PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33020580-4	2020	Combining structural analyses of cryo-electron microscopy data with molecular dynamic simulations, here we show that the cofactor NADH is a key player in the GDH regulation process.	NAD	130-134	glutamate dehydrogenase 1	Homo sapiens	158-161	
33020580-5	2020	Our structural analysis indicates that, binding to the regulatory sites in proximity of the antenna region, NADH acts as a positive allosteric modulator by enhancing both the affinity of the inhibitor GTP binding and inhibition of GDH catalytic activity.	NAD	108-112	glutamate dehydrogenase 1	Homo sapiens	231-234	
33020580-6	2020	We further show that the binding of GTP to the NADH-bound GDH activates a triangular allosteric network, interlinking the inhibitor with regulatory and catalytic sites.	NAD	47-51	glutamate dehydrogenase 1	Homo sapiens	58-61