PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9950956-8	1999	This effect on AQP2 phosphorylation was mimicked by the vasopressin (V2) agonist, 1-desamino-[8-D-arginine]vasopressin (DDAVP), or forskolin.	Colforsin	131-140	aquaporin 2	Rattus norvegicus	15-19	
9950956-9	1999	Two-dimensional phosphopeptide mapping indicated that AVP and forskolin stimulated the phosphorylation of the same site in AQP2.	Colforsin	62-71	aquaporin 2	Rattus norvegicus	123-127	
9815137-5	1998	Immunofluorescence and biochemical studies indicate a shuttling of AQP-2-bearing vesicles after stimulation with vasopressin or forskolin.	Colforsin	128-137	aquaporin 2	Rattus norvegicus	67-72	
17626240-9	2007	After internalization of AQP2, induced by removal of AVP, forskolin triggered the AQP2 redistribution to the plasma membrane even if microtubules were depolymerized and without the previous positioning of AQP2 in the perinuclear recycling compartment.	Colforsin	58-67	aquaporin 2	Rattus norvegicus	25-29	
17626240-9	2007	After internalization of AQP2, induced by removal of AVP, forskolin triggered the AQP2 redistribution to the plasma membrane even if microtubules were depolymerized and without the previous positioning of AQP2 in the perinuclear recycling compartment.	Colforsin	58-67	aquaporin 2	Rattus norvegicus	82-86	
17626240-9	2007	After internalization of AQP2, induced by removal of AVP, forskolin triggered the AQP2 redistribution to the plasma membrane even if microtubules were depolymerized and without the previous positioning of AQP2 in the perinuclear recycling compartment.	Colforsin	58-67	aquaporin 2	Rattus norvegicus	82-86	
17598476-3	2007	It is known that inhibition of G(i)-proteins with pertussis toxin blocks redistribution of AQP2 into the apical membrane following the application of vasopressin or forskolin.	Colforsin	165-174	aquaporin 2	Rattus norvegicus	91-95	
15625084-2	2005	In transiently transfected MDCK-C7 cells, stimulation with forskolin induced translocation of AQP2-WT to the plasma membrane.	Colforsin	59-68	aquaporin 2	Rattus norvegicus	94-101	
15625084-3	2005	Treatment of AQP2-WT cells with the PKA inhibitor H-89 following forskolin stimulation resulted in internalization of AQP2-WT.	Colforsin	65-74	aquaporin 2	Rattus norvegicus	13-17	
15625084-3	2005	Treatment of AQP2-WT cells with the PKA inhibitor H-89 following forskolin stimulation resulted in internalization of AQP2-WT.	Colforsin	65-74	aquaporin 2	Rattus norvegicus	13-20	
15625084-4	2005	Moreover, H-89 treatment of AQP2-S256D (mimicking constitutively phosphorylated AQP2 and hence localized to the plasma membrane) resulted in redistribution of AQP2-S256D to intracellular vesicles, even in the presence of forskolin.	Colforsin	221-230	aquaporin 2	Rattus norvegicus	28-32	
15625084-4	2005	Moreover, H-89 treatment of AQP2-S256D (mimicking constitutively phosphorylated AQP2 and hence localized to the plasma membrane) resulted in redistribution of AQP2-S256D to intracellular vesicles, even in the presence of forskolin.	Colforsin	221-230	aquaporin 2	Rattus norvegicus	80-84	
15625084-4	2005	Moreover, H-89 treatment of AQP2-S256D (mimicking constitutively phosphorylated AQP2 and hence localized to the plasma membrane) resulted in redistribution of AQP2-S256D to intracellular vesicles, even in the presence of forskolin.	Colforsin	221-230	aquaporin 2	Rattus norvegicus	80-84	
15625084-5	2005	Both PGE2 and dopamine stimulation induced endocytosis of AQP2-WT and AQP2-S256D, respectively, in forskolin-stimulated cells.	Colforsin	99-108	aquaporin 2	Rattus norvegicus	58-62	
12829746-4	2003	However, AVP-, dibutyryl cAMP- and forskolin-induced AQP2 translocation was strongly inhibited.	Colforsin	35-44	aquaporin 2	Rattus norvegicus	53-57	
9988736-3	1999	In nonstimulated IMCD cells the majority of AQP-2 staining was detected intracellularly but became mainly localized within the cell membrane after stimulation with AVP or forskolin.	Colforsin	171-180	aquaporin 2	Rattus norvegicus	44-49	
9988736-4	1999	Quantitative analysis revealed that preincubation of the cells with the synthetic peptide S-Ht31, which prevents the binding between AKAPs and regulatory subunits of PKA, strongly inhibited AQP-2 translocation in response to forskolin.	Colforsin	225-234	aquaporin 2	Rattus norvegicus	190-195	
9988736-5	1999	Preincubation of the cells with the PKA inhibitor H89 prior to forskolin stimulation abolished AQP-2 translocation.	Colforsin	63-72	aquaporin 2	Rattus norvegicus	95-100