PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11707461-11	2002	Of the three identified functionally important residues, the Ser-67 and Thr-128 Gbeta mutants significantly inhibited basal currents of a channel point mutant that displays Gbetagamma-mediated basal but not agonist-induced currents.	gbetagamma	173-183	succinate-CoA ligase GDP-forming subunit beta	Homo sapiens	80-85	
27108799-4	2016	The majority of these 13 mutations affect known Gbeta binding sites, which suggests that a likely disease mechanism is through the disruption of the protein interface required for Galpha-Gbetagamma interaction (resulting in a constitutively active Gbetagamma) or through the disruption of residues relevant for interaction between Gbetagamma and certain downstream effectors (resulting in reduced interaction with the effectors).	gbetagamma	187-197	succinate-CoA ligase GDP-forming subunit beta	Homo sapiens	48-53	
11560937-8	2001	Our data reveal that the degree of inhibition by a particular Gbeta subunit is strongly dependent on the specific calcium channel beta subunit, with N-type channels containing the beta(4) subunit being less susceptible to Gbetagamma-induced inhibition.	gbetagamma	222-232	succinate-CoA ligase GDP-forming subunit beta	Homo sapiens	62-67	
9065414-6	1997	To evaluate further the significance of the C-terminal region of Gbeta in the formation of a Gbetagamma complex and its signal transduction, we constructed several C-terminal mutants and expressed them in human embryonal kidney 293 cells.	gbetagamma	93-103	succinate-CoA ligase GDP-forming subunit beta	Homo sapiens	65-70	
20881007-9	2011	Mass spectrometry and site-directed mutagenesis indicate that SIGC(-cysteamine) specifically and efficiently leads to cysteamine (half-cystamine) modification of a single site on Gbeta, likely GbetaCys204, and inhibits Gbetagamma more than a hundred times more potently than cystamine.	gbetagamma	219-229	succinate-CoA ligase GDP-forming subunit beta	Homo sapiens	179-184