139. Siu T et al (2008) The design and synthesis of potent and cell-active allosteric dual Akt
1 and 2 inhibitors devoid of hERG activity. Bioorg Med Chem Lett 18(14):4191–4194
140. Bjune K et al (2018) MK-2206, an allosteric inhibitor of AKT, stimulates LDLR expression
and LDL uptake: a potential hypocholesterolemic agent. Atherosclerosis 276:28–38
141. Huang BX et al (2017) Identification of 4-phenylquinolin-2(1H)-one as a specific allosteric
inhibitor of Akt. Sci Rep 7(1):11673
142. Ahad AM et al (2011) Development of sulfonamide AKT PH domain inhibitors. Bioorg Med
Chem 19(6):2046–2054
143. Kim D et al (2010) A small molecule inhibits Akt through direct binding to Akt and preventing
Akt membrane translocation. J Biol Chem 285(11):8383–8394
144. Ranieri C et al (2018) In vitro efficacy of ARQ 092, an allosteric AKT inhibitor, on primary
fibroblast cells derived from patients with PIK3CA-related overgrowth spectrum (PROS).
Neurogenetics 19(2):77–91
145. Jeffrey PD et al (1995) Mechanism of CDK activation revealed by the structure of a
cyclinA-CDK2 complex. Nature 376(6538):313–320
146. Roskoski Jr R (2018) Cyclin-dependent protein serine/threonine kinase inhibitors as
anticancer drugs. Pharmacol Res 139:471–488
147. Thill M, Schmidt M (2018) Management of adverse events during cyclin-dependent
kinase 4/6 (CDK4/6) inhibitor-based treatment in breast cancer. Ther Adv Med Oncol
10:1758835918793326
148. Christodoulou MS et al (2017) Probing an allosteric pocket of CDK2 with small molecules.
ChemMedChem 12(1):33–41
149. Mariaule G, Belmont P (2014) Cyclin-dependent kinase inhibitors as marketed anticancer
drugs: where are we now? A short survey. Molecules 19(9):14366–14382
150. Betzi S et al (2011) Discovery of a potential allosteric ligand binding site in CDK2.
ACS Chem Biol 6(5):492–501
151. Zhao P et al (2018) Crystal structure of EGFR T790M/C797S/V948R in complex
with EAI045. Biochem Biophys Res Commun 502(3):332–337
152. Jia Y et al (2016) Overcoming EGFR(T790M) and EGFR(C797S) resistance with
mutant-selective allosteric inhibitors. Nature 534(7605):129–132
153. Caporuscio F et al (2018) Identification of small-molecule EGFR allosteric inhibitors
by high-throughput docking. Future Med Chem 10(13):1545–1553
154. Carlino L et al (2018) Structure-activity relationships of Hexahydrocyclopenta[c]quinoline
derivatives as allosteric inhibitors of CDK2 and EGFR. ChemMedChem 13(24):2627–2634
155. Liu H et al (2018) A novel allosteric inhibitor that prevents IKKbeta activation.
MedChemComm 9(2):239–243
24
S. Röhm et al.
1 and 2 inhibitors devoid of hERG activity. Bioorg Med Chem Lett 18(14):4191–4194
140. Bjune K et al (2018) MK-2206, an allosteric inhibitor of AKT, stimulates LDLR expression
and LDL uptake: a potential hypocholesterolemic agent. Atherosclerosis 276:28–38
141. Huang BX et al (2017) Identification of 4-phenylquinolin-2(1H)-one as a specific allosteric
inhibitor of Akt. Sci Rep 7(1):11673
142. Ahad AM et al (2011) Development of sulfonamide AKT PH domain inhibitors. Bioorg Med
Chem 19(6):2046–2054
143. Kim D et al (2010) A small molecule inhibits Akt through direct binding to Akt and preventing
Akt membrane translocation. J Biol Chem 285(11):8383–8394
144. Ranieri C et al (2018) In vitro efficacy of ARQ 092, an allosteric AKT inhibitor, on primary
fibroblast cells derived from patients with PIK3CA-related overgrowth spectrum (PROS).
Neurogenetics 19(2):77–91
145. Jeffrey PD et al (1995) Mechanism of CDK activation revealed by the structure of a
cyclinA-CDK2 complex. Nature 376(6538):313–320
146. Roskoski Jr R (2018) Cyclin-dependent protein serine/threonine kinase inhibitors as
anticancer drugs. Pharmacol Res 139:471–488
147. Thill M, Schmidt M (2018) Management of adverse events during cyclin-dependent
kinase 4/6 (CDK4/6) inhibitor-based treatment in breast cancer. Ther Adv Med Oncol
10:1758835918793326
148. Christodoulou MS et al (2017) Probing an allosteric pocket of CDK2 with small molecules.
ChemMedChem 12(1):33–41
149. Mariaule G, Belmont P (2014) Cyclin-dependent kinase inhibitors as marketed anticancer
drugs: where are we now? A short survey. Molecules 19(9):14366–14382
150. Betzi S et al (2011) Discovery of a potential allosteric ligand binding site in CDK2.
ACS Chem Biol 6(5):492–501
151. Zhao P et al (2018) Crystal structure of EGFR T790M/C797S/V948R in complex
with EAI045. Biochem Biophys Res Commun 502(3):332–337
152. Jia Y et al (2016) Overcoming EGFR(T790M) and EGFR(C797S) resistance with
mutant-selective allosteric inhibitors. Nature 534(7605):129–132
153. Caporuscio F et al (2018) Identification of small-molecule EGFR allosteric inhibitors
by high-throughput docking. Future Med Chem 10(13):1545–1553
154. Carlino L et al (2018) Structure-activity relationships of Hexahydrocyclopenta[c]quinoline
derivatives as allosteric inhibitors of CDK2 and EGFR. ChemMedChem 13(24):2627–2634
155. Liu H et al (2018) A novel allosteric inhibitor that prevents IKKbeta activation.
MedChemComm 9(2):239–243
24
S. Röhm et al.