PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23460207-6	2013	Consistent with the Shu complex containing Rad51 paralogues, the methyl methanesulphonate sensitivity of Csm2 is exacerbated at colder temperatures.	Methyl Methanesulfonate	65-89	recombinase RAD51	Saccharomyces cerevisiae S288C	43-48	
30894431-10	2019	The E108L-rad51 strain manifested severe sensitivity toward methyl methanesulfonate (MMS) and a complete loss of gene conversion efficiency, a phenotype similar to that of the Deltarad51 strain.	Methyl Methanesulfonate	60-83	recombinase RAD51	Saccharomyces cerevisiae S288C	10-15	
30894431-10	2019	The E108L-rad51 strain manifested severe sensitivity toward methyl methanesulfonate (MMS) and a complete loss of gene conversion efficiency, a phenotype similar to that of the Deltarad51 strain.	Methyl Methanesulfonate	85-88	recombinase RAD51	Saccharomyces cerevisiae S288C	10-15	
25380755-8	2015	The most significant observations include the dramatic abrogation of HR activity and the marked decrease in Rad51 focus formation in the charged linker deletion mutant of Hsp82 upon MMS treatment.	Methyl Methanesulfonate	182-185	recombinase RAD51	Saccharomyces cerevisiae S288C	108-113	
23798704-7	2013	Interestingly, a hybrid protein containing the N-terminal region of Rad54, responsible for Rad51 interaction, fused to the Swi2/Snf2 core of Rdh54 is able to effectively complement the sensitivity to both methyl methanesulfonate and excess Rad51 in rdh54 null cells.	Methyl Methanesulfonate	205-228	recombinase RAD51	Saccharomyces cerevisiae S288C	91-96	
27001511-7	2016	Regulation of HR by NMD extends to multiple targets beyond RAD55, including RAD51, RAD54 and RAD57 Finally, we demonstrate that loss of NMD results in an increase in recombination rates and resistance to the DNA damaging agent methyl methanesulfonate, suggesting this pathway negatively regulates HR under normal growth conditions.	Methyl Methanesulfonate	227-250	recombinase RAD51	Saccharomyces cerevisiae S288C	76-81	
17671161-3	2007	Here, we have identified a specific role for the Shu proteins in a Rad51/Rad54-dependent HRR pathway(s) to repair MMS-induced lesions during S-phase.	Methyl Methanesulfonate	114-117	recombinase RAD51	Saccharomyces cerevisiae S288C	67-72	
23328489-5	2013	Therefore, we expressed the wild-type BRCA2 in yeast and determined the effect of BRCA2 on yeast homologous recombination, methyl methanesulphonate (MMS)-induced Rad51 and Rad52 foci and MMS sensitivity.	Methyl Methanesulfonate	123-147	recombinase RAD51	Saccharomyces cerevisiae S288C	162-167	
23328489-5	2013	Therefore, we expressed the wild-type BRCA2 in yeast and determined the effect of BRCA2 on yeast homologous recombination, methyl methanesulphonate (MMS)-induced Rad51 and Rad52 foci and MMS sensitivity.	Methyl Methanesulfonate	149-152	recombinase RAD51	Saccharomyces cerevisiae S288C	162-167	
17671161-4	2007	We show that, although mutation of RAD51 or RAD54 prevented the formation of MMS-induced HRR intermediates (X-molecules) arising during replication in sgs1 cells, mutation of SHU genes attenuated the level of these structures.	Methyl Methanesulfonate	77-80	recombinase RAD51	Saccharomyces cerevisiae S288C	35-40	
8910403-6	1996	Consistent with the results from the biochemical analyses, expression of the rad51 Arg-191 protein in a rad51 null mutant confers normal cellular resistance to the DNA damaging agent methylmethane sulfonate, suggesting that nucleotide binding by Rad51 is sufficient for biological function.	Methyl Methanesulfonate	183-206	recombinase RAD51	Saccharomyces cerevisiae S288C	77-82	
10409728-4	1999	The PCNA-binding defect alone had little effect on mutation, recombination, and the methyl methanesulfonate (MMS) response in repair-competent cells, but it greatly amplified the MMS sensitivity of a rad51 mutant.	Methyl Methanesulfonate	179-182	recombinase RAD51	Saccharomyces cerevisiae S288C	200-205	
9171366-5	1997	Strikingly, overexpression of Rad54p can functionally suppress the UV and methyl methanesulfonate sensitivity caused by a deletion of the RAD51 gene.	Methyl Methanesulfonate	74-97	recombinase RAD51	Saccharomyces cerevisiae S288C	138-143	
8910403-6	1996	Consistent with the results from the biochemical analyses, expression of the rad51 Arg-191 protein in a rad51 null mutant confers normal cellular resistance to the DNA damaging agent methylmethane sulfonate, suggesting that nucleotide binding by Rad51 is sufficient for biological function.	Methyl Methanesulfonate	183-206	recombinase RAD51	Saccharomyces cerevisiae S288C	104-109	
7958917-6	1994	The effect of this allele was dependent on the presence of wild-type Rad51 because MMS sensitivity of rad51 delta strains were not increased by its expression.	Methyl Methanesulfonate	83-86	recombinase RAD51	Saccharomyces cerevisiae S288C	69-74	
7958917-6	1994	The effect of this allele was dependent on the presence of wild-type Rad51 because MMS sensitivity of rad51 delta strains were not increased by its expression.	Methyl Methanesulfonate	83-86	recombinase RAD51	Saccharomyces cerevisiae S288C	102-107