PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21186793-1 2011 Structure-based design was applied to the optimization of a series of 2-(quinazolin-2-yl)phenols to generate potent and selective ATP-competitive inhibitors of the DNA damage response signaling enzyme checkpoint kinase 2 (CHK2). Adenosine Triphosphate 130-133 checkpoint kinase 2 Homo sapiens 201-220 26437226-2 2015 Fragment elaboration by structure guided design was utilized to identify and develop a novel series of Chk1 inhibitors culminating in the identification of V158411, a potent ATP-competitive inhibitor of the Chk1 and Chk2 kinases. Adenosine Triphosphate 174-177 checkpoint kinase 2 Homo sapiens 216-220 23058106-1 2012 Two closely related binding modes have previously been proposed for the ATP-competitive benzimidazole class of checkpoint kinase 2 (CHK2) inhibitors; however, neither binding mode is entirely consistent with the reported SAR. Adenosine Triphosphate 72-75 checkpoint kinase 2 Homo sapiens 111-130 23058106-1 2012 Two closely related binding modes have previously been proposed for the ATP-competitive benzimidazole class of checkpoint kinase 2 (CHK2) inhibitors; however, neither binding mode is entirely consistent with the reported SAR. Adenosine Triphosphate 72-75 checkpoint kinase 2 Homo sapiens 132-136 23058106-2 2012 Unconstrained rigid docking of benzimidazole ligands into representative CHK2 protein crystal structures reveals an alternative binding mode involving a water-mediated interaction with the hinge region; docking which incorporates protein side chain flexibility for selected residues in the ATP binding site resulted in a refinement of the water-mediated hinge binding mode that is consistent with observed SAR. Adenosine Triphosphate 290-293 checkpoint kinase 2 Homo sapiens 73-77 21239475-4 2011 X-ray crystallography confirmed that CCT241533 bound to CHK2 in the ATP pocket. Adenosine Triphosphate 68-71 checkpoint kinase 2 Homo sapiens 56-60 23776527-0 2013 Fragment-based screening maps inhibitor interactions in the ATP-binding site of checkpoint kinase 2. Adenosine Triphosphate 60-63 checkpoint kinase 2 Homo sapiens 80-99 21186793-1 2011 Structure-based design was applied to the optimization of a series of 2-(quinazolin-2-yl)phenols to generate potent and selective ATP-competitive inhibitors of the DNA damage response signaling enzyme checkpoint kinase 2 (CHK2). Adenosine Triphosphate 130-133 checkpoint kinase 2 Homo sapiens 222-226 17616632-9 2007 NSC 109555 was shown to be a competitive inhibitor of Chk2 with respect to ATP, which was supported by docking of NSC 109555 into the ATP binding pocket of the Chk2 catalytic domain. Adenosine Triphosphate 134-137 checkpoint kinase 2 Homo sapiens 160-164 20022510-2 2010 Rapid exploration of the hits through straightforward chemistry established structure-activity relationships and a proposed ATP-competitive binding mode which was verified by X-ray crystallography of several analogues bound to CHK2. Adenosine Triphosphate 124-127 checkpoint kinase 2 Homo sapiens 227-231 19207465-1 2009 Isothiazole-carboxamidines are potent ATP competitive checkpoint kinases (Chk2) inhibitors. Adenosine Triphosphate 38-41 checkpoint kinase 2 Homo sapiens 74-78 20962588-7 2010 The ISA involves incubating the re-natured Rad53 protein with gamma 32P labeled ATP after electrophoresis and western blotting. Adenosine Triphosphate 80-83 checkpoint kinase 2 Homo sapiens 43-48 19741151-5 2009 The cocrystal structure of PV1019 bound in the ATP binding pocket of Chk2 confirmed enzymatic/biochemical observations that PV1019 acts as a competitive inhibitor of Chk2 with respect to ATP. Adenosine Triphosphate 47-50 checkpoint kinase 2 Homo sapiens 69-73 19741151-5 2009 The cocrystal structure of PV1019 bound in the ATP binding pocket of Chk2 confirmed enzymatic/biochemical observations that PV1019 acts as a competitive inhibitor of Chk2 with respect to ATP. Adenosine Triphosphate 47-50 checkpoint kinase 2 Homo sapiens 166-170 19741151-5 2009 The cocrystal structure of PV1019 bound in the ATP binding pocket of Chk2 confirmed enzymatic/biochemical observations that PV1019 acts as a competitive inhibitor of Chk2 with respect to ATP. Adenosine Triphosphate 187-190 checkpoint kinase 2 Homo sapiens 69-73 19741151-5 2009 The cocrystal structure of PV1019 bound in the ATP binding pocket of Chk2 confirmed enzymatic/biochemical observations that PV1019 acts as a competitive inhibitor of Chk2 with respect to ATP. Adenosine Triphosphate 187-190 checkpoint kinase 2 Homo sapiens 166-170 17616632-9 2007 NSC 109555 was shown to be a competitive inhibitor of Chk2 with respect to ATP, which was supported by docking of NSC 109555 into the ATP binding pocket of the Chk2 catalytic domain. Adenosine Triphosphate 75-78 checkpoint kinase 2 Homo sapiens 54-58 17616632-9 2007 NSC 109555 was shown to be a competitive inhibitor of Chk2 with respect to ATP, which was supported by docking of NSC 109555 into the ATP binding pocket of the Chk2 catalytic domain. Adenosine Triphosphate 75-78 checkpoint kinase 2 Homo sapiens 160-164 17616632-9 2007 NSC 109555 was shown to be a competitive inhibitor of Chk2 with respect to ATP, which was supported by docking of NSC 109555 into the ATP binding pocket of the Chk2 catalytic domain. Adenosine Triphosphate 134-137 checkpoint kinase 2 Homo sapiens 54-58 16150728-10 2005 When Chk2 is incubated with chromatin-enriched fractions in vitro in the presence of ATP, hyperphosphorylated forms of Chk2 bind more weakly to chromatin than hypophosphorylated forms. Adenosine Triphosphate 85-88 checkpoint kinase 2 Homo sapiens 5-9 16150728-10 2005 When Chk2 is incubated with chromatin-enriched fractions in vitro in the presence of ATP, hyperphosphorylated forms of Chk2 bind more weakly to chromatin than hypophosphorylated forms. Adenosine Triphosphate 85-88 checkpoint kinase 2 Homo sapiens 119-123 33762357-8 2021 Cells with DNA damage and elevated CHK2 relied significantly on glycolysis for ATP production due to dysfunctional mitochondria, which was abolished by CHK2 knockdown. Adenosine Triphosphate 79-82 checkpoint kinase 2 Homo sapiens 35-39 33762357-8 2021 Cells with DNA damage and elevated CHK2 relied significantly on glycolysis for ATP production due to dysfunctional mitochondria, which was abolished by CHK2 knockdown. Adenosine Triphosphate 79-82 checkpoint kinase 2 Homo sapiens 152-156 31343838-5 2019 Also, 3 p exhibited weak inhibition of the enzymatic activity of human topoisomerase I. Molecular docking studies indicated preferential binding of the compounds to the ATP-binding pocket of the human checkpoint 2 kinase (Chk2) catalytic domain, thus, identifying a novel diaryl 2-propenone chemotype for the development of potent inhibitors of Chk2. Adenosine Triphosphate 169-172 checkpoint kinase 2 Homo sapiens 201-220 31343838-5 2019 Also, 3 p exhibited weak inhibition of the enzymatic activity of human topoisomerase I. Molecular docking studies indicated preferential binding of the compounds to the ATP-binding pocket of the human checkpoint 2 kinase (Chk2) catalytic domain, thus, identifying a novel diaryl 2-propenone chemotype for the development of potent inhibitors of Chk2. Adenosine Triphosphate 169-172 checkpoint kinase 2 Homo sapiens 222-226 31343838-5 2019 Also, 3 p exhibited weak inhibition of the enzymatic activity of human topoisomerase I. Molecular docking studies indicated preferential binding of the compounds to the ATP-binding pocket of the human checkpoint 2 kinase (Chk2) catalytic domain, thus, identifying a novel diaryl 2-propenone chemotype for the development of potent inhibitors of Chk2. Adenosine Triphosphate 169-172 checkpoint kinase 2 Homo sapiens 345-349 17035018-3 2007 The structure-activity relationship studies were performed on the scaffold, and enzymatic kinetic analysis showed they are simple ATP competitive inhibitors with K(i) values as low as 11 nM for Chk2. Adenosine Triphosphate 130-133 checkpoint kinase 2 Homo sapiens 194-198 15771432-5 2005 Compound 2h is an ATP-competitive inhibitor of chk2 that dose dependently protects human CD4(+) and CD8(+) T-cells from apoptosis due to ionizing radiation. Adenosine Triphosphate 18-21 checkpoint kinase 2 Homo sapiens 47-51