-CoV-2 main protease reveals structural features of ligand binding for COVID-19 drug discovery
Liang Xu, Ru Chen, Jie Liu, et al.
Drug Discovery Today (2023) Vol. 28, Iss. 10, pp. 103727-103727
Closed Access | Times Cited: 5

Identification of amentoflavone as a potent SARS-CoV-2 M pro inhibitor: a combination of computational studies and in vitro biological evaluation
Prabuddha Bhattacharya, Anirban Mandal
Journal of Biomolecular Structure and Dynamics (2024), pp. 1-19
Closed Access | Times Cited: 1

Repurposing the Open Global Health Library for the discovery of novel Mpro destabilizers with scope as broad-spectrum antivirals
Francisco Castillo, David Ramírez, María C. Ramos, et al.
Frontiers in Pharmacology (2024) Vol. 15
Open Access | Times Cited: 1

Thermodynamic and structural insights into the repurposing of drugs that bind to SARS-CoV-2 main protease
Shunzhou Wan, Agastya P. Bhati, Alexander D. Wade, et al.
Molecular Systems Design & Engineering (2021) Vol. 7, Iss. 2, pp. 123-131
Open Access | Times Cited: 12

The Functional Landscape of SARS-CoV-2 3CL Protease
Sho Iketani, Seo Jung Hong, Jenny Sheng, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 6

In silico evaluation of flavonoids as potential inhibitors of SARS-CoV-2 main nonstructural proteins (Nsps)—amentoflavone as a multitarget candidate
Andrés Portilla-Martínez, Miguel Ortíz-Flores, Isabel Carrillo‐Hidalgo, et al.
Journal of Molecular Modeling (2022) Vol. 28, Iss. 12
Open Access | Times Cited: 6

Gating interactions steer loop conformational changes in the active site of the L1 metallo-β-lactamase
Zhuoran Zhao, Xiayu Shen, Shuang Chen, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 3

The Role of Hydrophobic Nodes in the Dynamics of Class A β-Lactamases
Edgar Olehnovics, Junqi Yin, Adrià Pérez, et al.
Frontiers in Microbiology (2021) Vol. 12
Open Access | Times Cited: 8

How Distinct Structural Flexibility within SARS-CoV-2 Spike Protein Reveals Potential Therapeutic Targets
Serena H. Chen, M. Todd Young, John Gounley, et al.
2021 IEEE International Conference on Big Data (Big Data) (2021), pp. 4333-4341
Open Access | Times Cited: 8

Genetic surveillance of SARS-CoV-2 Mpro reveals high sequence and structural conservation prior to the introduction of protease inhibitor Paxlovid
Jonathan T. Lee, Qingyi Yang, Alexey V. Gribenko, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 5

Development of novel ligands against SARS‐CoV‐2 Mpro enzyme: an in silico and in vitro Study
Navid Kaboudi, Nadine Krüger, Maryam Hamzeh‐Mivehroud
Molecular Informatics (2023) Vol. 42, Iss. 11
Closed Access | Times Cited: 2

Discovery of SARS-CoV-2 MproPeptide Inhibitors from Modelling Substrate and Ligand Binding
H. T. Henry Chan, Marc A. Moesser, Rebecca K. Walters, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 5

SARS-CoV-2 3CLPro Dihedral Angles Reveal Allosteric Signaling
Daniel J. Evans, Samreen Sheraz, Albert Y. Lau
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Comprehensive fitness landscape of SARS-CoV-2 Mpro reveals insights into viral resistance mechanisms
Julia M. Flynn, Neha S. Samant, Gily Schneider-Nachum, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 3

Adaptive Language Model Training for Molecular Design
A.J. Blanchard, Debsindhu Bhowmik, John Gounley, et al.
(2022)
Open Access | Times Cited: 3

Substrate recognition and selectivity in SARS-CoV-2 main protease: Unveiling the role of subsite interactions through dynamical nonequilibrium molecular dynamics simulations
H. T. Henry Chan, A. Sofia F. Oliveira, Adrian J. Mulholland, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1

Developing evolution-resistant drugs for COVID-19
Daniel Weinreich
eLife (2022) Vol. 11
Open Access | Times Cited: 2

Dynamical nonequilibrium molecular dynamics simulations identify allosteric sites and positions associated with drug resistance in the SARS-CoV-2 main protease
H. T. Henry Chan, A. Sofia F. Oliveira, Christopher J. Schofield, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 1

Adaptive Language Model Training for Molecular Design
Andrew E. Blanchard, Debsindhu Bhowmik, Zachary Fox, et al.
(2023)
Open Access

Adaptive Language Model Training for Molecular Design
Andrew E. Blanchard, Debsindhu Bhowmik, Zachary Fox, et al.
(2023)
Open Access

Binding kinetics of ten small-molecule drug candidates on SARS-CoV-2 3CLpro revealed by biomolecular simulations
Yifei Zhou, Xubo Lin
Medicine in Novel Technology and Devices (2023) Vol. 20, pp. 100257-100257
Open Access

Previous Page - Page 2

Scroll to top