Design of a Janus Kinase 3 (JAK3) Specific Inhibitor 1-((2 S,5 R)-5-((7 H-Pyrrolo[2,3-d]pyrimidin-4-yl)amino)-2-methylpiperidin-1-yl)prop-2-en-1-one (PF-06651600) Allowing for the Interrogation of JAK3 Signaling in Humans

[20] Processing of X-ray diffraction data collected in oscillation mode

Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475 · see citing works

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Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works

Refinement of Macromolecular Structures by the Maximum-Likelihood Method

Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,671 · see citing works

Overview of the <i>CCP</i> 4 suite and current developments

Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353 · see citing works

Recent advances in the cross-coupling reactions of organoboron derivatives with organic electrophiles, 1995–1998

Suzuki, A. (1999) · Journal of Organometallic Chemistry · doi:10.1016/s0022-328x(98)01055-9 · Cited by 2,927 · see citing works

Mutation of Jak3 in a Patient with SCID: Essential Role of Jak3 in Lymphoid Development

Russell, S. M., Tayebi, N., Nakajima, H., Riedy, M. C., Roberts, J. L., Aman, M. J., Migone, T., Noguchi, M., Markert, M. L., Buckley, R. H., et al. (1995) · Science · doi:10.1126/science.270.5237.797 · Cited by 801 · see citing works

Developing Irreversible Inhibitors of the Protein Kinase Cysteinome

Liu, Q., Sabnis, Y. A., Zhao, Z., Zhang, T., Buhrlage, S. J., Jones, L. H., & Gray, N. S. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.12.006 · Cited by 662 · see citing works

Discovery and Development of Janus Kinase (JAK) Inhibitors for Inflammatory Diseases

Clark, J. D., Flanagan, M. E., & Telliez, J. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401490p · Cited by 615 · see citing works

Global Kinetic Explorer: A new computer program for dynamic simulation and fitting of kinetic data

Johnson, K. A., Simpson, Z. B., & Blom, T. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2008.12.024 · Cited by 596 · see citing works

Transporter-Mediated Permeation of Drugs Across the Blood–Brain Barrier

Tamai, I., & Tsuji, A. (2000) · Journal of Pharmaceutical Sciences · doi:10.1002/1520-6017(200011)89:11 · Cited by 363 · see citing works

Chemical and Computational Methods for the Characterization of Covalent Reactive Groups for the Prospective Design of Irreversible Inhibitors

Flanagan, M. E., Abramite, J. A., Anderson, D. P., AULABAUGH, A. E., Dahal, U. P., Gilbert, A. M., Li, C., Montgomery, J. I., Oppenheimer, S. R., Ryder, T. F., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm501412a · Cited by 337 · see citing works

Covalent EGFR inhibitor analysis reveals importance of reversible interactions to potency and mechanisms of drug resistance

Schwartz, P. A., Kuzmic, P., Solowiej, J., Bergqvist, S., Bolanos, B., Almaden, C., Nagata, A., Ryan, K., Feng, J., Dalvie, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313733111 · Cited by 281 · see citing works

Tyrosine Kinase Inhibitors. 17. Irreversible Inhibitors of the Epidermal Growth Factor Receptor:  4-(Phenylamino)quinazoline- and 4-(Phenylamino)pyrido[3,2-<i>d</i>]pyrimidine-6-acrylamides Bearing Additional Solubilizing Functions

Smaill, J. B., Rewcastle, G. W., Loo, J. A., Greis, K. D., Chan, O. H., Reyner, E. L., Lipka, E., Showalter, H. D. H., Vincent, P. W., Elliott, W. L., et al. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm990482t · Cited by 269 · see citing works

Photochemical preparation of a pyridone containing tetracycle: A jak protein kinase inhibitor

Thompson, J. E., Cubbon, R. M., Cummings, R. T., Wicker, L. S., Frankshun, R. A., Cunningham, B. R., Cameron, P. M., Meinke, P. T., Liverton, N. J., Weng, Y., et al. (2002) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(02)00106-3 · Cited by 268 · see citing works

Chapter 23 Fitting Enzyme Kinetic Data with KinTek Global Kinetic Explorer

Johnson, K. A. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(09)67023-3 · Cited by 240 · see citing works

Structural and Thermodynamic Characterization of the TYK2 and JAK3 Kinase Domains in Complex with CP-690550 and CMP-6

Chrencik, J., Patny, A., Leung, I., Korniski, B., Emmons, T. L., Hall, T., Weinberg, R. A., Gormley, J. A., Williams, J. M., Day, J. E., et al. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.05.020 · Cited by 231 · see citing works

Discovery of a JAK3-Selective Inhibitor: Functional Differentiation of JAK3-Selective Inhibition over pan-JAK or JAK1-Selective Inhibition

Telliez, J.-B., Dowty, M. E., Wang, L., Jussif, J., Lin, T., Li, L., Moy, E., Balbo, P., Li, W., Zhao, Y., et al. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00677 · Cited by 204 · see citing works

Development of Selective Covalent Janus Kinase 3 Inhibitors

Tan, L., Akahane, K., McNally, R., Reyskens, K. M. S. E., Ficarro, S. B., Liu, S., Herter-Sprie, G. S., Koyama, S., Pattison, M. J., Labella, K., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00710 · Cited by 122 · see citing works

Different protein turnover of interleukin‐6‐type cytokine signalling components

Siewert, E., Müller‐Esterl, W., Starr, R., Heinrich, P. C., & Schaper, F. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00719.x · Cited by 121 · see citing works

The Role of Extrahepatic Metabolism in the Pharmacokinetics of the Targeted Covalent Inhibitors Afatinib, Ibrutinib, and Neratinib

Shibata, Y., & Chiba, M. (2014) · Drug Metabolism and Disposition · doi:10.1124/dmd.114.061424 · Cited by 112 · see citing works

Tricyclic Covalent Inhibitors Selectively Target Jak3 through an Active Site Thiol

Goedken, E. R., Argiriadi, M. A., Banach, D. L., Fiamengo, B. A., Foley, S. E., Frank, K. E., George, J. S., Harris, C. M., Hobson, A. D., Ihle, D. C., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.595181 · Cited by 101 · see citing works

JAK Kinases in Health and Disease: An Update

Laurence, A. D. J., Pesu, M., Silvennoinen, O., & O’Shea, J. J. (2012) · The Open Rheumatology Journal · doi:10.2174/1874312901206010232 · Cited by 96 · see citing works

Discovery of a Series of 2,5-Diaminopyrimidine Covalent Irreversible Inhibitors of Bruton’s Tyrosine Kinase with in Vivo Antitumor Activity

Li, X., Zuo, Y., Tang, G., Wang, Y., Zhou, Y., Wang, X., Guo, T., Xia, M., Ding, N., & Pan, Z. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm4017762 · Cited by 63 · see citing works

Imidazo[1,5-a]quinoxalines as irreversible BTK inhibitors for the treatment of rheumatoid arthritis

Kim, K., Maderna, A., Schnute, M. E., Hegen, M., Mohan, S., Miyashiro, J. S., Lin, L., Li, E., Keegan, S., Lussier, J., et al. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.09.008 · Cited by 63 · see citing works

ATP-Mediated Kinome Selectivity: The Missing Link in Understanding the Contribution of Individual JAK Kinase Isoforms to Cellular Signaling

Thorarensen, A., Banker, M. E., Fensome, A., Telliez, J., Juba, B. M., Vincent, F., Czerwiński, R., & Casimiro‐Garcia, A. (2014) · ACS Chemical Biology · doi:10.1021/cb5002125 · Cited by 62 · see citing works

Selective inhibitors of the Janus kinase Jak3—Are they effective?

Thoma, G., Drückes, P., & Zerwes, H. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.08.046 · Cited by 57 · see citing works

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L. Alicea-Velazquez, N., & J. Boggon, T. (2011) · Current Drug Targets · doi:10.2174/138945011794751528 · Cited by 53 · see citing works

Clearance Prediction of Targeted Covalent Inhibitors by In Vitro-In Vivo Extrapolation of Hepatic and Extrahepatic Clearance Mechanisms

Leung, L. Y., Yang, X., Strelevitz, T. J., Montgomery, J. I., Brown, M. F., Zientek, M. A., Banfield, C. R., Gilbert, A. M., Thorarensen, A., & Dowty, M. E. (2016) · Drug Metabolism and Disposition · doi:10.1124/dmd.116.072983 · Cited by 52 · see citing works

Selective JAK1 inhibitor and selective Tyk2 inhibitor patents

Norman, P. (2012) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2012.723693 · Cited by 37 · see citing works

Recent patents in the discovery of small molecule inhibitors of JAK3

Wilson, L. J. (2010) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543771003709767 · Cited by 35 · see citing works

Discovery of novel spirocyclic inhibitors of fatty acid amide hydrolase (FAAH). Part 2. Discovery of 7-azaspiro[3.5]nonane urea PF-04862853, an orally efficacious inhibitor of fatty acid amide hydrolase (FAAH) for pain

Meyers, M. J., Long, S. A., Pelc, M. J., Wang, J. L., Bowen, S. J., Schweitzer, B. A., Wilcox, M. V., McDonald, J. J., Smith, S. E., Foltin, S. K., et al. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.08.048 · Cited by 31 · see citing works

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Patil, Y. S., Bonde, N. L., Kekan, A. S., et al. (2014) · Organic Process Research & Development · doi:10.1021/op500274j · Cited by 25 · see citing works

Discovery of an Oral Potent Selective Inhibitor of Hematopoietic Prostaglandin D Synthase (HPGDS)

Carron, C. P., Trujillo, J. I., Olson, K. L., et al. (2010) · ACS Medicinal Chemistry Letters · doi:10.1021/ml900025z · Cited by 24 · see citing works

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Boike, L., Henning, N. J., & Nomura, D. K. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00542-z · Cited by 823 · see citing works

Biology and regulation of IL-2: from molecular mechanisms to human therapy

Spolski, R., Li, P., & Leonard, W. J. (2018) · Nature Reviews Immunology · doi:10.1038/s41577-018-0046-y · Cited by 637 · see citing works

Chemical Proteomics Identifies Druggable Vulnerabilities in a Genetically Defined Cancer

Bar-Peled, L., Kemper, E. K., Suciu, R. M., Vinogradova, E. V., Backus, K. M., Horning, B. D., Paul, T. A., Ichu, T.-A., Svensson, R. U., Olucha, J., et al. (2017) · Cell · doi:10.1016/j.cell.2017.08.051 · Cited by 262 · see citing works

Discovery of highly potent, selective, covalent inhibitors of JAK3

Kempson, J., Ovalle, D., Guo, J., Wrobleski, S. T., Lin, S., Spergel, S. H., Duan, J. J.-W., Jiang, B., Lu, Z., Das, J., et al. (2017) · Bioorganic &amp; Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.09.023 · Cited by 32 · see citing works

Structural Analysis of Janus Kinases.

Boggon, T. J., Li, Y., & Eck, M. J. (2004) · Blood · doi:10.1182/blood.v104.11.3863.3863

Janus kinase-3 (JAK3; JAK-3)

(2009) · Science-Business eXchange · doi:10.1038/scibx.2009.136

Selective inhibitors of the Janus kinase Jak3—Are they effective?

Thoma, G., Drückes, P., & Zerwes, H. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.08.046 · Cited by 57 · see citing works

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Wu, W. D., & Sun, X.-H. (2011) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmr105 · Cited by 24 · see citing works

JAK3 Specific Kinase Inhibitors: When Specificity Is Not Enough

Cox, L., & Cools, J. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.03.002 · Cited by 17 · see citing works