OpenAlex Citation Counts

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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:

Recent advances in the development of covalent inhibitors
Hyunsoo Kim, Yoon Soo Hwang, Mingi Kim, et al.
RSC Medicinal Chemistry (2021) Vol. 12, Iss. 7, pp. 1037-1045
Open Access | Times Cited: 64

Showing 26-50 of 64 citing articles:

DNA encoded peptide library for SARS-CoV-2 3CL protease covalent inhibitor discovery and profiling
Yuyu Xing, Huiya Zhang, Yanhui Wang, et al.
RSC Chemical Biology (2024) Vol. 5, Iss. 7, pp. 691-702
Open Access | Times Cited: 2

Inhibitors of the Structural and Nonstructural Proteins of Alphaviruses
Damilohun Samuel Metibemu, Olawale Samuel Adeyinka, John Adeolu Falode, et al.
ACS Infectious Diseases (2024) Vol. 10, Iss. 8, pp. 2507-2524
Closed Access | Times Cited: 2

Systematic Targeting of Protein Complexes with Molecular COUPLrs
Diane Yang, Stefan Harry, Harrison B. Chong, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access | Times Cited: 2

Advancements, challenges, and future frontiers in covalent inhibitors and covalent drugs: A review
Muhammad Salman Hameed, Hongxuan Cao, Li Guo, et al.
European Journal of Medicinal Chemistry Reports (2024), pp. 100217-100217
Open Access | Times Cited: 2

Pan-Transcriptional Enhanced Associated Domain Palmitoylation Pocket Covalent Inhibitor
J S Kim, Hadong Kim, Jongwan Kim, et al.
Journal of Medicinal Chemistry (2024) Vol. 67, Iss. 21, pp. 18957-18968
Closed Access | Times Cited: 2

Species-specific lipophilicities of fluorinated diketones in complex equilibria systems and their potential as multifaceted reversible covalent warheads
Ishay Columbus, Lee Ghindes‐Azaria, Ido M. Herzog, et al.
Communications Chemistry (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 5

Strategies in the Design and Development of Non-Nucleoside Reverse Transcriptase Inhibitors (NNRTIs)
Murugesan Vanangamudi, Palaniappan Senthilkumar, M. K. Kathiravan, et al.
Viruses (2023) Vol. 15, Iss. 10, pp. 1992-1992
Open Access | Times Cited: 5

Two-Step Covalent Docking with Attracting Cavities
Mathilde Goullieux, Vincent Zoete, Ute F. Röhrig
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 24, pp. 7847-7859
Open Access | Times Cited: 5

Research progress of anticancer drugs targeting CDK12
Zhijia Yan, Yongli Du, Haibin Zhang, et al.
RSC Medicinal Chemistry (2023) Vol. 14, Iss. 9, pp. 1629-1644
Open Access | Times Cited: 4

Nitrogen Heterocycle Synthesis through Hydride Abstraction of Acyclic Carbamates and Related Species: Scope, Mechanism, Stereoselectivity, and Product Conformation Studies
Jenna L. Miller, Krishnan Damodaran, Paul E. Floreancig
Chemistry - A European Journal (2023) Vol. 29, Iss. 71
Closed Access | Times Cited: 4

Targeting PfCLK3 with Covalent Inhibitors: A Novel Strategy for Malaria Treatment
Andrew G. Jamieson, Skye Brettell, Omar Jahna, et al.
(2024)
Open Access | Times Cited: 1

Slow-Binding and Covalent HDAC Inhibition: A New Paradigm?
Yasir S. Raouf, Carlos Moreno–Yruela
JACS Au (2024) Vol. 4, Iss. 11, pp. 4148-4161
Open Access | Times Cited: 1

Exploring the landscape of post-translational modification in drug discovery
Yuhao Cao, Tianyi Yu, Zhiguang Zhu, et al.
Pharmacology & Therapeutics (2024) Vol. 265, pp. 108749-108749
Closed Access | Times Cited: 1

Innovative design and potential applications of covalent strategy in drug discovery
Tianxi Tang, Jiaxiang Luo, Dan Zhang, et al.
European Journal of Medicinal Chemistry (2024) Vol. 284, pp. 117202-117202
Closed Access | Times Cited: 1

Targeted anticancer pre-vinylsulfone covalent inhibitors of carbonic anhydrase IX
Aivaras Vaškevičius, Denis Baronas, Jānis Leitāns, et al.
eLife (2024) Vol. 13
Open Access | Times Cited: 1

Extended Applications of Small-Molecule Covalent Inhibitors toward Novel Therapeutic Targets
Jesang Lee, Seung Bum Park
Pharmaceuticals (2022) Vol. 15, Iss. 12, pp. 1478-1478
Open Access | Times Cited: 6

Protein labeling and crosslinking by covalent aptamers
Mary Cacace, Yaniv Tivon, Alexander Deiters
Methods in enzymology on CD-ROM/Methods in enzymology (2022), pp. 413-428
Open Access | Times Cited: 6

Disintegrate (DIN) Theory Enabling Precision Engineering of Proteins
Preeti Chauhan, V. Ragendu, Mohan Kumar, et al.
ACS Central Science (2023) Vol. 9, Iss. 2, pp. 137-150
Open Access | Times Cited: 2

A temperature-regulated bioorthogonal reaction to target lysine: Hemiacetal pharmacophore in genipin irreversibly binds with UCP2, inhibiting mitochondrial thermogenesis
Fukui Shen, Wen Yang, Kaixue Zhang, et al.
Chinese Chemical Letters (2023) Vol. 34, Iss. 10, pp. 108203-108203
Closed Access | Times Cited: 2

Targeted covalent inhibitors for novel therapeutics
Jingya Zhang, Wenshuo Gao, Yixia Wang, et al.
Future Medicinal Chemistry (2023) Vol. 15, Iss. 19, pp. 1739-1741
Closed Access | Times Cited: 2

Pinpointing Acidic Residues in Proteins
Weimin Xuan, Jun‐An Ma
ChemMedChem (2024) Vol. 19, Iss. 5
Closed Access

Covalent penicillin-protein conjugates elicit anti-drug antibodies that are clonally and functionally restricted
Lachlan P. Deimel, L. Moynié, Guoxuan Sun, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access

Targeting PfCLK3 with Covalent Inhibitors: A Novel Strategy for Malaria Treatment
Skye Brettell, Omar Janha, Abbey Begen, et al.
Journal of Medicinal Chemistry (2024) Vol. 67, Iss. 21, pp. 18895-18910
Open Access

Computational Insights into Acrylamide Fragment Inhibition of SARS-CoV-2 Main Protease
Ping Chen, Liyuan Wu, Bo Qin, et al.
Current Issues in Molecular Biology (2024) Vol. 46, Iss. 11, pp. 12847-12865
Open Access

Amino-Based Probe for Natural Products with Covalent Binding Ability to Lysine and Mechanism of Action of Medermycin
Jiaxu Shang, Shupeng Yin, Jingjing Shen, et al.
Organic Letters (2024)
Closed Access

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