PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
11300786-3	2001	After immunoaffinity and HPLC purification, MALDI/MS measured a higher molecular mass for r-p53 from okadaic acid treatment relative to control, suggesting a higher phosphorylation state.	Okadaic Acid	101-113	retinol dehydrogenase 12	Homo sapiens	90-95
12226107-7	2002	Furthermore, photoreceptor RDH12 could be involved in the production of 11-cis-retinal from 11-cis-retinol during regeneration of the cone visual pigments.	Retinaldehyde	72-86	retinol dehydrogenase 12	Homo sapiens	27-32
12226107-7	2002	Furthermore, photoreceptor RDH12 could be involved in the production of 11-cis-retinal from 11-cis-retinol during regeneration of the cone visual pigments.	Vitamin A	92-106	retinol dehydrogenase 12	Homo sapiens	27-32
34850377-6	2022	In contrast, S. cerevisiae harboring human RDH12 produced retinol selectively with negligible production of retinal.	Vitamin A	58-65	retinol dehydrogenase 12	Homo sapiens	43-48
34850377-7	2022	The resulting strain (SR8A-RDH12) produced retinol only.	Vitamin A	43-50	retinol dehydrogenase 12	Homo sapiens	27-32
34850377-12	2022	In conclusion, we achieved selective production of retinol efficiently from xylose by introducing human RDH12 and NADH oxidase into S. cerevisiae.	Vitamin A	51-58	retinol dehydrogenase 12	Homo sapiens	104-109
34850377-12	2022	In conclusion, we achieved selective production of retinol efficiently from xylose by introducing human RDH12 and NADH oxidase into S. cerevisiae.	Xylose	76-82	retinol dehydrogenase 12	Homo sapiens	104-109
35282004-0	2022	New associations of serum beta-carotene, lycopene, and zeaxanthin concentrations with NR1H3, APOB, RDH12, AND CYP genes.	beta Carotene	26-39	retinol dehydrogenase 12	Homo sapiens	99-104
35491887-1	2022	Retinol dehydrogenase 12 (RDH12) is a small gene located on chromosome 14, encoding an enzyme capable of metabolizing retinoids.	Retinoids	118-127	retinol dehydrogenase 12	Homo sapiens	0-24
35491887-1	2022	Retinol dehydrogenase 12 (RDH12) is a small gene located on chromosome 14, encoding an enzyme capable of metabolizing retinoids.	Retinoids	118-127	retinol dehydrogenase 12	Homo sapiens	26-31
35282004-9	2022	Retinol dehydrogenase 12 (RDH12) "functional partner" polymorphism rs756473 (p = 7.422 x 10-5) was associated with higher lycopene concentration.	Lycopene	122-130	retinol dehydrogenase 12	Homo sapiens	0-24
35282004-9	2022	Retinol dehydrogenase 12 (RDH12) "functional partner" polymorphism rs756473 (p = 7.422 x 10-5) was associated with higher lycopene concentration.	Lycopene	122-130	retinol dehydrogenase 12	Homo sapiens	26-31
34567070-6	2021	RT-PCR is employed to find that there is a skipping of exon 10 in MFSD8 and a 15-nucleotide retention of intron5 in RDH12.	15-nucleotide	78-91	retinol dehydrogenase 12	Homo sapiens	116-121
34445569-1	2021	Retinol dehydrogenase 12 (RDH12) is expressed in photoreceptor inner segments and catalyses the reduction of all-trans retinal (atRAL) to all-trans retinol (atROL), as part of the visual cycle.	Vitamin A	148-155	retinol dehydrogenase 12	Homo sapiens	0-24
34445569-1	2021	Retinol dehydrogenase 12 (RDH12) is expressed in photoreceptor inner segments and catalyses the reduction of all-trans retinal (atRAL) to all-trans retinol (atROL), as part of the visual cycle.	Vitamin A	148-155	retinol dehydrogenase 12	Homo sapiens	26-31
35282004-0	2022	New associations of serum beta-carotene, lycopene, and zeaxanthin concentrations with NR1H3, APOB, RDH12, AND CYP genes.	Zeaxanthins	55-65	retinol dehydrogenase 12	Homo sapiens	99-104
35282004-12	2022	Zeaxanthin, lycopene, and beta-carotene serum concentrations might depend on genetic variation in NR1H3, APOB, RDH12 and CYP2C9, CYP2C18, and CYP2C19 genes.	Zeaxanthins	0-10	retinol dehydrogenase 12	Homo sapiens	111-116
26596838-7	2016	Aspirin also acetylated recombinant p53 (rp53) in vitro suggesting that it occurs through a non-enzymatic chemical reaction.	Aspirin	0-7	retinol dehydrogenase 12	Homo sapiens	41-45
35282004-12	2022	Zeaxanthin, lycopene, and beta-carotene serum concentrations might depend on genetic variation in NR1H3, APOB, RDH12 and CYP2C9, CYP2C18, and CYP2C19 genes.	Lycopene	12-20	retinol dehydrogenase 12	Homo sapiens	111-116
35282004-12	2022	Zeaxanthin, lycopene, and beta-carotene serum concentrations might depend on genetic variation in NR1H3, APOB, RDH12 and CYP2C9, CYP2C18, and CYP2C19 genes.	beta Carotene	26-39	retinol dehydrogenase 12	Homo sapiens	111-116
31237438-4	2019	In the retina, RDH12 plays a critical role in reducing toxic retinaldehydes generated by visual cycle activity that is required for the light response of the photoreceptor cells.	Retinaldehyde	61-75	retinol dehydrogenase 12	Homo sapiens	15-20
26596838-8	2016	Mass spectrometry analysis and immunoblotting identified 10 acetylated lysines on rp53, and molecular modeling showed that all lysines targeted by aspirin are surface exposed.	Lysine	71-78	retinol dehydrogenase 12	Homo sapiens	82-86
26596838-8	2016	Mass spectrometry analysis and immunoblotting identified 10 acetylated lysines on rp53, and molecular modeling showed that all lysines targeted by aspirin are surface exposed.	Aspirin	147-154	retinol dehydrogenase 12	Homo sapiens	82-86
22181347-8	2012	Besides 11beta-hydroxysteroid dehydrogenase 1, it has been reported, so far, that retinol dehydrogenase 12 participates only in the detoxification of unsaturated aldehydes formed upon oxidative stress.	unsaturated aldehydes	150-171	retinol dehydrogenase 12	Homo sapiens	82-106
20600834-4	2010	On immunoblots, the purified antibodies did not react with native p53 or recombinant p53 (rp53), but readily detected the glutathionylated or cysteinylated or ethanethiol-treated rp53 only under nonreducing conditions.	ethanethiol	159-170	retinol dehydrogenase 12	Homo sapiens	179-183
21232531-1	2011	Retinol dehydrogenase 12 (RDH12) is a microsomal enzyme that catalyzes the reduction of all-trans-retinaldehyde to all-trans-retinol when expressed in cells.	Retinaldehyde	88-111	retinol dehydrogenase 12	Homo sapiens	0-24
21232531-1	2011	Retinol dehydrogenase 12 (RDH12) is a microsomal enzyme that catalyzes the reduction of all-trans-retinaldehyde to all-trans-retinol when expressed in cells.	Retinaldehyde	88-111	retinol dehydrogenase 12	Homo sapiens	26-31
21232531-1	2011	Retinol dehydrogenase 12 (RDH12) is a microsomal enzyme that catalyzes the reduction of all-trans-retinaldehyde to all-trans-retinol when expressed in cells.	Vitamin A	115-132	retinol dehydrogenase 12	Homo sapiens	0-24
21232531-1	2011	Retinol dehydrogenase 12 (RDH12) is a microsomal enzyme that catalyzes the reduction of all-trans-retinaldehyde to all-trans-retinol when expressed in cells.	Vitamin A	115-132	retinol dehydrogenase 12	Homo sapiens	26-31
21232531-7	2011	T49M-expressing living cells treated with the inhibitors of proteosome activity or with dimethyl sulfoxide exhibited an increase in the conversion of retinaldehyde to retinol, consistent with the recovery of functional RDH12 protein.	Dimethyl Sulfoxide	88-106	retinol dehydrogenase 12	Homo sapiens	219-224
17512723-0	2007	RDH12, a retinol dehydrogenase causing Leber"s congenital amaurosis, is also involved in steroid metabolism.	Steroids	89-96	retinol dehydrogenase 12	Homo sapiens	0-5
19686838-0	2010	Retinol dehydrogenase 12 detoxifies 4-hydroxynonenal in photoreceptor cells.	4-hydroxy-2-nonenal	36-52	retinol dehydrogenase 12	Homo sapiens	0-24
19686838-3	2010	Previous studies showed that RDH12, and the closely related retinol dehydrogenase RDH11, can enzymatically reduce toxic lipid peroxidation products such as 4-hydroxynonenal (4-HNE), in vitro.	4-hydroxy-2-nonenal	156-172	retinol dehydrogenase 12	Homo sapiens	29-34
19686838-3	2010	Previous studies showed that RDH12, and the closely related retinol dehydrogenase RDH11, can enzymatically reduce toxic lipid peroxidation products such as 4-hydroxynonenal (4-HNE), in vitro.	4-hydroxy-2-nonenal	174-179	retinol dehydrogenase 12	Homo sapiens	29-34
18396173-2	2008	In vitro, RDH12 recognizes both retinoids and medium-chain aldehydes as substrates.	Retinoids	32-41	retinol dehydrogenase 12	Homo sapiens	10-15
18396173-2	2008	In vitro, RDH12 recognizes both retinoids and medium-chain aldehydes as substrates.	Aldehydes	59-68	retinol dehydrogenase 12	Homo sapiens	10-15
18396173-3	2008	Our previous study suggested that RDH12 protects cells against toxic levels of retinaldehyde and retinoic acid [S.A. Lee, O.V.	Retinaldehyde	79-92	retinol dehydrogenase 12	Homo sapiens	34-39
18396173-3	2008	Our previous study suggested that RDH12 protects cells against toxic levels of retinaldehyde and retinoic acid [S.A. Lee, O.V.	Tretinoin	97-110	retinol dehydrogenase 12	Homo sapiens	34-39
18396173-5	2008	Popov, N.Y. Kedishvili, Overproduction of bioactive retinoic acid in cells expressing disease-associated mutants of retinol dehydrogenase 12, J. Biol.	Tretinoin	52-65	retinol dehydrogenase 12	Homo sapiens	116-140
18396173-8	2008	Here, we investigated whether RDH12 can also protect cells against highly reactive medium-chain aldehydes.	Aldehydes	96-105	retinol dehydrogenase 12	Homo sapiens	30-35
18396173-10	2008	At high concentrations, nonanal inhibited the activity of RDH12 towards retinaldehyde, suggesting that nonanal was metabolized by RDH12.	Retinaldehyde	72-85	retinol dehydrogenase 12	Homo sapiens	58-63
18396173-10	2008	At high concentrations, nonanal inhibited the activity of RDH12 towards retinaldehyde, suggesting that nonanal was metabolized by RDH12.	Retinaldehyde	72-85	retinol dehydrogenase 12	Homo sapiens	130-135
18396173-12	2008	Thus, the results of this study showed that RDH12 is more effective in protection against retinaldehyde than against medium-chain aldehydes, and that medium-chain aldehydes, especially 4-hydroxynonenal, severely disrupt cellular retinoid homeostasis.	Retinaldehyde	90-103	retinol dehydrogenase 12	Homo sapiens	44-49
18396173-12	2008	Thus, the results of this study showed that RDH12 is more effective in protection against retinaldehyde than against medium-chain aldehydes, and that medium-chain aldehydes, especially 4-hydroxynonenal, severely disrupt cellular retinoid homeostasis.	Aldehydes	130-139	retinol dehydrogenase 12	Homo sapiens	44-49
18039331-6	2008	Similar to the microsomal RDHs, RDH11, RDH12 and RDH14, RDH13 exhibits a much lower Km value for NADPH than for NADH and has a greater catalytic efficiency in the reductive than in the oxidative direction.	NADP	97-102	retinol dehydrogenase 12	Homo sapiens	39-44
18039331-6	2008	Similar to the microsomal RDHs, RDH11, RDH12 and RDH14, RDH13 exhibits a much lower Km value for NADPH than for NADH and has a greater catalytic efficiency in the reductive than in the oxidative direction.	NAD	112-116	retinol dehydrogenase 12	Homo sapiens	39-44
15865448-8	2005	Together, the tissue distribution of RDH12 and its catalytic properties suggest that, in most tissues, RDH12 primarily contributes to the reduction of all-trans-retinaldehyde; however, at saturating concentrations of peroxidic aldehydes in the cells undergoing oxidative stress, for example, photoreceptors, RDH12 might also play a role in detoxification of lipid peroxidation products.	trans-retinaldehyde	155-174	retinol dehydrogenase 12	Homo sapiens	37-42
16965872-6	2006	RESULTS: Estimated 4-year BFS rates were superior for patients treated with BTC (BTC 72%, BTM 25%, RP 53%; p < 0.001).	btc	76-79	retinol dehydrogenase 12	Homo sapiens	99-104
15865448-0	2005	Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids.	Retinoids	103-112	retinol dehydrogenase 12	Homo sapiens	41-65
15865448-0	2005	Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids.	Retinoids	103-112	retinol dehydrogenase 12	Homo sapiens	67-72
15865448-0	2005	Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids.	Aldehydes	120-129	retinol dehydrogenase 12	Homo sapiens	41-65
15865448-0	2005	Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids.	Aldehydes	120-129	retinol dehydrogenase 12	Homo sapiens	67-72
15865448-0	2005	Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids.	Retinoids	279-288	retinol dehydrogenase 12	Homo sapiens	41-65
15865448-0	2005	Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids.	Retinoids	279-288	retinol dehydrogenase 12	Homo sapiens	67-72
15865448-3	2005	RDH12 exhibits approximately 2000-fold lower K(m) values for NADP(+) and NADPH than for NAD(+) and NADH and recognizes both retinoids and lipid peroxidation products (C(9) aldehydes) as substrates.	NADP	61-68	retinol dehydrogenase 12	Homo sapiens	0-5
15865448-3	2005	RDH12 exhibits approximately 2000-fold lower K(m) values for NADP(+) and NADPH than for NAD(+) and NADH and recognizes both retinoids and lipid peroxidation products (C(9) aldehydes) as substrates.	NADP	73-78	retinol dehydrogenase 12	Homo sapiens	0-5
15865448-3	2005	RDH12 exhibits approximately 2000-fold lower K(m) values for NADP(+) and NADPH than for NAD(+) and NADH and recognizes both retinoids and lipid peroxidation products (C(9) aldehydes) as substrates.	NAD	88-94	retinol dehydrogenase 12	Homo sapiens	0-5
15865448-3	2005	RDH12 exhibits approximately 2000-fold lower K(m) values for NADP(+) and NADPH than for NAD(+) and NADH and recognizes both retinoids and lipid peroxidation products (C(9) aldehydes) as substrates.	NAD	99-103	retinol dehydrogenase 12	Homo sapiens	0-5
15865448-3	2005	RDH12 exhibits approximately 2000-fold lower K(m) values for NADP(+) and NADPH than for NAD(+) and NADH and recognizes both retinoids and lipid peroxidation products (C(9) aldehydes) as substrates.	Aldehydes	172-181	retinol dehydrogenase 12	Homo sapiens	0-5
15865448-4	2005	The k(cat) values of RDH12 for retinaldehydes and C(9) aldehydes are similar, but the K(m) values are, in general, lower for retinoids.	Aldehydes	36-45	retinol dehydrogenase 12	Homo sapiens	21-26
15865448-4	2005	The k(cat) values of RDH12 for retinaldehydes and C(9) aldehydes are similar, but the K(m) values are, in general, lower for retinoids.	Retinoids	125-134	retinol dehydrogenase 12	Homo sapiens	21-26
15865448-6	2005	Analysis of RDH12 activity toward retinoids in the presence of cellular retinol-binding protein (CRBP) type I or cellular retinaldehyde-binding protein (CRALBP) suggests that RDH12 utilizes the unbound forms of all-trans- and 11-cis-retinoids.	Retinoids	34-43	retinol dehydrogenase 12	Homo sapiens	12-17
15865448-6	2005	Analysis of RDH12 activity toward retinoids in the presence of cellular retinol-binding protein (CRBP) type I or cellular retinaldehyde-binding protein (CRALBP) suggests that RDH12 utilizes the unbound forms of all-trans- and 11-cis-retinoids.	Retinoids	34-43	retinol dehydrogenase 12	Homo sapiens	175-180
15865448-6	2005	Analysis of RDH12 activity toward retinoids in the presence of cellular retinol-binding protein (CRBP) type I or cellular retinaldehyde-binding protein (CRALBP) suggests that RDH12 utilizes the unbound forms of all-trans- and 11-cis-retinoids.	Retinoids	233-242	retinol dehydrogenase 12	Homo sapiens	175-180
15865448-8	2005	Together, the tissue distribution of RDH12 and its catalytic properties suggest that, in most tissues, RDH12 primarily contributes to the reduction of all-trans-retinaldehyde; however, at saturating concentrations of peroxidic aldehydes in the cells undergoing oxidative stress, for example, photoreceptors, RDH12 might also play a role in detoxification of lipid peroxidation products.	trans-retinaldehyde	155-174	retinol dehydrogenase 12	Homo sapiens	103-108
15865448-8	2005	Together, the tissue distribution of RDH12 and its catalytic properties suggest that, in most tissues, RDH12 primarily contributes to the reduction of all-trans-retinaldehyde; however, at saturating concentrations of peroxidic aldehydes in the cells undergoing oxidative stress, for example, photoreceptors, RDH12 might also play a role in detoxification of lipid peroxidation products.	trans-retinaldehyde	155-174	retinol dehydrogenase 12	Homo sapiens	103-108
15865448-8	2005	Together, the tissue distribution of RDH12 and its catalytic properties suggest that, in most tissues, RDH12 primarily contributes to the reduction of all-trans-retinaldehyde; however, at saturating concentrations of peroxidic aldehydes in the cells undergoing oxidative stress, for example, photoreceptors, RDH12 might also play a role in detoxification of lipid peroxidation products.	Aldehydes	227-236	retinol dehydrogenase 12	Homo sapiens	37-42
15865448-8	2005	Together, the tissue distribution of RDH12 and its catalytic properties suggest that, in most tissues, RDH12 primarily contributes to the reduction of all-trans-retinaldehyde; however, at saturating concentrations of peroxidic aldehydes in the cells undergoing oxidative stress, for example, photoreceptors, RDH12 might also play a role in detoxification of lipid peroxidation products.	Aldehydes	227-236	retinol dehydrogenase 12	Homo sapiens	103-108
15865448-8	2005	Together, the tissue distribution of RDH12 and its catalytic properties suggest that, in most tissues, RDH12 primarily contributes to the reduction of all-trans-retinaldehyde; however, at saturating concentrations of peroxidic aldehydes in the cells undergoing oxidative stress, for example, photoreceptors, RDH12 might also play a role in detoxification of lipid peroxidation products.	Aldehydes	227-236	retinol dehydrogenase 12	Homo sapiens	103-108