PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17670971-3	2007	Here, we demonstrate that reducing agents as well as endogenous metal chelators sensitize C-type dorsal root ganglion nociceptors by chelating Zn2+ ions off specific extracellular histidine residues on Ca(v)3.2 T-channels, thus relieving tonic channel inhibition, enhancing Ca(v)3.2 currents, and lowering the threshold for nociceptor excitability in vitro and in vivo.	Zinc	143-147	immunoglobulin lambda variable 7-43	Homo sapiens	202-210	
22131323-3	2011	Divalent cations Zn(2+), Cu(2+) and Ni(2+) inhibit Ca(V)3.2 channels more efficiently than Ca(V)3.1 and Ca(V)3.3 channels via second high-affinity binding site including histidine H191 specific for the Ca(V)3.2 channel.	Zinc	17-19	immunoglobulin lambda variable 7-43	Homo sapiens	51-59	
22131323-3	2011	Divalent cations Zn(2+), Cu(2+) and Ni(2+) inhibit Ca(V)3.2 channels more efficiently than Ca(V)3.1 and Ca(V)3.3 channels via second high-affinity binding site including histidine H191 specific for the Ca(V)3.2 channel.	Zinc	17-19	immunoglobulin lambda variable 7-43	Homo sapiens	202-210	
17670971-3	2007	Here, we demonstrate that reducing agents as well as endogenous metal chelators sensitize C-type dorsal root ganglion nociceptors by chelating Zn2+ ions off specific extracellular histidine residues on Ca(v)3.2 T-channels, thus relieving tonic channel inhibition, enhancing Ca(v)3.2 currents, and lowering the threshold for nociceptor excitability in vitro and in vivo.	Zinc	143-147	immunoglobulin lambda variable 7-43	Homo sapiens	274-282