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:

Cell‐Active, Reversible, and Irreversible Covalent Inhibitors That Selectively Target the Catalytic Lysine of BCR‐ABL Kinase
Peng Chen, Jie Sun, Chengjun Zhu, et al.
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 26
Closed Access | Times Cited: 47

Showing 1-25 of 47 citing articles:

Expanding Chemical Probe Space: Quality Criteria for Covalent and Degrader Probes
Ingo V. Hartung, Joachim Rudolph, Mary M. Mader, et al.
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 14, pp. 9297-9312
Open Access | Times Cited: 47

Emerging and Re-emerging Warheads for Targeted Covalent Inhibitors: An Update
Laura Hillebrand, Xiaojun Julia Liang, Ricardo Augusto Massarico Serafim, et al.
Journal of Medicinal Chemistry (2024) Vol. 67, Iss. 10, pp. 7668-7758
Closed Access | Times Cited: 37

Global Reactivity Profiling of the Catalytic Lysine in Human Kinome for Covalent Inhibitor Development
Guanghui Tang, Wei Wang, Chengjun Zhu, et al.
Angewandte Chemie International Edition (2024) Vol. 63, Iss. 12
Closed Access | Times Cited: 12

2-Ethynylbenzaldehyde-Based, Lysine-Targeting Irreversible Covalent Inhibitors for Protein Kinases and Nonkinases
Peng Chen, Guanghui Tang, Chengjun Zhu, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 7, pp. 3844-3849
Closed Access | Times Cited: 29

Small-molecule probes from bench to bedside: advancing molecular analysis of drug–target interactions toward precision medicine
Sijun Pan, Aixiang Ding, Yisi Li, et al.
Chemical Society Reviews (2023) Vol. 52, Iss. 16, pp. 5706-5743
Closed Access | Times Cited: 26

Development of covalent inhibitors: Principle, design, and application in cancer
Lang Zheng, Yang Li, Defa Wu, et al.
MedComm – Oncology (2023) Vol. 2, Iss. 4
Open Access | Times Cited: 20

Catalyst-free late-stage functionalization to assemble α-acyloxyenamide electrophiles for selectively profiling conserved lysine residues
Yuanyuan Zhao, Duan Kang, Youlong Fan, et al.
Communications Chemistry (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 8

Applications of covalent chemistry in targeted protein degradation
Dong Lu, Xin Yu, Hanfeng Lin, et al.
Chemical Society Reviews (2022) Vol. 51, Iss. 22, pp. 9243-9261
Open Access | Times Cited: 29

How many kinases are druggable? A review of our current understanding
Brian Anderson, Peter Rosston, Han Wee Ong, et al.
Biochemical Journal (2023) Vol. 480, Iss. 16, pp. 1331-1363
Open Access | Times Cited: 18

The expanding repertoire of covalent warheads for drug discovery
Namrashee V. Mehta, Mariam S. Degani
Drug Discovery Today (2023) Vol. 28, Iss. 12, pp. 103799-103799
Closed Access | Times Cited: 17

Technologies for Direct Detection of Covalent Protein–Drug Adducts
Elma Mons, Robbert Q. Kim, Monique P. C. Mulder
Pharmaceuticals (2023) Vol. 16, Iss. 4, pp. 547-547
Open Access | Times Cited: 14

Sulfur-fluoride exchange (SuFEx)-enabled lead discovery of AChE inhibitors by fragment linking strategies
Ziwen Zhang, Shilong Zhang, Chengyao Wu, et al.
European Journal of Medicinal Chemistry (2023) Vol. 257, pp. 115502-115502
Closed Access | Times Cited: 12

Small Molecule-Induced Post-Translational Acetylation of Catalytic Lysine of Kinases in Mammalian Cells
Guanghui Tang, Xuan Wang, Huisi Huang, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 34, pp. 23978-23988
Closed Access | Times Cited: 2

Bifunctional Lipid-Derived Affinity-Based Probes (AfBPs) for Analysis of Lipid–Protein Interactome
Jingyan Ge, Shubo Du, Shao Q. Yao
Accounts of Chemical Research (2022) Vol. 55, Iss. 24, pp. 3663-3674
Closed Access | Times Cited: 12

Chemoselective Reactions of Functionalized Sulfonyl Halides
Oleksandr S. Liashuk, Vladyslav A. Andriashvili, Andriy O. Tolmachev, et al.
The Chemical Record (2023) Vol. 24, Iss. 2
Open Access | Times Cited: 6

Cell-active, irreversible covalent inhibitors that selectively target the catalytic lysine of EGFR by using fluorosulfate-based SuFEx chemistry
Guanghui Tang, Wei Wang, Xuan Wang, et al.
European Journal of Medicinal Chemistry (2023) Vol. 259, pp. 115671-115671
Closed Access | Times Cited: 5

Kinase Inhibition via Small Molecule‐Induced Intramolecular Protein Cross‐Linking
Xuan Wang, Jie Sun, Huisi Huang, et al.
Angewandte Chemie (2024) Vol. 136, Iss. 28
Closed Access | Times Cited: 1

Aminomethyl Salicylaldehydes Lock onto a Surface Lysine by Forming an Extended Intramolecular Hydrogen Bond Network
Jacqueline Weaver, Gregory B. Craven, Linh Tram, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 35, pp. 24233-24237
Closed Access | Times Cited: 1

Chemoselective Reagents for the Traceless Bioreversible Modification of Native Proteins
Yana Petri, Forrest G. FitzGerald, Ronald T. Raines
Bioconjugate Chemistry (2024) Vol. 35, Iss. 9, pp. 1300-1308
Open Access | Times Cited: 1

A Tight Contact: The Expanding Application of Salicylaldehydes in Lysine‐Targeting Covalent Drugs
Mattia Mason, Laura Belvisi, Luca Pignataro, et al.
ChemBioChem (2023) Vol. 25, Iss. 7
Open Access | Times Cited: 4

RGD Cyclopeptide Equipped with a Lysine‐Engaging Salicylaldehyde Showing Enhanced Integrin Affinity and Cell Detachment Potency
Giovanni Sacco, Daniela Arosio, Mayra Paolillo, et al.
Chemistry - A European Journal (2023) Vol. 29, Iss. 19
Open Access | Times Cited: 3

Structural elements that enable specificity for mutant EGFR kinase domains with next-generation small-molecule inhibitors
Tahereh Damghani, Florian Wittlinger, Tyler S. Beyett, et al.
Methods in enzymology on CD-ROM/Methods in enzymology (2023), pp. 171-198
Open Access | Times Cited: 3

Multitarget inhibitors/probes that target LRRK2 and AURORA A kinases noncovalently and covalently
Wei Wang, Xuan Wang, Guanghui Tang, et al.
Chemical Communications (2023) Vol. 59, Iss. 72, pp. 10789-10792
Closed Access | Times Cited: 3

Targeted Reversible Covalent Modification of a Noncatalytic Lysine of the Krev Interaction Trapped 1 Protein Enables Site-Directed Screening for Protein–Protein Interaction Inhibitors
Karol R. Francisco, Jessica Bruystens, Carmine Varricchio, et al.
ACS Pharmacology & Translational Science (2023) Vol. 6, Iss. 11, pp. 1651-1658
Open Access | Times Cited: 3

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