PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24436330-0	2014	Comprehensive cysteine-scanning mutagenesis reveals Claudin-2 pore-lining residues with different intrapore locations.	Cysteine	14-22	claudin 2	Canis lupus familiaris	52-61	
27359349-7	2017	Claudin-2 mutants (I66C and S68C) with substitution of the pore-lining amino acids with cysteine were used to test the effect of steric blocking of the claudin-2 pore by thiol-reactive reagents.	Cysteine	88-96	claudin 2	Canis lupus familiaris	0-9	
24436330-2	2014	We aimed to map the pore-lining residues of claudin-2 by comprehensive cysteine-scanning mutagenesis of ECL1.	Cysteine	71-79	claudin 2	Canis lupus familiaris	44-53	
19538299-0	2009	Cysteine mutagenesis to study the structure of claudin-2 paracellular pores.	Cysteine	0-8	claudin 2	Canis lupus familiaris	47-56	
19690347-3	2009	Here we applied cysteine scanning to map the paracellular pathway of ion permeation across claudin-2-transfected Madin-Darby canine kidney type I cells.	Cysteine	16-24	claudin 2	Canis lupus familiaris	91-100	
19690347-8	2009	The conductance of wild-type claudin-2 and the other cysteine mutants was only weakly affected.	Cysteine	53-61	claudin 2	Canis lupus familiaris	29-38	
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