PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	tumor protein p53	Homo sapiens	58-61	
32353067-6	2020	We find that not only the epitope residues (F19, W23 and L26), but also the hydrocarbon linker of the stapled p53 impart significant contributions.	Hydrocarbons	76-87	tumor protein p53	Homo sapiens	110-113	
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	tumor protein p53	Homo sapiens	28-31	
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	tumor protein p53	Homo sapiens	94-97	
24817343-3	2014	We also demonstrate a K24R mutation, necessary for cellular activity in hydrocarbon-stapled p53 peptides, is not required for analogous "double-click" peptides.	Hydrocarbons	72-83	tumor protein p53	Homo sapiens	92-95	
24418072-2	2014	In this study, the alpha-helical conformation and structural stability of single and double stapled all-hydrocarbon cross-linked p53 peptides when bound and unbound to MDM2 are investigated.	Hydrocarbons	104-115	tumor protein p53	Homo sapiens	129-132