PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10585721-1	1999	The human vitamin D receptor (VDR) and retinoid X receptor-alpha (RXRalpha) modulate gene activity by forming homodimeric or heterodimeric complexes with specific DNA sequences and interaction with other elements of the transcriptional apparatus in the presence of their known endogenous ligands 1alpha,25-dihydroxyvitamin D3 (1, 25-[OH]2D3) and 9-cis-retinoic acid (9-c-RA).	Alitretinoin	346-365	vitamin D receptor	Homo sapiens	10-28	
18400206-4	2008	9-cis-RA and all-trans-RA preferentially transactivated the RXR/VDR heterodimers and RXR homodimers.	Alitretinoin	0-8	vitamin D receptor	Homo sapiens	64-67	
12898515-0	2003	9-cis retinoic acid accelerates calcitriol-induced osteocalcin production and promotes degradation of both vitamin D receptor and retinoid X receptor in human osteoblastic cells.	Alitretinoin	0-19	vitamin D receptor	Homo sapiens	107-125	
12939463-1	2003	The vitamin D(3) receptor, which is the nuclear receptor for 1alpha,25-dihydroxyvitamin D(3) (VD(3)), forms a heterodimer with the retinoid X receptor (RXR), which is the nuclear receptor for 9-cis-retinoic acid (9-cis-RA).	Alitretinoin	192-211	vitamin D receptor	Homo sapiens	4-25	
12898515-9	2003	The reduction was accompanied by an increased degradation rate of both VDR and RXRbeta in the presence of 9-cisRA.	Alitretinoin	106-113	vitamin D receptor	Homo sapiens	71-74	
12898515-10	2003	Furthermore, 9-cisRA increased the formation of RXRbeta-VDR-VDRE complex on the osteocalcin gene VDRE.	Alitretinoin	13-20	vitamin D receptor	Homo sapiens	56-59	
12898515-11	2003	These results suggest that 9-cisRA accelerates calcitriol-induced osteocalcin production in human osteoblastic cells through increased formation of transcriptionally active chromatin complexes and, subsequently, promotes degradation of the heterodimeric complex of VDR and RXR.	Alitretinoin	27-34	vitamin D receptor	Homo sapiens	265-268	
10585721-1	1999	The human vitamin D receptor (VDR) and retinoid X receptor-alpha (RXRalpha) modulate gene activity by forming homodimeric or heterodimeric complexes with specific DNA sequences and interaction with other elements of the transcriptional apparatus in the presence of their known endogenous ligands 1alpha,25-dihydroxyvitamin D3 (1, 25-[OH]2D3) and 9-cis-retinoic acid (9-c-RA).	Alitretinoin	346-365	vitamin D receptor	Homo sapiens	30-33	
10585721-4	1999	Addition of 9-c-RA increased RXRalpha homodimer-OP VDRE complexes, and addition of 1,25-(OH) 2D3 resulted in formation of 1, 25-(OH)2D 3-VDR-RXRalpha-OP VDRE complexes.	Alitretinoin	12-18	vitamin D receptor	Homo sapiens	51-54	
9336462-6	1997	Moreover, the transactivation domains of both VDR and RXR were shown to be essential for obtaining responsiveness of the heterodimers to VD and 9- cis retinoic acid (the RXR ligand).	Alitretinoin	144-164	vitamin D receptor	Homo sapiens	46-49	
8076631-10	1994	The presence of an accessory factor in the VDR-DNA complexes was indirectly shown by treatment of the cells with 9-cis retinoic acid and by cycloheximide.	Alitretinoin	113-132	vitamin D receptor	Homo sapiens	43-46	
9077483-2	1997	VDR functions in physiology as a dimer complexed with retinoid X receptor (RXR), whose natural ligand is 9-cis-retinoic acid (9-c-RA).	Alitretinoin	105-124	vitamin D receptor	Homo sapiens	0-3	
8605168-10	1996	9-cis-Retinoic acid attenuates the stimulating effect of 1,25-dihydroxyvitamin D3 by decreasing the rate of VDR-RXR heterodimer formation and simultaneously by increasing the affinity of RXR homodimerization.	Alitretinoin	0-19	vitamin D receptor	Homo sapiens	108-111	
7626514-8	1995	A natural ligand for the RXR co-receptor, 9-cis retinoic acid, suppresses both VDR-RXR binding to the VDRE and 1,25(OH)2D3 stimulated transcription, indicating that 9-cis retinoic acid recruits RXR away from VDR to instead form RXR homodimers.	Alitretinoin	42-61	vitamin D receptor	Homo sapiens	79-82	
7626514-8	1995	A natural ligand for the RXR co-receptor, 9-cis retinoic acid, suppresses both VDR-RXR binding to the VDRE and 1,25(OH)2D3 stimulated transcription, indicating that 9-cis retinoic acid recruits RXR away from VDR to instead form RXR homodimers.	Alitretinoin	42-61	vitamin D receptor	Homo sapiens	102-105	
7626514-8	1995	A natural ligand for the RXR co-receptor, 9-cis retinoic acid, suppresses both VDR-RXR binding to the VDRE and 1,25(OH)2D3 stimulated transcription, indicating that 9-cis retinoic acid recruits RXR away from VDR to instead form RXR homodimers.	Alitretinoin	165-184	vitamin D receptor	Homo sapiens	79-82	
7626514-8	1995	A natural ligand for the RXR co-receptor, 9-cis retinoic acid, suppresses both VDR-RXR binding to the VDRE and 1,25(OH)2D3 stimulated transcription, indicating that 9-cis retinoic acid recruits RXR away from VDR to instead form RXR homodimers.	Alitretinoin	165-184	vitamin D receptor	Homo sapiens	102-105	
9121440-2	1997	The receptors for 9-cis retinoic acid and 1,25-dihydroxyvitamin D3 [1,25(OH)2D3], RXR and VDR, respectively, as members of this superfamily, form a heterodimeric complex and bind cooperatively to vitamin D responsive elements (VDREs) to activate or repress the transcription of a multitude of genes which regulate a variety of physiological functions.	Alitretinoin	18-37	vitamin D receptor	Homo sapiens	90-93	
8579895-7	1995	The natural ligand for the RXR coreceptor, 9-cis retinoic acid, suppresses both VDR-RXR binding to the VDRE and 1,25(OH)2D3-stimulated transcription, indicating that 9-cis retinoic acid diverts RXR away from being the silent partner of VDR to instead form RXR homodimers.	Alitretinoin	43-62	vitamin D receptor	Homo sapiens	80-83	
8579895-7	1995	The natural ligand for the RXR coreceptor, 9-cis retinoic acid, suppresses both VDR-RXR binding to the VDRE and 1,25(OH)2D3-stimulated transcription, indicating that 9-cis retinoic acid diverts RXR away from being the silent partner of VDR to instead form RXR homodimers.	Alitretinoin	43-62	vitamin D receptor	Homo sapiens	103-106	
8579895-7	1995	The natural ligand for the RXR coreceptor, 9-cis retinoic acid, suppresses both VDR-RXR binding to the VDRE and 1,25(OH)2D3-stimulated transcription, indicating that 9-cis retinoic acid diverts RXR away from being the silent partner of VDR to instead form RXR homodimers.	Alitretinoin	166-185	vitamin D receptor	Homo sapiens	80-83	
8579895-7	1995	The natural ligand for the RXR coreceptor, 9-cis retinoic acid, suppresses both VDR-RXR binding to the VDRE and 1,25(OH)2D3-stimulated transcription, indicating that 9-cis retinoic acid diverts RXR away from being the silent partner of VDR to instead form RXR homodimers.	Alitretinoin	166-185	vitamin D receptor	Homo sapiens	103-106	
7862109-6	1995	Like most DR3-type VD response elements, both IP9s are preferentially bound by VDR-RXR heterodimers with a 5"-RXR-VDR-3" polarity, whose transcriptional activity can be enhanced by costimulation with 9-cis retinoic acid.	Alitretinoin	200-219	vitamin D receptor	Homo sapiens	79-82	
7862109-6	1995	Like most DR3-type VD response elements, both IP9s are preferentially bound by VDR-RXR heterodimers with a 5"-RXR-VDR-3" polarity, whose transcriptional activity can be enhanced by costimulation with 9-cis retinoic acid.	Alitretinoin	200-219	vitamin D receptor	Homo sapiens	114-117