PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23677799-0	2013	Claudin-2 pore function requires an intramolecular disulfide bond between two conserved extracellular cysteines.	Cysteine	102-111	claudin 2	Canis lupus familiaris	0-9	
23677799-5	2013	Immunoblotting showed a higher molecular mass band in the mutants with a single cysteine mutation, consistent with a claudin-2 dimer, suggesting that the two conserved cysteines normally form an intramolecular disulfide bond in wild-type claudin-2.	Cysteine	80-88	claudin 2	Canis lupus familiaris	117-126	
23677799-5	2013	Immunoblotting showed a higher molecular mass band in the mutants with a single cysteine mutation, consistent with a claudin-2 dimer, suggesting that the two conserved cysteines normally form an intramolecular disulfide bond in wild-type claudin-2.	Cysteine	168-177	claudin 2	Canis lupus familiaris	117-126	
23677799-5	2013	Immunoblotting showed a higher molecular mass band in the mutants with a single cysteine mutation, consistent with a claudin-2 dimer, suggesting that the two conserved cysteines normally form an intramolecular disulfide bond in wild-type claudin-2.	Cysteine	168-177	claudin 2	Canis lupus familiaris	238-247	
23677799-9	2013	We conclude that the disulfide bond between the conserved extracellular cysteines in claudin-2 is necessary for pore formation, probably by stabilizing the ECL1 fold, but is not required for correct protein trafficking.	Cysteine	72-81	claudin 2	Canis lupus familiaris	85-94