PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
21660968-3	2011	EGF decreased surface and total levels of CLDN2, which was inhibited by U0126, a MEK inhibitor.	U 0126	72-77	claudin 2	Canis lupus familiaris	42-47
22396724-0	2012	The PIKfyve inhibitor YM201636 blocks the continuous recycling of the tight junction proteins claudin-1 and claudin-2 in MDCK cells.	6-amino-N-(3-(4-(4-morpholinyl)pyrido(3',2'-4,5)furo(3,2-d)pyrimidin-2-yl)phenyl)-3-pyridinecarboxamide	22-30	claudin 2	Canis lupus familiaris	108-117
22396724-8	2012	Claudin-2 was also found to constantly recycle in confluent MDCK cells and treatment with YM201636 blocked this recycling and caused accumulation of intracellular claudin-2.	6-amino-N-(3-(4-(4-morpholinyl)pyrido(3',2'-4,5)furo(3,2-d)pyrimidin-2-yl)phenyl)-3-pyridinecarboxamide	90-98	claudin 2	Canis lupus familiaris	0-9
22396724-8	2012	Claudin-2 was also found to constantly recycle in confluent MDCK cells and treatment with YM201636 blocked this recycling and caused accumulation of intracellular claudin-2.	6-amino-N-(3-(4-(4-morpholinyl)pyrido(3',2'-4,5)furo(3,2-d)pyrimidin-2-yl)phenyl)-3-pyridinecarboxamide	90-98	claudin 2	Canis lupus familiaris	163-172
22143774-5	2011	Claudin-2, a molecule responsible for the Na(+) and H(2)O permeability of the TJs, is also present at the cilium, as it colocalizes and coprecipitates with acetylated alpha-tubulin.	Water	52-57	claudin 2	Canis lupus familiaris	0-9
21660968-5	2011	The fluorescence signal for CLDN2 disappeared on treatment with EGF, which was inhibited by U0126.	U 0126	92-97	claudin 2	Canis lupus familiaris	28-33
21660968-6	2011	EGF accelerated the decrease in CLDN2 in the presence of cycloheximide, a translation inhibitor, indicating that EGF reduces the stability of the protein.	Cycloheximide	57-70	claudin 2	Canis lupus familiaris	32-37
21660968-7	2011	Chloroquine, a lysosomal protease inhibitor, blocked the EGF-induced decrease in CLDN2 protein and caused the co-localization of CLDN2 with Lamp-1, a marker of lysosome.	Chloroquine	0-11	claudin 2	Canis lupus familiaris	81-86
21660968-7	2011	Chloroquine, a lysosomal protease inhibitor, blocked the EGF-induced decrease in CLDN2 protein and caused the co-localization of CLDN2 with Lamp-1, a marker of lysosome.	Chloroquine	0-11	claudin 2	Canis lupus familiaris	129-134
21660968-8	2011	Monodancylcadaverine, an inhibitor of endocytosis, and clathrin siRNA blocked the EGF-induced decrease in CLDN2 and the translocation of CLDN2 from the TJs to the lysosome.	monodancylcadaverine	0-20	claudin 2	Canis lupus familiaris	137-142
21660968-9	2011	EGF increased the association of CLDN2 with clathrin and adaptin alpha which was inhibited by U0126.	U 0126	94-99	claudin 2	Canis lupus familiaris	33-38
31188544-3	2020	Claudin-2, but not claudin-10b, also forms water channels.	Water	43-48	claudin 2	Canis lupus familiaris	0-9
20717932-4	2011	To knockdown claudin-2 expression, we made the cells expressing doxycycline-inducible claudin-2 shRNA vector.	Doxycycline	64-75	claudin 2	Canis lupus familiaris	13-22
20717932-4	2011	To knockdown claudin-2 expression, we made the cells expressing doxycycline-inducible claudin-2 shRNA vector.	Doxycycline	64-75	claudin 2	Canis lupus familiaris	86-95
19538292-3	2009	It is also known that inducible expression of claudin-2, but not claudin-4, will selectively increase the permeability for polyethylene glycol (PEG) molecules which are <0.4 A in radius, but it is not known whether permeability is controlled by the same regions of claudins which control charge selectivity.	Polyethylene Glycols	123-142	claudin 2	Canis lupus familiaris	46-55
19538292-3	2009	It is also known that inducible expression of claudin-2, but not claudin-4, will selectively increase the permeability for polyethylene glycol (PEG) molecules which are <0.4 A in radius, but it is not known whether permeability is controlled by the same regions of claudins which control charge selectivity.	Polyethylene Glycols	144-147	claudin 2	Canis lupus familiaris	46-55
19538292-4	2009	Using inducible expression of chimeras of claudin-2 and claudin-4 in monolayers of MDCK II cells we show that the extracellular loops alone are responsible for controlling the permeability for noncharged PEGs as well as for charge selectivity.	Polyethylene Glycols	204-208	claudin 2	Canis lupus familiaris	42-51
19538299-0	2009	Cysteine mutagenesis to study the structure of claudin-2 paracellular pores.	Cysteine	0-8	claudin 2	Canis lupus familiaris	47-56
19538299-3	2009	Using stable transfected Madin Darby canine kidney type I cells, induced to express claudin-2, we show that paracellular cation transport can be blocked by sulfhydryl-specific methanethiosulfonate (MTS) and that SCAM can be used to identify residues that line paracellular pores.	sulfhydryl-specific methanethiosulfonate	156-196	claudin 2	Canis lupus familiaris	84-93
19538299-3	2009	Using stable transfected Madin Darby canine kidney type I cells, induced to express claudin-2, we show that paracellular cation transport can be blocked by sulfhydryl-specific methanethiosulfonate (MTS) and that SCAM can be used to identify residues that line paracellular pores.	methanethiosulfonate	198-201	claudin 2	Canis lupus familiaris	84-93
15569684-9	2005	U0126 treatment of MDCK strain I cells decreased active ERK 1/2 levels, induced expression of claudin-2 protein, and decreased TER by approximately 20-fold.	U 0126	0-5	claudin 2	Canis lupus familiaris	94-103
33120983-4	2020	The effect of flavonoids on the protein expression level of claudin (CLD)-2 and its subcellular localization were investigated.	Flavonoids	14-24	claudin 2	Canis lupus familiaris	60-75
20807759-0	2010	Calcium inhibits paracellular sodium conductance through claudin-2 by competitive binding.	Calcium	0-7	claudin 2	Canis lupus familiaris	57-66
20807759-4	2010	To investigate the underlying molecular mechanisms, we studied the effects of calcium on the permeability of claudin-2, expressed in an inducible MDCK I cell line.	Calcium	78-85	claudin 2	Canis lupus familiaris	109-118
20807759-5	2010	We found that in the physiological range, calcium acts as a reversible inhibitor of the total conductance and Na(+) permeability of claudin-2, without causing changes in tight junction structure.	Calcium	42-49	claudin 2	Canis lupus familiaris	132-141
20460438-7	2010	Under all conditions, water flux in claudin-2-transfected cells was elevated compared with vector controls, indicating claudin-2-mediated paracellular water permeability.	Water	22-27	claudin 2	Canis lupus familiaris	36-45
20460438-7	2010	Under all conditions, water flux in claudin-2-transfected cells was elevated compared with vector controls, indicating claudin-2-mediated paracellular water permeability.	Water	22-27	claudin 2	Canis lupus familiaris	119-128
20460438-7	2010	Under all conditions, water flux in claudin-2-transfected cells was elevated compared with vector controls, indicating claudin-2-mediated paracellular water permeability.	Water	151-156	claudin 2	Canis lupus familiaris	36-45
20460438-7	2010	Under all conditions, water flux in claudin-2-transfected cells was elevated compared with vector controls, indicating claudin-2-mediated paracellular water permeability.	Water	151-156	claudin 2	Canis lupus familiaris	119-128
20460438-10	2010	We conclude that claudin-2, but not claudin-10b, forms a paracellular water channel and thus mediates paracellular water transport in leaky epithelia.	Water	70-75	claudin 2	Canis lupus familiaris	17-26
20460438-10	2010	We conclude that claudin-2, but not claudin-10b, forms a paracellular water channel and thus mediates paracellular water transport in leaky epithelia.	Water	115-120	claudin 2	Canis lupus familiaris	17-26
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
33806674-7	2021	Accordingly, diclofenac and indomethacin were found to decrease the subcellular localization of claudin (CLD)-2 but not occludin and ZO-1 at the apicolateral intercellular compartment of Madin-Darby canine kidney (MDCK) II cells.	Diclofenac	13-23	claudin 2	Canis lupus familiaris	96-111
33806674-7	2021	Accordingly, diclofenac and indomethacin were found to decrease the subcellular localization of claudin (CLD)-2 but not occludin and ZO-1 at the apicolateral intercellular compartment of Madin-Darby canine kidney (MDCK) II cells.	Indomethacin	28-40	claudin 2	Canis lupus familiaris	96-111
31188544-15	2020	CONCLUSION: Claudin-15, similar to claudin-2, forms a paracellular cation and water channel.	Water	78-83	claudin 2	Canis lupus familiaris	35-44
27359349-0	2017	Claudin-2-mediated cation and water transport share a common pore.	Water	30-35	claudin 2	Canis lupus familiaris	0-9
30468279-5	2019	Immunofluorescence and Western blot analyses showed that mannitol treatment induced a significant increase in the tight junctional and cellular content of claudin-1 (a barrier-forming claudin) as well as a significant decrease in claudin-2 (a pore-forming claudin) junctional and cellular contents.	Mannitol	57-65	claudin 2	Canis lupus familiaris	230-239
29474583-9	2018	While ochratoxin A and citrinin are known to be nephrotoxic, only deoxynivalenol reduced claudin-2 expression in MDCK II cells derived from the renal tubule.	deoxynivalenol	66-80	claudin 2	Canis lupus familiaris	89-98
27359349-2	2017	Former studies revealed that claudin-2 forms paracellular channels for small cations like sodium and potassium and also paracellular channels for water.	Water	146-151	claudin 2	Canis lupus familiaris	29-38
27359349-3	2017	This study analyses whether the diffusive transport of sodium and water occurs through a common pore of the claudin-2 channel.	Sodium	55-61	claudin 2	Canis lupus familiaris	108-117
27359349-3	2017	This study analyses whether the diffusive transport of sodium and water occurs through a common pore of the claudin-2 channel.	Water	66-71	claudin 2	Canis lupus familiaris	108-117
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
27359349-10	2017	CONCLUSION: Our results indicate that claudin-2-mediated cation and water transport are frictionally coupled and share a common pore.	Water	68-73	claudin 2	Canis lupus familiaris	38-47
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
25825272-2	2015	Here, we found that the hyperosmolarity-induced decrease in claudin-2 expression is inhibited by Go6983, a non-selective protein kinase C (PKC) inhibitor, and PKCbeta specific inhibitor in Madin-Darby canine kidney II cells.	2-(1-(3-dimethylaminopropyl)-5-methoxyindol-3-yl)-3-(1H-indol-3-yl)maleimide	97-103	claudin 2	Canis lupus familiaris	60-69
25825272-4	2015	Phorbol 12-myristate 13-acetate, a PKC activator, decreased claudin-2 expression.	Tetradecanoylphorbol Acetate	0-31	claudin 2	Canis lupus familiaris	60-69
25825272-6	2015	Hyperosmolarity decreased promoter activity of claudin-2, which was inhibited by Go6983 and PKCbeta inhibitor similar to those in real-time PCR and Western blotting.	2-(1-(3-dimethylaminopropyl)-5-methoxyindol-3-yl)-3-(1H-indol-3-yl)maleimide	81-87	claudin 2	Canis lupus familiaris	47-56
25825272-8	2015	Claudin-2 has hyperosmolarity-sensitive region in its promoter, which includes GATA binding site.	gata	79-83	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
23760508-3	2013	To test this, we generated MDCK I Tet-off cells stably transfected with claudin-2 Tyr(67) mutants.	Tyrosine	82-85	claudin 2	Canis lupus familiaris	72-81
24140471-6	2014	OUA-induced degradation of proteins is either sensitive (CLDN-4, OCLN and ZO-1) or insensitive (CLDN-2) to ERK1/2 inhibition.	Ouabain	0-3	claudin 2	Canis lupus familiaris	96-102
24140471-7	2014	In agreement with the protein degradation findings, OUA decreases the cellular content of ZO-1 and CLDN-2 mRNAs but surprisingly, increases the mRNA of CLDN-4 and OCLN.	Ouabain	52-55	claudin 2	Canis lupus familiaris	99-105
23677799-0	2013	Claudin-2 pore function requires an intramolecular disulfide bond between two conserved extracellular cysteines.	Disulfides	51-60	claudin 2	Canis lupus familiaris	0-9
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
23677799-5	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.	Disulfides	210-219	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.	Disulfides	210-219	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.	Disulfides	21-30	claudin 2	Canis lupus familiaris	85-94
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
22825868-0	2012	Phosphorylation of claudin-2 on serine 208 promotes membrane retention and reduces trafficking to lysosomes.	Serine	32-38	claudin 2	Canis lupus familiaris	19-28
22825868-3	2012	In this study, we used mass spectrometry (MS) analysis of purified claudin-2 from MDCK II cells and found that the cytoplasmic tail is multiply phosphorylated on serines, a threonine and tyrosines.	Serine	162-169	claudin 2	Canis lupus familiaris	67-76
22825868-3	2012	In this study, we used mass spectrometry (MS) analysis of purified claudin-2 from MDCK II cells and found that the cytoplasmic tail is multiply phosphorylated on serines, a threonine and tyrosines.	Threonine	173-182	claudin 2	Canis lupus familiaris	67-76
22825868-3	2012	In this study, we used mass spectrometry (MS) analysis of purified claudin-2 from MDCK II cells and found that the cytoplasmic tail is multiply phosphorylated on serines, a threonine and tyrosines.	Tyrosine	187-196	claudin 2	Canis lupus familiaris	67-76
22825868-6	2012	Mutations at sites that were previously reported to interfere with plasma membrane targeting of claudin-2 reduced phosphorylation at S208, suggesting that membrane localisation is required for phosphorylation; however phosphorylation at S208 did not affect binding to ZO-1 or ZO-2 Administration of forskolin or PGE2 resulted in dephosphorylation at S208 and transient small increases in transepithelial electrical resistance (TER).	Colforsin	299-308	claudin 2	Canis lupus familiaris	96-105
22825868-6	2012	Mutations at sites that were previously reported to interfere with plasma membrane targeting of claudin-2 reduced phosphorylation at S208, suggesting that membrane localisation is required for phosphorylation; however phosphorylation at S208 did not affect binding to ZO-1 or ZO-2 Administration of forskolin or PGE2 resulted in dephosphorylation at S208 and transient small increases in transepithelial electrical resistance (TER).	Dinoprostone	312-316	claudin 2	Canis lupus familiaris	96-105