PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25115702-8	2014	Additionally, as seen in other stapled peptide structures, the hydrocarbon staple itself contributes to binding through favourable interactions with Mdm2.	Hydrocarbons	63-74	MDM2 proto-oncogene	Homo sapiens	149-153	
31226791-14	2019	Overall, macrocyclization by hydrocarbon stapling appears to overcome the destabilization of alpha-helicity by helix breaking residues and, in the specific case of d-Trp7-modification, a highly potent ATSP-7041 analog (Mdm2 Kd = 30 nM; cellular EC50 = 600 nM) was identified.	Hydrocarbons	29-40	MDM2 proto-oncogene	Homo sapiens	219-223	
31316744-1	2019	All-hydrocarbon, i, i+7 stapled peptide inhibitors of the p53-Mdm2 interaction have emerged as promising new leads for cancer therapy.	Hydrocarbons	4-15	MDM2 proto-oncogene	Homo sapiens	62-66	
26189498-4	2015	We then synthesized stapled p53 mimetic analogues using pure hydrocarbon linkers and demonstrated their abilities to block the p53-MDM2 interaction and selectively kill p53 wild-type colorectal carcinoma HCT-116 cells but not p53 null cells.	Hydrocarbons	61-72	MDM2 proto-oncogene	Homo sapiens	131-135	
21088491-1	2010	Atomistic simulations of a set of stapled peptides derived from the transactivation domain of p53 (designed by Verdine & colleagues, JACS 2007 129:2456) and complexed to MDM2 reveal that the good binders are uniquely characterized by higher helicity and by extensive interactions between the hydrocarbon staples and the MDM2 surface; in contrast the poor binders have reduced helicity and their staples are mostly solvent exposed.	Hydrocarbons	296-307	MDM2 proto-oncogene	Homo sapiens	174-178	
21088491-1	2010	Atomistic simulations of a set of stapled peptides derived from the transactivation domain of p53 (designed by Verdine & colleagues, JACS 2007 129:2456) and complexed to MDM2 reveal that the good binders are uniquely characterized by higher helicity and by extensive interactions between the hydrocarbon staples and the MDM2 surface; in contrast the poor binders have reduced helicity and their staples are mostly solvent exposed.	Hydrocarbons	296-307	MDM2 proto-oncogene	Homo sapiens	324-328