PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
32897053-3	2020	Here, we utilize the highly specific recognition of ribose by ribose-binding protein (RBP) to develop a single-protein ribose sensor detectable via a sensitive NMR technique known as hyperpolarized 129Xe chemical exchange saturation transfer (hyper-CEST).	Ribose	52-58	retinol binding protein 4	Homo sapiens	62-84	
32897053-3	2020	Here, we utilize the highly specific recognition of ribose by ribose-binding protein (RBP) to develop a single-protein ribose sensor detectable via a sensitive NMR technique known as hyperpolarized 129Xe chemical exchange saturation transfer (hyper-CEST).	Ribose	52-58	retinol binding protein 4	Homo sapiens	86-89	
32897053-3	2020	Here, we utilize the highly specific recognition of ribose by ribose-binding protein (RBP) to develop a single-protein ribose sensor detectable via a sensitive NMR technique known as hyperpolarized 129Xe chemical exchange saturation transfer (hyper-CEST).	Ribose	62-68	retinol binding protein 4	Homo sapiens	86-89	
32897053-4	2020	We demonstrate that RBP, with a tunable ribose-binding site and further engineered to bind xenon, enables the quantitation of ribose over a wide concentration range (nM to mM).	Ribose	40-46	retinol binding protein 4	Homo sapiens	20-23	
32897053-4	2020	We demonstrate that RBP, with a tunable ribose-binding site and further engineered to bind xenon, enables the quantitation of ribose over a wide concentration range (nM to mM).	Ribose	126-132	retinol binding protein 4	Homo sapiens	20-23	
32897053-5	2020	Ribose binding induces the RBP "closed" conformation, which slows Xe exchange to a rate detectable by hyper-CEST.	Ribose	0-6	retinol binding protein 4	Homo sapiens	27-30	
16157349-1	2005	The ribose-binding protein (RBP) is a sugar-binding bacterial periplasmic protein whose function is associated with a large allosteric conformational change from an open to a closed conformation upon binding to ribose.	Ribose	4-10	retinol binding protein 4	Homo sapiens	28-31	
33728914-7	2021	The ribose is easily dissociated from the binding site of wild-type RBP and RBPG134R in the cMD simulations starting from the open and open-like forms.	Ribose	4-10	retinol binding protein 4	Homo sapiens	68-71