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:

DrugMap: A quantitative pan-cancer analysis of cysteine ligandability
Mariko Takahashi, Harrison B. Chong, Siwen Zhang, et al.
Cell (2024) Vol. 187, Iss. 10, pp. 2536-2556.e30
Open Access | Times Cited: 20

Showing 20 citing articles:

Redox regulation: mechanisms, biology and therapeutic targets in diseases
Bowen Li, Hui Ming, Siyuan Qin, et al.
Signal Transduction and Targeted Therapy (2025) Vol. 10, Iss. 1
Open Access | Times Cited: 1

Functional implications of fumarate-induced cysteine succination
Iva Guberović, Christian Frezza
Trends in Biochemical Sciences (2024) Vol. 49, Iss. 9, pp. 775-790
Open Access | Times Cited: 7

Redirecting the pioneering function of FOXA1 with covalent small molecules
Sang Joon Won, Yuxiang Zhang, Christopher J. Reinhardt, et al.
Molecular Cell (2024)
Closed Access | Times Cited: 7

Covalent fragment-based drug discovery for target tractability
William J. McCarthy, Antonie J. van der Zouwen, Jacob T. Bush, et al.
Current Opinion in Structural Biology (2024) Vol. 86, pp. 102809-102809
Open Access | Times Cited: 5

Functionalizing tandem mass tags for streamlining click-based quantitative chemoproteomics
Nikolas R. Burton, Keriann M. Backus
Communications Chemistry (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 4

Targeted Covalent Modification Strategies for Drugging the Undruggable Targets
Tomonori Tamura, Masaharu Kawano, Itaru Hamachi
Chemical Reviews (2025)
Closed Access

Proteomic Ligandability Maps of Phosphorus(V) Stereoprobes Iden-tify Covalent TLCD1 Inhibitors
Hayden A. Sharma, Michael Bielecki, Meredith A. Holm, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access

Recent Advances in Mass Spectrometry-Based Bottom-Up Proteomics
Cameron S. Movassaghi, Jie Sun, Yuming Jiang, et al.
Analytical Chemistry (2025)
Closed Access

Sulfinyl Aziridines as Stereoselective Covalent Destabilizing Degraders of the Oncogenic Transcription Factor MYC
Hannah T. Rosen, Kelvin Li, Erin L. Li, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access

Opportunities to Modulate Tumor Ecosystem Toward Successful Glioblastoma Immunotherapy
Mariko Takahashi, Darina Mukhamejanova, Himani Jasewicz, et al.
Cancer Science (2025)
Open Access

Oxidation of retromer complex controls mitochondrial translation
Junbing Zhang, Md Yousuf Ali, Harrison B. Chong, et al.
Nature (2025)
Closed Access

Unraveling the nexus: Genomic instability and metabolism in cancer
Vaibhavi Gujar, Haojian Li, Tanya T. Paull, et al.
Cell Reports (2025) Vol. 44, Iss. 4, pp. 115540-115540
Open Access

Discovery of Thioether-Cyclized Macrocyclic Covalent Inhibitors by mRNA Display
Tong Lan, Cheng Peng, Xiyuan Yao, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 34, pp. 24053-24060
Closed Access | Times Cited: 3

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

Ligand discovery by activity-based protein profiling
Micah J. Niphakis, Benjamin F. Cravatt
Cell chemical biology (2024) Vol. 31, Iss. 9, pp. 1636-1651
Closed Access | Times Cited: 2

Cell cycle-dependent S-sulfenyl proteomics uncover a redox switch in p21-CDK feedback governing the proliferation-senescence decision
Julia Vorhauser, Theodoros I. Roumeliotis, Jacky K. Leung, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

CySP3-96 enables scalable, streamlined, and low-cost sample preparation for cysteine chemoproteomic applications
Flowreen Shikwana, Beeta S. Heydari, Samuel Ofori, et al.
Molecular & Cellular Proteomics (2024), pp. 100898-100898
Open Access | Times Cited: 1

Mapping cysteine ligandability
Sarah Crunkhorn
Nature Reviews Drug Discovery (2024) Vol. 23, Iss. 6, pp. 420-420
Closed Access

Chemical proteomic mapping of reversible small molecule binding sites in native systems
Jacob M. Wozniak, Weichao Li, Christopher G. Parker
Trends in Pharmacological Sciences (2024)
Closed Access

Page 1

Scroll to top