PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28468825-4	2017	We found that two molecules, doxycycline and rifamycin SV, can inhibit beta2m amyloid formation in vitro by causing the formation of amorphous, redissolvable aggregates.	rifamycin SV	45-57	beta-2-microglobulin	Homo sapiens	71-77	
28468825-8	2017	Overall, our results suggest that doxycycline and rifamycin are general inhibitors of Cu(II)-induced beta2m amyloid formation.	rifamycin SV	50-59	beta-2-microglobulin	Homo sapiens	101-107	
25633201-5	2015	In the presence of the antibiotic rifamycin SV, which inhibits amyloid growth of wild-type beta2m, [MePro32]beta2m was nearly quantitatively converted into different spherical oligomeric species.	rifamycin SV	34-46	beta-2-microglobulin	Homo sapiens	91-97	
25633201-5	2015	In the presence of the antibiotic rifamycin SV, which inhibits amyloid growth of wild-type beta2m, [MePro32]beta2m was nearly quantitatively converted into different spherical oligomeric species.	rifamycin SV	34-46	beta-2-microglobulin	Homo sapiens	108-114	
28455257-0	2017	Molecular insights into the inhibitory mechanism of rifamycin SV against beta2-microglobulin aggregation: A molecular dynamics simulation study.	rifamycin SV	52-61	beta-2-microglobulin	Homo sapiens	73-92	
28455257-3	2017	In the present study, molecular docking and molecular dynamics (MD) simulations were performed to elucidate the inhibitory mechanism of an antibiotic, rifamycin SV (C1) reported for its in vitro anti-aggregation activity against beta2m.	rifamycin SV	151-163	beta-2-microglobulin	Homo sapiens	229-235