Open Access Helper

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:

Showing 1-25 of 63 citing articles:

The Substitutions L50F, E166A, and L167F in SARS-CoV-2 3CLpro Are Selected by a Protease Inhibitor In Vitro and Confer Resistance To Nirmatrelvir
Dirk Jochmans, Liu C, Kim Donckers, et al.
mBio (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 127
Global prevalence of SARS-CoV-2 3CL protease mutations associated with nirmatrelvir or ensitrelvir resistance
Jonathan Daniel Ip, Allen Wing‐Ho Chu, Wan-Mui Chan, et al.
EBioMedicine (2023) Vol. 91, pp. 104559-104559
Open Access | Times Cited: 67
Therapeutics for COVID-19
Sima S. Toussi, Jennifer Hammond, Brian S. Gerstenberger, et al.
Nature Microbiology (2023) Vol. 8, Iss. 5, pp. 771-786
Open Access | Times Cited: 66
Structure and function of SARS-CoV and SARS-CoV-2 main proteases and their inhibition: A comprehensive review
Xin Li, Yongcheng Song
European Journal of Medicinal Chemistry (2023) Vol. 260, pp. 115772-115772
Open Access | Times Cited: 51
Alkyne Derivatives of SARS-CoV-2 Main Protease Inhibitors Including Nirmatrelvir Inhibit by Reacting Covalently with the Nucleophilic Cysteine
Lennart Brewitz, Leo Dumjahn, Yilin Zhao, et al.
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 4, pp. 2663-2680
Open Access | Times Cited: 46
In vitro and in vivo characterization of SARS-CoV-2 resistance to ensitrelvir
Maki Kiso, Seiya Yamayoshi, Shun Iida, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 39
Preclinical evaluation of the SARS-CoV-2 Mpro inhibitor RAY1216 shows improved pharmacokinetics compared with nirmatrelvir
Xiaoxin Chen, Xiaodong Huang, Qinhai Ma, et al.
Nature Microbiology (2024) Vol. 9, Iss. 4, pp. 1075-1088
Open Access | Times Cited: 26
The substitutions L50F, E166A and L167F in SARS-CoV-2 3CLpro are selected by a protease inhibitorin vitroand confer resistance to nirmatrelvir
Dirk Jochmans, Liu C, Kim Donckers, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 42
Ensitrelvir is effective against SARS-CoV-2 3CL protease mutants circulating globally
Sho Kawashima, Yuki Matsui, Takumi Adachi, et al.
Biochemical and Biophysical Research Communications (2023) Vol. 645, pp. 132-136
Open Access | Times Cited: 33
In vitro and in vivo characterization of SARS-CoV-2 strains resistant to nirmatrelvir
Maki Kiso, Yuri Furusawa, Ryuta Uraki, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 29
An orally bioavailable SARS-CoV-2 main protease inhibitor exhibits improved affinity and reduced sensitivity to mutations
Michael Westberg, Yichi Su, Xinzhi Zou, et al.
Science Translational Medicine (2024) Vol. 16, Iss. 738
Open Access | Times Cited: 12
In vitro selection and analysis of SARS-CoV-2 nirmatrelvir resistance mutations contributing to clinical virus resistance surveillance
Yuao Zhu, Irina Yurgelonis, Stephen Noell, et al.
Science Advances (2024) Vol. 10, Iss. 30
Open Access | Times Cited: 10
MD simulations indicate Omicron P132H of SARS-CoV-2 Mpro is a potential allosteric mutant involved in modulating the dynamics of catalytic site entry loop
Zahoor Ahmad Bhat, Mohd Muzammil Khan, Ayyub Rehman, et al.
International Journal of Biological Macromolecules (2024) Vol. 262, pp. 130077-130077
Closed Access | Times Cited: 7
Medicinal chemistry strategies towards the development of non-covalent SARS-CoV-2 Mpro inhibitors
Letian Song, Shenghua Gao, Bing Ye, et al.
Acta Pharmaceutica Sinica B (2023) Vol. 14, Iss. 1, pp. 87-109
Open Access | Times Cited: 19
Kinetic comparison of all eleven viral polyprotein cleavage site processing events by SARS-CoV-2 Main Protease using a linked protein FRET platform
Calem Kenward, M. Vuckovic, Mark Paetzel, et al.
Journal of Biological Chemistry (2024) Vol. 300, Iss. 6, pp. 107367-107367
Open Access | Times Cited: 6
Design, Synthesis, X-ray Crystallography, and Biological Activities of Covalent, Non-Peptidic Inhibitors of SARS-CoV-2 Main Protease
Md Ashraf-Uz-Zaman, Teck Khiang Chua, Xin Li, et al.
ACS Infectious Diseases (2024) Vol. 10, Iss. 2, pp. 715-731
Closed Access | Times Cited: 5
SARS-CoV-2 Mpro oligomerization as a potential target for therapy
Kinga Lis, Jacek Plewka, Filipe Menezes, et al.
International Journal of Biological Macromolecules (2024) Vol. 267, pp. 131392-131392
Open Access | Times Cited: 5
Non-peptidic inhibitors targeting SARS-CoV-2 main protease: A review
Ya-Qi Xiao, Jiao Long, Shuang‐Shuang Zhang, et al.
Bioorganic Chemistry (2024) Vol. 147, pp. 107380-107380
Closed Access | Times Cited: 5
Broad-spectrum coronavirus 3C-like protease peptidomimetic inhibitors effectively block SARS-CoV-2 replication in cells: Design, synthesis, biological evaluation, and X-ray structure determination
Irina Stefanelli, Angela Corona, Carmen Cerchia, et al.
European Journal of Medicinal Chemistry (2023) Vol. 253, pp. 115311-115311
Open Access | Times Cited: 14
Prevalence of Low-Frequency, Antiviral Resistance Variants in SARS-CoV-2 Isolates in Ontario, Canada, 2020-2023
Calvin Sjaarda, Lynette Lau, Jared T. Simpson, et al.
JAMA Network Open (2023) Vol. 6, Iss. 7, pp. e2324963-e2324963
Open Access | Times Cited: 12
Study of key residues in MERS-CoV and SARS-CoV-2 main proteases for resistance against clinically applied inhibitors nirmatrelvir and ensitrelvir
Laura Krismer, Helge Schöppe, Stefanie Rauch, et al.
npj Viruses (2024) Vol. 2, Iss. 1
Open Access | Times Cited: 4
A ricin-based peptide BRIP from Hordeum vulgare inhibits Mpro of SARS-CoV-2
Prakriti Kashyap, Vijay Kumar Bhardwaj, Mahima Chauhan, et al.
Scientific Reports (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 20
Detailed Insights into the Inhibitory Mechanism of New Ebselen Derivatives against Main Protease (Mpro) of Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2)
Pritiranjan Sahoo, Dipti Lenka, Monojit Batabyal, et al.
ACS Pharmacology & Translational Science (2022) Vol. 6, Iss. 1, pp. 171-180
Open Access | Times Cited: 20
Design, molecular docking and MD simulation of novel estradiol-pyrimidine analogues as potential inhibitors of Mpro and ACE2 for COVID-19
Darakhshan Parveen, Ruhi Ali, Mohammad Shaquiquzzaman, et al.
Chemical Physics Impact (2024) Vol. 8, pp. 100560-100560
Open Access | Times Cited: 3
High-Resolution Substrate Specificity Profiling of SARS-CoV-2 Mpro; Comparison to SARS-CoV Mpro
Rasha M. Yaghi, Collin L. Andrews, Dennis Wylie, et al.
ACS Chemical Biology (2024) Vol. 19, Iss. 7, pp. 1474-1483
Open Access | Times Cited: 3
Page 1 - Next Page

Scroll to top