PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17121826-4 2007 By constructing chimeras between human PMAT and ENT1, we showed that a chimera consisting of transmembrane domains (TM) 1-6 of PMAT and TM7-11 of hENT1 behaved like PMAT, transporting 1-methyl-4-phenylpyridinium (MPP+, an organic cation) but not uridine (a nucleoside), suggesting that TM1-6 contains critical domains responsible for substrate recognition. 1-Methyl-4-phenylpyridinium 184-211 solute carrier family 29 member 1 (Augustine blood group) Homo sapiens 48-52 17121826-4 2007 By constructing chimeras between human PMAT and ENT1, we showed that a chimera consisting of transmembrane domains (TM) 1-6 of PMAT and TM7-11 of hENT1 behaved like PMAT, transporting 1-methyl-4-phenylpyridinium (MPP+, an organic cation) but not uridine (a nucleoside), suggesting that TM1-6 contains critical domains responsible for substrate recognition. 1-Methyl-4-phenylpyridinium 184-211 solute carrier family 29 member 1 (Augustine blood group) Homo sapiens 146-151