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A Chemical Probe for Dark Kinase STK17B Derives Its Potency and High Selectivity through a Unique P-Loop Conformation.

Picado A, Chaikuad A, Wells CI, Shrestha S, Zuercher WJ, Pickett JE, Kwarcinski FE, Sinha P, de Silva CS, Zutshi R, Liu S, Kannan N, Knapp S, Drewry DH, Willson TM
J Med Chem 63 14626-14646 (2020)
Related entries: 3lm5, 6y6h, 6zjf, 7akg

Cited: 9 times
EuropePMC logo PMID: 33215924

Abstract

STK17B is a member of the death-associated protein kinase family and has been genetically linked to the development of diverse diseases. However, the role of STK17B in normal and disease pathology is poorly defined. Here, we present the discovery of thieno[3,2-d] pyrimidine

Articles - 6y6f mentioned but not cited (3)

  1. A Chemical Probe for Dark Kinase STK17B Derives Its Potency and High Selectivity through a Unique P-Loop Conformation. Picado A, Chaikuad A, Wells CI, Shrestha S, Zuercher WJ, Pickett JE, Kwarcinski FE, Sinha P, de Silva CS, Zutshi R, Liu S, Kannan N, Knapp S, Drewry DH, Willson TM. J Med Chem 63 14626-14646 (2020)
  2. Understanding the P-Loop Conformation in the Determination of Inhibitor Selectivity Toward the Hepatocellular Carcinoma-Associated Dark Kinase STK17B. Liu C, Li Z, Liu Z, Yang S, Wang Q, Chai Z. Front Mol Biosci 9 901603 (2022)
  3. Mechanistic Insights into the Mechanism of Inhibitor Selectivity toward the Dark Kinase STK17B against Its High Homology STK17A. Liu C, Zhang Y, Zhang Y, Liu Z, Mao F, Chai Z. Molecules 27 4655 (2022)


Articles citing this publication (6)

  1. AD Informer Set: Chemical tools to facilitate Alzheimer's disease drug discovery. Potjewyd FM, Annor-Gyamfi JK, Aubé J, Chu S, Conlon IL, Frankowski KJ, Guduru SKR, Hardy BP, Hopkins MD, Kinoshita C, Kireev DB, Mason ER, Moerk CT, Nwogbo F, Pearce KH, Richardson TI, Rogers DA, Soni DM, Stashko M, Wang X, Wells C, Willson TM, Frye SV, Young JE, Axtman AD. Alzheimers Dement (N Y) 8 e12246 (2022)
  2. Discovery of potent Plasmodium falciparum protein kinase 6 (PfPK6) inhibitors with a type II inhibitor pharmacophore. Ong HW, Truong A, Kwarcinski F, de Silva C, Avalani K, Havener TM, Chirgwin M, Galal KA, Willis C, Krämer A, Liu S, Knapp S, Derbyshire ER, Zutshi R, Drewry DH. Eur J Med Chem 249 115043 (2023)
  3. How many kinases are druggable? A review of our current understanding. Anderson B, Rosston P, Ong HW, Hossain MA, Davis-Gilbert ZW, Drewry DH. Biochem J 480 1331-1363 (2023)
  4. New Compounds with Bioisosteric Replacement of Classic Choline Kinase Inhibitors Show Potent Antiplasmodial Activity. Aguilar-Troyano FJ, Torretta A, Rubbini G, Fasiolo A, Luque-Navarro PM, Carrasco-Jimenez MP, Pérez-Moreno G, Bosch-Navarrete C, González-Pacanowska D, Parisini E, Lopez-Cara LC. Pharmaceutics 13 1842 (2021)
  5. Developing a Kinase Chemogenomic Set: Facilitating Investigation into Kinase Biology by Linking Phenotypes to Targets. Wells CI, Drewry DH. Methods Mol Biol 2706 11-24 (2023)
  6. PoSSuM v.3: A Major Expansion of the PoSSuM Database for Finding Similar Binding Sites of Proteins. Tsuchiya Y, Yonezawa T, Yamamori Y, Inoura H, Osawa M, Ikeda K, Tomii K. J Chem Inf Model 63 7578-7587 (2023)


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