PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23166498-8	2012	We show that all of the anti-HCV ribonucleoside analogues are substrates for human mitochondrial RNA polymerase (POLRMT) and eukaryotic core RNA polymerase II (Pol II) in vitro.	Ribonucleosides	33-47	RNA polymerase mitochondrial	Homo sapiens	113-119	
23166498-11	2012	Evaluation of transcription in cells confirmed sensitivity of POLRMT to antiviral ribonucleosides, while Pol II remained predominantly refractory.	Ribonucleosides	82-97	RNA polymerase mitochondrial	Homo sapiens	62-68	
29739852-2	2018	Therefore, it is essential that all new ribonucleoside analogue drugs be accurately screened for POLRMT inhibition.	Ribonucleosides	40-54	RNA polymerase mitochondrial	Homo sapiens	97-103	
29180528-1	2018	There is a growing body of evidence suggesting that some ribonucleoside/ribonucleotide analogs may be incorporated into mitochondrial RNA by human mitochondrial DNA-dependent RNA polymerase (POLRMT) and disrupt mitochondrial RNA synthesis.	Ribonucleosides	57-71	RNA polymerase mitochondrial	Homo sapiens	191-197	
28412183-2	2017	Some have hypothesized that the active metabolites of toxic ribonucleoside analogs, the triphosphate forms, inadvertently target human mitochondrial RNA polymerase (POLRMT), thus inhibiting mitochondrial RNA transcription and protein synthesis.	Ribonucleosides	60-74	RNA polymerase mitochondrial	Homo sapiens	165-171