PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34896074-0	2022	Exploring the permeation of fluoroquinolone metalloantibiotics across outer membrane porins by combining molecular dynamics simulations and a porin-mimetic in vitro model.	Fluoroquinolones	28-43	voltage dependent anion channel 1	Homo sapiens	142-147	
34896074-2	2022	Porin channels are crucial for the permeation of fluoroquinolones across the outer membrane of Gram-negative bacteria and modifications in porin expression are an important mechanism of bacterial resistance.	Fluoroquinolones	49-65	voltage dependent anion channel 1	Homo sapiens	0-5	
34896074-2	2022	Porin channels are crucial for the permeation of fluoroquinolones across the outer membrane of Gram-negative bacteria and modifications in porin expression are an important mechanism of bacterial resistance.	Fluoroquinolones	49-65	voltage dependent anion channel 1	Homo sapiens	139-144	
34896074-7	2022	Molecular dynamics simulations showed that the translocation of the metalloantibiotic through this porin is less favorable than that of free fluoroquinolone, as it presented a much larger free energy barrier to cross the narrow constriction region of the pore.	Fluoroquinolones	141-156	voltage dependent anion channel 1	Homo sapiens	99-104	
34896074-8	2022	Lastly, permeability studies of different fluoroquinolones and their respective copper complexes using a porin-mimetic in vitro model corroborated the lower rate of permeation for the metalloantibiotics relative to the free antibiotics.	Fluoroquinolones	42-58	voltage dependent anion channel 1	Homo sapiens	105-110