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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:

Identification of a Potent Janus Kinase 3 Inhibitor with High Selectivity within the Janus Kinase Family
Gebhard Thoma, François Nuninger, Rocco Falchetto, et al.
Journal of Medicinal Chemistry (2010) Vol. 54, Iss. 1, pp. 284-288
Closed Access | Times Cited: 95

Showing 1-25 of 95 citing articles:

The role of JAK-STAT signaling pathway and its regulators in the fate of T helper cells
Farhad Seif, Majid Khoshmirsafa, Hossein Aazami, et al.
Cell Communication and Signaling (2017) Vol. 15, Iss. 1
Open Access | Times Cited: 686
Discovery and Development of Janus Kinase (JAK) Inhibitors for Inflammatory Diseases
James D. Clark, Mark E. Flanagan, Jean‐Baptiste Telliez
Journal of Medicinal Chemistry (2014) Vol. 57, Iss. 12, pp. 5023-5038
Closed Access | Times Cited: 535
The emerging safety profile of JAK inhibitors in rheumatic disease
Kevin Winthrop
Nature Reviews Rheumatology (2017) Vol. 13, Iss. 4, pp. 234-243
Closed Access | Times Cited: 520
Preclinical Characterization of GLPG0634, a Selective Inhibitor of JAK1, for the Treatment of Inflammatory Diseases
Luc Van Rompaey, René Galien, Ellen M. van der Aar, et al.
The Journal of Immunology (2013) Vol. 191, Iss. 7, pp. 3568-3577
Closed Access | Times Cited: 204
A Comprehensive Overview of Globally Approved JAK Inhibitors
Ahmed M. Shawky, Faisal A. Almalki, Ashraf N. Abdalla, et al.
Pharmaceutics (2022) Vol. 14, Iss. 5, pp. 1001-1001
Open Access | Times Cited: 198
Jak1 Has a Dominant Role over Jak3 in Signal Transduction through γc-Containing Cytokine Receptors
Claude Haan, Catherine Rolvering, Friedrich Raulf, et al.
Chemistry & Biology (2011) Vol. 18, Iss. 3, pp. 314-323
Open Access | Times Cited: 194
Lead identification of novel and selective TYK2 inhibitors
Jun Liang, Vickie Tsui, Anne van Abbema, et al.
European Journal of Medicinal Chemistry (2013) Vol. 67, pp. 175-187
Closed Access | Times Cited: 113
Selective JAK3 Inhibitors with a Covalent Reversible Binding Mode Targeting a New Induced Fit Binding Pocket
Michael Förster, A. Chaikuad, Silke M. Bauer, et al.
Cell chemical biology (2016) Vol. 23, Iss. 11, pp. 1335-1340
Open Access | Times Cited: 113
Development of Selective Covalent Janus Kinase 3 Inhibitors
Li Tan, Koshi Akahane, Randall McNally, et al.
Journal of Medicinal Chemistry (2015) Vol. 58, Iss. 16, pp. 6589-6606
Open Access | Times Cited: 103
Molecular docking study of sea urchin (Arbacia lixula) peptides as multi-target inhibitor for non-small cell lung cancer (NSCLC) associated proteins
Muhammad Hermawan Widyananda, Setyaki Kevin Pratama, Rizky Senna Samoedra, et al.
Journal of Pharmacy & Pharmacognosy Research (2021) Vol. 9, Iss. 4, pp. 484-496
Open Access | Times Cited: 67
Real-world efficacy and safety of tofacitinib treatment in Asian patients with ulcerative colitis
Kentaro Kojima, Kenji Watanabe, Mikio Kawai, et al.
World Journal of Gastroenterology (2024) Vol. 30, Iss. 13, pp. 1871-1886
Open Access | Times Cited: 10
JAK Kinases in Health and Disease: An Update
Arian Laurence, Marko Pesu, Olli Silvennoinen, et al.
The Open Rheumatology Journal (2012) Vol. 6, Iss. 1, pp. 232-244
Open Access | Times Cited: 92
Lead Optimization of a 4-Aminopyridine Benzamide Scaffold To Identify Potent, Selective, and Orally Bioavailable TYK2 Inhibitors
Jun Liang, Anne van Abbema, Mercedesz Balázs, et al.
Journal of Medicinal Chemistry (2013) Vol. 56, Iss. 11, pp. 4521-4536
Closed Access | Times Cited: 88
Mutations in RIPK4 Cause the Autosomal-Recessive Form of Popliteal Pterygium Syndrome
Ersan Kalay, Orhan Sezgın, Vasant Chellappa, et al.
The American Journal of Human Genetics (2011) Vol. 90, Iss. 1, pp. 76-85
Open Access | Times Cited: 88
Discovery of VX-509 (Decernotinib): A Potent and Selective Janus Kinase 3 Inhibitor for the Treatment of Autoimmune Diseases
Luc J. Farmer, Mark W. Ledeboer, Thomas Hoock, et al.
Journal of Medicinal Chemistry (2015) Vol. 58, Iss. 18, pp. 7195-7216
Closed Access | Times Cited: 81
Advances in the Discovery of Selective JAK Inhibitors
Christel Menet, Luc Van Rompaey, Raphaël Geney
Progress in medicinal chemistry (2013), pp. 153-223
Closed Access | Times Cited: 74
Identification of Cyanamide-Based Janus Kinase 3 (JAK3) Covalent Inhibitors
Agustin Casimiro‐Garcia, John I. Trujillo, F.F. Vajdos, et al.
Journal of Medicinal Chemistry (2018) Vol. 61, Iss. 23, pp. 10665-10699
Closed Access | Times Cited: 64
Insight into Janus kinases specificity: From molecular architecture to cancer therapeutics
Tian‐Hua Wei, Meng‐Yi Lu, Sihui Yao, et al.
MedComm – Oncology (2024) Vol. 3, Iss. 1
Open Access | Times Cited: 7
3-Amido Pyrrolopyrazine JAK Kinase Inhibitors: Development of a JAK3 vs JAK1 Selective Inhibitor and Evaluation in Cellular and in Vivo Models
Michael Soth, Johannes C. Hermann, Calvin Yee, et al.
Journal of Medicinal Chemistry (2012) Vol. 56, Iss. 1, pp. 345-356
Closed Access | Times Cited: 65
Kinase inhibitors in the treatment of immune-mediated disease
Apostolos Kontzias, Arian Laurence, Massimo Gadina, et al.
F1000 Medicine Reports (2012) Vol. 4
Open Access | Times Cited: 58
ATP-Mediated Kinome Selectivity: The Missing Link in Understanding the Contribution of Individual JAK Kinase Isoforms to Cellular Signaling
Atli Thorarensen, Mary Ellen Banker, Andrew Fensome, et al.
ACS Chemical Biology (2014) Vol. 9, Iss. 7, pp. 1552-1558
Closed Access | Times Cited: 56
Selective inhibitors of the Janus kinase Jak3—Are they effective?
Gebhard Thoma, Peter Drückes, Hans‐Günter Zerwes
Bioorganic & Medicinal Chemistry Letters (2014) Vol. 24, Iss. 19, pp. 4617-4621
Closed Access | Times Cited: 53
Development, Optimization, and Structure–Activity Relationships of Covalent-Reversible JAK3 Inhibitors Based on a Tricyclic Imidazo[5,4-d]pyrrolo[2,3-b]pyridine Scaffold
Michael Förster, A. Chaikuad, Teodor Dimitrov, et al.
Journal of Medicinal Chemistry (2018) Vol. 61, Iss. 12, pp. 5350-5366
Closed Access | Times Cited: 53
Identification of broad anti-coronavirus chemical agents for repurposing against SARS-CoV-2 and variants of concern
Luca Murer, Romain Volle, Vardan Andriasyan, et al.
Current Research in Virological Science (2022) Vol. 3, pp. 100019-100019
Open Access | Times Cited: 26
Discovery and Optimization of C-2 Methyl Imidazopyrrolopyridines as Potent and Orally Bioavailable JAK1 Inhibitors with Selectivity over JAK2
Mark Zak, Rohan Mendonca, Mercedesz Balázs, et al.
Journal of Medicinal Chemistry (2012) Vol. 55, Iss. 13, pp. 6176-6193
Closed Access | Times Cited: 55
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