PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7756271-3	1995	The m-poly(ethylene glycol)-porin (m-PEG-SC-Porin 50) conjugate, containing one poly(ethylene glycol) chain, was water soluble.	Water	113-118	voltage dependent anion channel 1	Homo sapiens	28-33	
7756271-0	1995	A poly(ethylene glycol) water-soluble conjugate of porin: refolding to the native state.	Water	24-29	voltage dependent anion channel 1	Homo sapiens	51-56	
8874494-7	1996	A model for water-coordinated transport, providing a qualitative view of the porin transport mechanism, is also described.	Water	12-17	voltage dependent anion channel 1	Homo sapiens	77-82	
7756271-3	1995	The m-poly(ethylene glycol)-porin (m-PEG-SC-Porin 50) conjugate, containing one poly(ethylene glycol) chain, was water soluble.	Water	113-118	voltage dependent anion channel 1	Homo sapiens	44-49	
7685033-1	1993	Pores formed in the outer membrane of mitochondria by mitochondrial porin make it permeable to water-soluble metabolites smaller than approximately 5 kDa.	Water	95-100	voltage dependent anion channel 1	Homo sapiens	68-73	
7770452-2	1995	Voltage gating is seen as a perturbation of the electrostatic screening inside the porin pore where, by the influence of the potential gradient, water and counter-ion distribution can be slightly displaced from their equilibrium distribution.	Water	145-150	voltage dependent anion channel 1	Homo sapiens	83-88	
2472293-1	1989	Negatively charged carboxyl groups of mitochondrial porin have been converted into positively charged ones by means of reaction with water-soluble carbodiimide in the presence of ethylenediamine.	Water	133-138	voltage dependent anion channel 1	Homo sapiens	52-57	
2960520-1	1987	The specific recognition by mitochondria of the precursor of porin and the insertion into the outer membrane were studied with a radiolabeled water-soluble form of porin derived from the mature protein.	Water	142-147	voltage dependent anion channel 1	Homo sapiens	164-169	
2850910-3	1988	Evidence from antibiotic MIC studies on porin-deficient mutants compared with their porin-sufficient parent strains has provided strong support for the proposal that some antibiotics, particularly beta-lactams, pass across the outer membrane through the water-filled channels of a class of proteins called porins.	Water	254-259	voltage dependent anion channel 1	Homo sapiens	40-45	
2850910-3	1988	Evidence from antibiotic MIC studies on porin-deficient mutants compared with their porin-sufficient parent strains has provided strong support for the proposal that some antibiotics, particularly beta-lactams, pass across the outer membrane through the water-filled channels of a class of proteins called porins.	Water	254-259	voltage dependent anion channel 1	Homo sapiens	84-89	
2960520-6	1987	Water-soluble porin competed for the specific binding and import of the precursor of the ADP/ATP carrier, an inner membrane protein.	Water	0-5	voltage dependent anion channel 1	Homo sapiens	14-19