PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15329499-6	2004	We found that the yeast Rad27 protein complements sensitivity to methyl methanesulfonate in an E. coli mutant.	Methyl Methanesulfonate	65-88	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	24-29	
24777061-4	2014	Pol beta expression rescued methyl methanesulfonate sensitivity in aprataxin (hnt3)- and FEN1 (rad27)-deficient yeast.	Methyl Methanesulfonate	28-51	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	89-93	
24777061-4	2014	Pol beta expression rescued methyl methanesulfonate sensitivity in aprataxin (hnt3)- and FEN1 (rad27)-deficient yeast.	Methyl Methanesulfonate	28-51	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	95-100	
23144716-3	2012	In S. cerevisiae, Rad27(Fen1) was suggested to protect against MMS-induced cytotoxicity by excising multinucleotide flaps generated during repair.	Methyl Methanesulfonate	63-66	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	18-23	
23144716-3	2012	In S. cerevisiae, Rad27(Fen1) was suggested to protect against MMS-induced cytotoxicity by excising multinucleotide flaps generated during repair.	Methyl Methanesulfonate	63-66	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	24-28	
23144716-6	2012	Human Pol beta was expressed in S. cerevisiae, and this partially rescued the MMS hypersensitivity observed with rad27(fen1)-null cells.	Methyl Methanesulfonate	78-81	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	113-118	
23144716-6	2012	Human Pol beta was expressed in S. cerevisiae, and this partially rescued the MMS hypersensitivity observed with rad27(fen1)-null cells.	Methyl Methanesulfonate	78-81	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	119-123	
23144716-9	2012	These results suggest that after MMS exposure, the 5"-dRP group in the repair intermediate is cytotoxic and that Rad27(Fen1) protection against MMS in wild-type cells is due to elimination of the 5"-dRP group.	Methyl Methanesulfonate	144-147	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	113-118	
23144716-9	2012	These results suggest that after MMS exposure, the 5"-dRP group in the repair intermediate is cytotoxic and that Rad27(Fen1) protection against MMS in wild-type cells is due to elimination of the 5"-dRP group.	Methyl Methanesulfonate	144-147	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	119-123	
12893088-7	2003	While generally similar findings were observed with RAD2, overexpression of RAD2, but not EXO1, suppressed the MMS sensitivity of the rad27 null mutant cells.	Methyl Methanesulfonate	111-114	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	134-139	
7876174-5	1995	The rth1 delta mutation does not affect UV or gamma-ray sensitivity but enhances sensitivity to the alkylating agent methyl methanesulfonate.	Methyl Methanesulfonate	117-140	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	4-8	
9927726-3	1999	The rad27 deletion mutants are highly sensitive to methylmethane sulfonate (MMS).	Methyl Methanesulfonate	51-74	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	4-9	
9927726-3	1999	The rad27 deletion mutants are highly sensitive to methylmethane sulfonate (MMS).	Methyl Methanesulfonate	76-79	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	4-9	
9927726-4	1999	By examining the role of Rad27 in different modes of DNA excision repair, we wish to understand why the cytotoxic effect of MMS is dramatically enhanced in the absence of Rad27.	Methyl Methanesulfonate	124-127	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	25-30	
9927726-8	1999	Surprisingly, we found that Apn1 endonuclease sensitizes rad27 mutant cells to MMS.	Methyl Methanesulfonate	79-82	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	57-62	
9927726-9	1999	Deleting the APN1 gene largely restored the resistance of rad27 mutants to MMS.	Methyl Methanesulfonate	75-78	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	58-63	
9852084-6	1998	In addition, expression from the Xenopus cDNAs complemented the temperature and methyl methanesulfonate sensitivity of a yeast rad27 deletion, which eliminates the endogenous FEN-1 gene product.	Methyl Methanesulfonate	80-103	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	127-132	
9852084-6	1998	In addition, expression from the Xenopus cDNAs complemented the temperature and methyl methanesulfonate sensitivity of a yeast rad27 deletion, which eliminates the endogenous FEN-1 gene product.	Methyl Methanesulfonate	80-103	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	175-180	
9837987-3	1998	All four rad27 mutants showed similar high levels of mitotic recombination, but varied in their growth rate at various temperatures, and sensitivity to the DNA damaging agent methyl methane sulfonate.	Methyl Methanesulfonate	175-199	multifunctional nuclease RAD27	Saccharomyces cerevisiae S288C	9-14