PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7666002-6 1995 In healthy retinol target-tissues and in cultured HepG2 cells, RBP2 levels were significantly and variably present compared to RBP and RBP1. Vitamin A 11-18 retinol binding protein 2 Homo sapiens 63-67 7666002-8 1995 RBP2 may have an important physiological role in retinol transport and/or recycling. Vitamin A 49-56 retinol binding protein 2 Homo sapiens 0-4 7864119-3 1995 Compared with control cell lines, retinol uptake increased up to twofold by overexpression of CRBP II and up to 2.9-fold by coexpression of CRBP and CRBP II. Vitamin A 34-41 retinol binding protein 2 Homo sapiens 94-101 7864119-3 1995 Compared with control cell lines, retinol uptake increased up to twofold by overexpression of CRBP II and up to 2.9-fold by coexpression of CRBP and CRBP II. Vitamin A 34-41 retinol binding protein 2 Homo sapiens 149-156 7864119-8 1995 Thus these studies provide evidence that intestinal retinol uptake, retinyl ester synthesis, and retinyl ester secretion are correlated with levels of CRBP and CRBP II and that the effects of CRBP on retinyl ester secretion can be distinguished from those of CRBP II. Vitamin A 52-59 retinol binding protein 2 Homo sapiens 160-167 8228637-0 1993 Intestinal vitamin A metabolism: coordinate distribution of enzymes and CRBP(II). Vitamin A 11-20 retinol binding protein 2 Homo sapiens 72-80 8422392-3 1993 In contrast, CRBP-II binds all-trans-retinol or -retinal and contains a glutamine residue in the corresponding position, residue 109. Vitamin A 37-44 retinol binding protein 2 Homo sapiens 13-20 8487303-9 1993 Exogenously added retinol was found within the cavity of each holo-cellular retinol-binding protein II molecule. Vitamin A 18-25 retinol binding protein 2 Homo sapiens 67-102 8487303-12 1993 The overall conformation of the bound retinol was derived from the four different molecules of holo-cellular retinol-binding protein II present in the triclinic form. Vitamin A 38-45 retinol binding protein 2 Homo sapiens 100-135 8463337-5 1993 Retinol uptake and retinyl ester synthesis were increased up to 2-fold by coexpression of CRBP or over-expression of CRBP II. Vitamin A 0-7 retinol binding protein 2 Homo sapiens 117-124 8463337-11 1993 These studies indicate that CRBP and CRBP II levels are determinants of intracellular retinol accumulation and esterification, and they suggest that CRBP-bound retinol or a metabolite can regulate the expression of CRBP II in the mammalian intestine. Vitamin A 86-93 retinol binding protein 2 Homo sapiens 37-44 8463337-11 1993 These studies indicate that CRBP and CRBP II levels are determinants of intracellular retinol accumulation and esterification, and they suggest that CRBP-bound retinol or a metabolite can regulate the expression of CRBP II in the mammalian intestine. Vitamin A 86-93 retinol binding protein 2 Homo sapiens 215-222 8463337-11 1993 These studies indicate that CRBP and CRBP II levels are determinants of intracellular retinol accumulation and esterification, and they suggest that CRBP-bound retinol or a metabolite can regulate the expression of CRBP II in the mammalian intestine. Vitamin A 160-167 retinol binding protein 2 Homo sapiens 215-222 8504149-5 1993 The chicks fed vitamin A-depleted diet showed significantly reduced LRAT activity and CRBP(II) in duodenum as early as 3 days after the start of the vitamin A-depleted diet. Vitamin A 15-24 retinol binding protein 2 Homo sapiens 86-94 8504149-7 1993 These results suggest that duodenal LRAT activity and CRBP(II) are modulated by dietary vitamin A during the perinatal period. Vitamin A 88-97 retinol binding protein 2 Homo sapiens 54-62 8463337-1 1993 The mammalian small intestine contains two related cellular retinol-binding proteins, CRBP and CRBP II, which are thought to have distinct functions. Vitamin A 60-67 retinol binding protein 2 Homo sapiens 95-102 1322170-2 1992 Retinol in cells is bound by either cellular retinol binding protein (CRBP), present in most tissues including liver, or cellular retinol binding protein type II [CRBP(II)], present in the absorptive cell of the small intestine. Vitamin A 0-7 retinol binding protein 2 Homo sapiens 121-161 1322170-4 1992 Esterification of free retinol by both liver and intestinal LRAT resulted in Km values (0.63 and 0.44 microM, respectively) similar to those obtained for esterification of retinol-CRBP (0.20 and 0.78 microM, respectively) and esterification of retinol-CRBP(II) (0.24 and 0.32 microM, respectively). Vitamin A 23-30 retinol binding protein 2 Homo sapiens 252-260 1322170-7 1992 Apo-CRBP(II), in contrast, was a poor competitor for esterification of retinol bound to CRBP(II). Vitamin A 71-78 retinol binding protein 2 Homo sapiens 4-12 1322170-7 1992 Apo-CRBP(II), in contrast, was a poor competitor for esterification of retinol bound to CRBP(II). Vitamin A 71-78 retinol binding protein 2 Homo sapiens 88-96 1542003-5 1992 The ability of pure hCRBP(II) to bind all-trans-retinol, retinal and retinoic acid was examined by competitive binding assay and compared with the binding specificity of pure human cellular retinol-binding protein (hCRBP). Vitamin A 38-55 retinol binding protein 2 Homo sapiens 20-29 1542003-7 1992 Retinal competed with retinol for binding to hCRBP(II) but not to hCRBP, consistent with what was observed for the homologous proteins of rats. Vitamin A 22-29 retinol binding protein 2 Homo sapiens 45-54 1542003-12 1992 These results provide tools for further investigation of the role of hCRBP(II) and suggest that previous results from rats, in this important aspect, are relevant to human metabolism of vitamin A. Vitamin A 186-195 retinol binding protein 2 Homo sapiens 69-78 1651173-2 1991 We provide evidence that expression of the gene for cellular retinol-binding protein type II (CRBPII), a key protein in the intestinal absorption of vitamin A, is dramatically up-regulated by retinoic acid in the presence of RXR but not RAR. Vitamin A 149-158 retinol binding protein 2 Homo sapiens 52-92 1651173-2 1991 We provide evidence that expression of the gene for cellular retinol-binding protein type II (CRBPII), a key protein in the intestinal absorption of vitamin A, is dramatically up-regulated by retinoic acid in the presence of RXR but not RAR. Vitamin A 149-158 retinol binding protein 2 Homo sapiens 94-100 3818619-5 1987 The apparent Km for retinol-CRBP(II) in the reaction with endogenous acyl donor was 2.4 X 10(-7) M. Retinol presented as a complex with CRBP(II) was esterified more than retinol presented as a complex with cellular retinol-binding protein or retinol-binding protein, two other proteins known to bind retinol in vivo, but about the same as retinol presented bound to bovine serum albumin or beta-lactoglobulin. Vitamin A 20-27 retinol binding protein 2 Homo sapiens 28-36 2271700-2 1990 Caco-2 cells contained cellular retinol-binding protein II, a protein which is abundant in human villus-associated enterocytes and may play an important role in the absorption of vitamin A. Vitamin A 179-188 retinol binding protein 2 Homo sapiens 23-58 34836244-5 2021 CRBP2 bound retinol is then converted into retinyl esters (REs) by the enzyme lecithin retinol acyltransferase (LRAT) in the endoplasmic reticulum, which is then packaged into chylomicrons and sent into the bloodstream for storage in hepatic stellate cells in the liver or for functional use in peripheral tissues such as the retina. Vitamin A 12-19 retinol binding protein 2 Homo sapiens 0-5 3579304-5 1987 On the other hand, cellular retinol-binding protein type II (CRBP(II], whose amino acid sequence shows a considerable similarity to CRBP, did compete for the transfer of retinol from the R-CRBP complex, but less effectively than CRBP. Vitamin A 28-35 retinol binding protein 2 Homo sapiens 61-69 3611082-1 1987 Cellular retinol-binding protein (CRBP) and cellular retinol-binding protein, type ii (CRBP(II] are cytoplasmic proteins that bind trans-retinol as an endogenous ligand. Vitamin A 131-144 retinol binding protein 2 Homo sapiens 44-85 3611082-1 1987 Cellular retinol-binding protein (CRBP) and cellular retinol-binding protein, type ii (CRBP(II] are cytoplasmic proteins that bind trans-retinol as an endogenous ligand. Vitamin A 131-144 retinol binding protein 2 Homo sapiens 87-94 3611082-3 1987 Employing fluorescence, absorbance, and competition studies, the ability of pure preparations of CRBP(II) and CRBP to bind various members of the vitamin A family has been examined. Vitamin A 146-155 retinol binding protein 2 Homo sapiens 97-105 3611082-9 1987 It appears that CRBP(II) and CRBP bind trans-retinol, 13-cis-retinol, and 3-dehydroretinol in a planar configuration. Vitamin A 39-52 retinol binding protein 2 Homo sapiens 16-24 3818619-5 1987 The apparent Km for retinol-CRBP(II) in the reaction with endogenous acyl donor was 2.4 X 10(-7) M. Retinol presented as a complex with CRBP(II) was esterified more than retinol presented as a complex with cellular retinol-binding protein or retinol-binding protein, two other proteins known to bind retinol in vivo, but about the same as retinol presented bound to bovine serum albumin or beta-lactoglobulin. Vitamin A 170-177 retinol binding protein 2 Homo sapiens 28-36 3818619-5 1987 The apparent Km for retinol-CRBP(II) in the reaction with endogenous acyl donor was 2.4 X 10(-7) M. Retinol presented as a complex with CRBP(II) was esterified more than retinol presented as a complex with cellular retinol-binding protein or retinol-binding protein, two other proteins known to bind retinol in vivo, but about the same as retinol presented bound to bovine serum albumin or beta-lactoglobulin. Vitamin A 170-177 retinol binding protein 2 Homo sapiens 28-36 3818619-5 1987 The apparent Km for retinol-CRBP(II) in the reaction with endogenous acyl donor was 2.4 X 10(-7) M. Retinol presented as a complex with CRBP(II) was esterified more than retinol presented as a complex with cellular retinol-binding protein or retinol-binding protein, two other proteins known to bind retinol in vivo, but about the same as retinol presented bound to bovine serum albumin or beta-lactoglobulin. Vitamin A 100-107 retinol binding protein 2 Homo sapiens 28-36 3818619-5 1987 The apparent Km for retinol-CRBP(II) in the reaction with endogenous acyl donor was 2.4 X 10(-7) M. Retinol presented as a complex with CRBP(II) was esterified more than retinol presented as a complex with cellular retinol-binding protein or retinol-binding protein, two other proteins known to bind retinol in vivo, but about the same as retinol presented bound to bovine serum albumin or beta-lactoglobulin. Vitamin A 170-177 retinol binding protein 2 Homo sapiens 28-36 3818619-5 1987 The apparent Km for retinol-CRBP(II) in the reaction with endogenous acyl donor was 2.4 X 10(-7) M. Retinol presented as a complex with CRBP(II) was esterified more than retinol presented as a complex with cellular retinol-binding protein or retinol-binding protein, two other proteins known to bind retinol in vivo, but about the same as retinol presented bound to bovine serum albumin or beta-lactoglobulin. Vitamin A 170-177 retinol binding protein 2 Homo sapiens 28-36 33631211-3 2021 To better understand the physiological role of CRBP2, we determined its protein-lipid interactome using a fluorescence-based retinol replacement assay adapted for a high-throughput screening format. Vitamin A 125-132 retinol binding protein 2 Homo sapiens 47-52 29567208-6 2018 In CRBP 2 a different distribution of the surface residues of the "cap region" allows retinol to access the binding cavity by sinking in a hydrophobic matrix between the two alpha-helices. Vitamin A 86-93 retinol binding protein 2 Homo sapiens 3-9 27830500-7 2016 Metabolic and functional defects manifested in knockouts of CRBP1, CRBP2 and CRBP3, however, illustrate their essentiality to health, and in the case of CRBP2, to survival during limited dietary vitamin A. Vitamin A 195-204 retinol binding protein 2 Homo sapiens 153-158 27524203-1 2016 Human Cellular Retinol Binding Protein II (hCRBPII), a member of the intracellular lipid-binding protein family, is a monomeric protein responsible for the intracellular transport of retinol and retinal. Vitamin A 183-190 retinol binding protein 2 Homo sapiens 6-41 27524203-1 2016 Human Cellular Retinol Binding Protein II (hCRBPII), a member of the intracellular lipid-binding protein family, is a monomeric protein responsible for the intracellular transport of retinol and retinal. Vitamin A 183-190 retinol binding protein 2 Homo sapiens 43-50 22815070-6 2012 We show here that STRA6 can couple strongly to both CRBP-I and CRBP-II for retinol efflux to apo-RBP. Vitamin A 75-82 retinol binding protein 2 Homo sapiens 63-70 25478840-3 2014 In addition, the retinol-bound human CRBPII (hCRBPII) structure shows partial occupancy of a noncanonical conformation of retinol in the binding pocket. Vitamin A 17-24 retinol binding protein 2 Homo sapiens 37-43 25478840-3 2014 In addition, the retinol-bound human CRBPII (hCRBPII) structure shows partial occupancy of a noncanonical conformation of retinol in the binding pocket. Vitamin A 17-24 retinol binding protein 2 Homo sapiens 45-52 25478840-3 2014 In addition, the retinol-bound human CRBPII (hCRBPII) structure shows partial occupancy of a noncanonical conformation of retinol in the binding pocket. Vitamin A 122-129 retinol binding protein 2 Homo sapiens 37-43 25478840-3 2014 In addition, the retinol-bound human CRBPII (hCRBPII) structure shows partial occupancy of a noncanonical conformation of retinol in the binding pocket. Vitamin A 122-129 retinol binding protein 2 Homo sapiens 45-52 25478840-4 2014 Here, the structure of retinal-bound hCRBPII and the structure of retinol-bound hCRBPII with retinol fully occupying the binding pocket are reported. Vitamin A 66-73 retinol binding protein 2 Homo sapiens 80-87 25478840-4 2014 Here, the structure of retinal-bound hCRBPII and the structure of retinol-bound hCRBPII with retinol fully occupying the binding pocket are reported. Vitamin A 93-100 retinol binding protein 2 Homo sapiens 80-87 14704332-2 2004 Lecithin:retinol acyltransferase (LRAT), a microsomal enzyme present in liver and several other retinol-metabolizing tissues, esterifies retinol that is associated with a cellular retinol-binding protein, CRBP or CRBP-II. Vitamin A 9-16 retinol binding protein 2 Homo sapiens 213-220 19965581-4 2010 The remarkable difference in intrinsic stability between the two homologs appears to modulate their binding properties: the stronger retinol binder CRBP-I displays a reduced flexibility of the backbone structure with respect to CRBP-II. Vitamin A 133-140 retinol binding protein 2 Homo sapiens 228-235 19147806-1 2009 Cellular retinol-binding protein type II (CRBPII) is abundantly expressed in the small intestinal enterocytes of many vertebrates and plays important physiological roles in intestinal absorption, transport, and metabolism of vitamin A. Vitamin A 225-234 retinol binding protein 2 Homo sapiens 0-40 19147806-1 2009 Cellular retinol-binding protein type II (CRBPII) is abundantly expressed in the small intestinal enterocytes of many vertebrates and plays important physiological roles in intestinal absorption, transport, and metabolism of vitamin A. Vitamin A 225-234 retinol binding protein 2 Homo sapiens 42-48 19147806-9 2009 These results suggest that HNF-4alpha is an important transcriptional factor that regulates human CRBPII gene expression and provide the possibility for a novel function of HNF-4alpha in the regulation of human intestinal vitamin A absorption and metabolism. Vitamin A 222-231 retinol binding protein 2 Homo sapiens 98-104 19965581-1 2010 The main retinol carriers in the cytosol are the cellular retinol-binding proteins types I and II (CRBP-I and CRBP-II), which exhibit distinct tissue distributions. Vitamin A 9-16 retinol binding protein 2 Homo sapiens 110-117 19965581-1 2010 The main retinol carriers in the cytosol are the cellular retinol-binding proteins types I and II (CRBP-I and CRBP-II), which exhibit distinct tissue distributions. Vitamin A 58-65 retinol binding protein 2 Homo sapiens 110-117 14704332-2 2004 Lecithin:retinol acyltransferase (LRAT), a microsomal enzyme present in liver and several other retinol-metabolizing tissues, esterifies retinol that is associated with a cellular retinol-binding protein, CRBP or CRBP-II. Vitamin A 96-103 retinol binding protein 2 Homo sapiens 213-220 14704332-2 2004 Lecithin:retinol acyltransferase (LRAT), a microsomal enzyme present in liver and several other retinol-metabolizing tissues, esterifies retinol that is associated with a cellular retinol-binding protein, CRBP or CRBP-II. Vitamin A 96-103 retinol binding protein 2 Homo sapiens 213-220 11274389-8 2001 CRBP III and all-trans-retinol form a complex (K(d) approximately 60 nM), the absorption spectrum of which is characterized by the peculiar fine structure typical of the spectra of holo-CRBP I and II. Vitamin A 13-30 retinol binding protein 2 Homo sapiens 186-199 9037178-1 1997 The cellular retinol binding proteins, CRBP and CRBP II, are implicated in the cellular uptake of retinol and intracellular trafficking of retinol between sites of metabolic processing. Vitamin A 13-20 retinol binding protein 2 Homo sapiens 48-55 11133659-3 2001 Three proteins involved in 1) serum transport of retinol (retinol binding protein [RBP]), 2) cellular transport and metabolism of retinol (cellular RBP [CRBP] I), and 3) retinoic acid (cellular retinoic acid binding protein [CRABP] I), respectively, have been located by immunohistochemistry during gestation in the porcine placenta. Vitamin A 49-56 retinol binding protein 2 Homo sapiens 83-91 11133659-3 2001 Three proteins involved in 1) serum transport of retinol (retinol binding protein [RBP]), 2) cellular transport and metabolism of retinol (cellular RBP [CRBP] I), and 3) retinoic acid (cellular retinoic acid binding protein [CRABP] I), respectively, have been located by immunohistochemistry during gestation in the porcine placenta. Vitamin A 58-65 retinol binding protein 2 Homo sapiens 83-91 10092641-1 1999 Cellular retinol-binding proteins types I and II (CRBP-I and CRBP-II) are known to differentially facilitate retinoid metabolism by several membrane-associated enzymes. Vitamin A 9-16 retinol binding protein 2 Homo sapiens 61-68 9037178-1 1997 The cellular retinol binding proteins, CRBP and CRBP II, are implicated in the cellular uptake of retinol and intracellular trafficking of retinol between sites of metabolic processing. Vitamin A 98-105 retinol binding protein 2 Homo sapiens 48-55 9037178-1 1997 The cellular retinol binding proteins, CRBP and CRBP II, are implicated in the cellular uptake of retinol and intracellular trafficking of retinol between sites of metabolic processing. Vitamin A 98-105 retinol binding protein 2 Homo sapiens 48-55 9037178-2 1997 19F-NMR studies of retinol transfer between CRBP and CRBP II and phospholipid vesicles, using either fluorine-labeled ligand or protein, demonstrated that there was significantly more transfer of retinol from CRBP II to lipid vesicles than from CRBP. Vitamin A 19-26 retinol binding protein 2 Homo sapiens 53-60 9037178-2 1997 19F-NMR studies of retinol transfer between CRBP and CRBP II and phospholipid vesicles, using either fluorine-labeled ligand or protein, demonstrated that there was significantly more transfer of retinol from CRBP II to lipid vesicles than from CRBP. Vitamin A 196-203 retinol binding protein 2 Homo sapiens 53-60 9037178-2 1997 19F-NMR studies of retinol transfer between CRBP and CRBP II and phospholipid vesicles, using either fluorine-labeled ligand or protein, demonstrated that there was significantly more transfer of retinol from CRBP II to lipid vesicles than from CRBP. Vitamin A 196-203 retinol binding protein 2 Homo sapiens 209-216 9040537-1 1997 Cellular retinol binding protein II (CRBPII) is an abundant small intestinal protein that facilitates vitamin A trafficking and metabolism. Vitamin A 102-111 retinol binding protein 2 Homo sapiens 0-35 9040537-1 1997 Cellular retinol binding protein II (CRBPII) is an abundant small intestinal protein that facilitates vitamin A trafficking and metabolism. Vitamin A 102-111 retinol binding protein 2 Homo sapiens 37-43 9040537-2 1997 The magnitude of retinol uptake and metabolism correlate to CRBPII levels in the human intestinal Caco-2 cell line. Vitamin A 17-24 retinol binding protein 2 Homo sapiens 60-66 8530418-2 1995 When binding to natural HREs, TR2 orphan receptor remains flexible with higher binding affinities to (a) cellular retinol-binding protein II promoter region (CRBPIIp) (DR1), SV40 +55 region (DR2), and retinoic acid response element beta (RARE beta) (DR5) than to (b) NGFI-B response element (NBRE) and also to (c) the palindromic thyroid hormone response element (TREpal). Vitamin A 114-121 retinol binding protein 2 Homo sapiens 158-165 8841765-3 1996 The retinol-binding proteins CRBP I and CRBP II appear to play an essential role in retinyl ester hydrolysis and formation and in retinoic acid formation. Vitamin A 4-11 retinol binding protein 2 Homo sapiens 40-47 8964570-5 1996 There is strong evidence that RBP2 is formed in vitamin A target tissues, and that after its release into blood circulation, it is cleared by the kidney in healthy people but accumulates in the serum of CRF patients. Vitamin A 48-57 retinol binding protein 2 Homo sapiens 30-34