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1 and the cholesterol efflux genes (eg, ABCG5, ABCG8).
2 ansporter G5 (ABCG5) and ABC transporter G8 (ABCG8).
3 LXR-regulated transcripts, CYP7A1, ABCG5, or ABCG8.
4 r expression of the sterol metabolizing gene ABCG8.
5 s or compound heterozygous variants in ABCG5/ABCG8.
6 endent post-translational N-glycosylation of ABCG8.
7 tors of disease-associated transporter ABCG5/ABCG8.
8  activity (3.2-fold, P = 0.003) only for the ABCG8-19H variant, which was also superior in nested log
9  decreased the level of high mannose form of ABCG8, a protein that heterodimerizes with ABCG5 to cont
10 ng ABCC3, ABCB6, ABCD1, ABCG1, ABCG4, ABCG5, ABCG8, ABCE1, ABCF1, ABCF2, and ABCF3, were expressed at
11  cholesterol metabolism related genes Abcg5, Abcg8, Abcg11, Cyp7a1 and Cyp8b1; and (6) induced higher
12 (1)), suggesting that expression of ABCG5 or ABCG8 alone yielded nonfunctional transporters.
13 bsorption is associated with risk alleles in ABCG8 and ABO and with CVD.
14                                  Variants in ABCG8 and ABO have been associated with circulating plan
15 nts a cardiovascular risk factor and to link ABCG8 and ABO variants to cardiovascular disease (CVD).
16 s may therefore mediate the relationships of ABCG8 and ABO variants with CVD.
17 ions of 6 single nucleotide polymorphisms in ABCG8 and ABO with CR in the LURIC (LUdwisghafen RIsk an
18 ic patients with a defect in either ABCG5 or ABCG8 and in either Abcg5/g8 double- or single-knockout
19 e (ABC) transporter family (six mutations in ABCG8 and one in ABCG5) in nine patients with sitosterol
20 -density lipoprotein (HDL) into bile in male Abcg8(-/-) and wild-type mice.
21 wnregulation of hepatic expression of ABCG5, ABCG8, and ABCB11 biliary transporters.
22 hepatic mRNA and protein levels of ABCG5 and ABCG8, and in hepatic mRNA levels of Niemann-Pick C1-Lik
23         Both gallstone disease and p.D19H of ABCG8 are associated with diminished cholesterol absorpt
24                                    ABCG5 and ABCG8 are both half-size transporters that have been pro
25                                    ABCG5 and ABCG8 are half-size ABC transporters that function as he
26           These data indicate that ABCG5 and ABCG8 are required for efficient secretion of cholestero
27                               Thus Abcg5 and Abcg8 are required for LXR agonist-associated changes in
28 entified the hepatic cholesterol transporter ABCG8 as a locus associated with risk for gallstone dise
29 llstone disease is associated with p.D19H of ABCG8 as well as alterations of cholesterol and bile aci
30 te [ABC] transporters subfamily G member 5), Abcg8 (ATP-binding cassette [ABC] transporters subfamily
31 g5 (ATP-binding cassette transporter G5) and Abcg8, but not Npc1l1 (Niemann-Pick C1 like 1), were sig
32 (canalicular) membrane when coexpressed with ABCG8, but not when expressed alone.
33 ia is caused by mutations in either ABCG5 or ABCG8, but simultaneous mutations of these genes have ne
34                 Mutations in either ABCG5 or ABCG8 cause sitosterolemia, a recessive disorder charact
35 s in either ATP-binding cassette (ABC) G5 or ABCG8 cause sitosterolemia, an autosomal recessive disor
36  The mature, glycosylated forms of ABCG5 and ABCG8 coimmunoprecipitated, consistent with heterodimeri
37                    The sterolin locus (ABCG5/ABCG8) confers susceptibility for cholesterol gallstone
38 ariants: ABCG5-R50C (P = 4.94 x 10(-9) ) and ABCG8-D19H (P = 1.74 x 10(-10) ) in high pairwise linkag
39         Sitosterolemia induced in Abcg5- and Abcg8-deficient mice fed a high plant sterol diet result
40  APOA5, LCAT) and two associated with LDL-C (ABCG8, DHODH).
41 n ATP-binding cassette subfamily G member 8 (ABCG8) did not associate with LDL cholesterol lowering.
42  Mutations in ABCG5 (encoding sterolin-1) or ABCG8 (encoding sterolin-2) cause this disease.
43 Mutations in two tandem ABC genes, ABCG5 and ABCG8, encoding sterolin-1 and -2, respectively, are now
44 , whereas reductions in Gata4 diminish Abcg5/Abcg8 expression and biliary cholesterol excretion.
45 anied by elevated jejunal ABCB1a, ABCG5, and ABCG8 expression, mediated by augmented levels of Liver
46  importance of the 19H variant on intestinal ABCG8 feature remains to be clarified.
47                                    ABCG5 and ABCG8 form a complex (G5G8) that opposes the absorption
48                                    ABCG5 and ABCG8 form a functional complex that limits dietary phyt
49                                    ABCG5 and ABCG8 form heterodimers that limit absorption of dietary
50                 Mice expressing no ABCG5 and ABCG8 (G5G8(-/-) mice) and their littermate controls wer
51 n of plant sterols in mice lacking ABCG5 and ABCG8 (G5G8-/- mice) profoundly perturbs cholesterol hom
52 g cassette (ABC) transporters ABCG5 (G5) and ABCG8 (G8) and is stimulated by cholesterol and by the n
53                               ABGG5 (G5) and ABCG8 (G8) are ABC half-transporters that dimerize withi
54                               ABCG5 (G5) and ABCG8 (G8) are ATP-binding cassette (ABC) transporters t
55                               ABCG5 (G5) and ABCG8 (G8) are ATP-binding cassette half-transporters th
56                   Mutations in ABCG5 (G5) or ABCG8 (G8) cause sitosterolemia, an autosomal recessive
57 binding cassette transporters ABCG5 (G5) and ABCG8 (G8) form a heterodimer that transports cholestero
58 ng cassette half-transporters ABCG5 (G5) and ABCG8 (G8) promote secretion of neutral sterols into bil
59                              Deletion of the Abcg8 gene alone significantly increases the mass of int
60  rs41360247, rs6576629, and rs4953023 of the ABCG8 gene and the minor allele of rs657152 of the ABO g
61         Polymorphism in the promoter for the ABCG8 gene has been linked to variations in response to
62       Here we demonstrate that the ABCG5 and ABCG8 genes are direct targets of the oxysterol receptor
63 ve expressed the recombinant human ABCG5 and ABCG8 genes in the yeast Pichia pastoris and purified th
64 ce doubly transgenic for the human ABCG5 and ABCG8 genes rescued platelet counts and volumes.
65 s, a P1 clone containing the human ABCG5 and ABCG8 genes was used to generate transgenic mice.
66 s or compound heterozygous variant for ABCG5/ABCG8 genes, confirming the genetic diagnosis of sitoste
67               This haplotype spans the ABCG5/ABCG8 genes, is carried by 1.8% of the islanders, and re
68 assette subfamily G members 5 or 8 (ABCG5 or ABCG8) genes.
69                           Purified ABCG5 and ABCG8 had very low ATPase activities (<5 nmol min(-)(1)
70 e that encodes the hepatobiliary transporter ABCG8 has been identified as a risk factor for gallstone
71 sive, but no longer; two intronic regions in ABCG8 have now been identified.
72 inding cassette (ABC) transporters ABCG5 and ABCG8 have recently been shown to cause the autosomal re
73 nding cassette (ABC) transporters, ABCG5 and ABCG8, have been proposed to limit sterol absorption and
74 o upregulates liver and intestinal ABCG5 and ABCG8, helping to promote biliary and fecal excretion of
75                                    The ABCG5/ABCG8 heterodimer (G5G8) mediates excretion of neutral s
76           The ABCG1 homodimer (G1) and ABCG5-ABCG8 heterodimer (G5G8), two members of the adenosine t
77  recombinant, epitope-tagged mouse ABCG5 and ABCG8 in cultured cells.
78 afficking of sterols, we disrupted Abcg5 and Abcg8 in mice (G5G8(-/-)).
79                     Overexpressing ABCG5 and ABCG8 in mice attenuates diet-induced atherosclerosis in
80 inding cassette (ABC) transporters ABCG5 and ABCG8 in patients with sitosterolemia suggests that thes
81 sults establish a central role for ABCG5 and ABCG8 in promoting cholesterol excretion in vivo.
82 NPC1L1 and increased expression of ABCG5 and ABCG8 in small intestine.
83 an disease Sitosterolemia, the role of ABCG5/ABCG8 in sterol trafficking and how newer data implicate
84 roles of hepatic versus intestinal ABCG5 and ABCG8 in sterol transport have not yet been investigated
85 epatic messenger RNA expression of Abcg5 and Abcg8 in strain PERA/Ei correlates positively with highe
86 he canalicular cholesterol transporter ABCG5/ABCG8 in the genetic susceptibility and pathogenesis of
87 sgenic mice that overexpress human ABCG5 and ABCG8 in the liver but not intestine (liver G5/G8-Tg) in
88 no effect on the T1317 induction of ABCG5 or ABCG8 in the rat hepatoma cell line, FTO-2B.
89          To elucidate the roles of ABCG5 and ABCG8 in the trafficking of sterols, we disrupted Abcg5
90 polypeptide (NTCP), OATP1, OATP2, ABCG5, and ABCG8) in the liver.
91   ATP-binding cassette subfamily G member 8 (ABCG8) is a protein that regulates cholesterol efflux fr
92  protein, termed "sterolin-2" and encoded by ABCG8, is mutated in the remaining pedigrees.
93 inding cassette (ABC) transporters Abcg5 and Abcg8, is required for both the increase in sterol excre
94 transgene specifically in the intestine, and ABCG8-knockout mice.
95 inding cassette (ABC) transporters ABCG5 and ABCG8 lead to sitosterolemia, a disorder characterized b
96 g cassette (ABC) half-transporters, ABCG5 or ABCG8, lead to reduced secretion of sterols into bile, i
97 -binding cassette transporter 1 (ABCA1), and ABCG8 levels on the membrane, thus significantly reducin
98               The ABC transporters ABCG5 and ABCG8 limit absorption and promote excretion of dietary
99 for 2 single-nucleotide polymorphisms at the ABCG8 locus: rs11887534 (OR, 1.69; 95% confidence interv
100 ariants associated with LDL cholesterol near ABCG8, MAFB, HNF1A and TIMD4; with HDL cholesterol near
101 used by a genetic defect of sterolins (ABCG5/ABCG8) mapped to the STSL locus.
102 olved on pathogenesis, and the role of ABCG5/ABCG8 may extend into other metabolic processes by alter
103 cholesterol biosynthesis and promoting ABCG5/ABCG8-mediated cholesterol excretion.
104         We found that ABCG5(-/-)/G8(-/-) and ABCG8 (-/-) mice displayed the same biliary and gallston
105 male wild-type (WT), ABCG5(-/-)/G8(-/-), and ABCG8 (-/-) mice fed a lithogenic diet or varying amount
106 lstones in WT, but not ABCG5(-/-)/G8(-/-) or ABCG8 (-/-), mice.
107 etected in WT, but not ABCG5(-/-)/G8(-/-) or ABCG8 (-/-), mice.
108 40% and approximately 500%, respectively, in Abcg8(-/-) mice in the setting of constant intraduodenal
109 tion still promoted cholesterol excretion in Abcg8(-/-) mice.
110  [(14)C]cholesterol were detected in bile of Abcg8(-/-) mice.
111 on of ABCA1 mRNA, and no change in ABCG5 and ABCG8 mRNA expression.
112 f the islanders are carriers of a frameshift ABCG8 mutation increasing PPS levels in carriers by 50%.
113                                     ABCG5 or ABCG8 mutations can cause sitosterolemia, in which patie
114            These data suggest that ABCG5 and ABCG8 normally cooperate to limit intestinal absorption
115 Immunoelectron microscopy revealed ABCG5 and ABCG8 on the plasma membrane of these cells.
116 anwhile, HRD1 increased the non-glycosylated ABCG8 regardless of its E3 activity, thereby suppressing
117                 Mutations in either ABCG5 or ABCG8 result in an identical clinical phenotype, suggest
118 e biliary cholesterol transporters Abcg5 and Abcg8, resulting in an increase in biliary cholesterol s
119 GWAS) and meta-analyses of GWAS revealed the ABCG8 rs11887534 variant as the most common genetic dete
120 ese data suggest that heterozygosity for the ABCG8 S107X mutation does not influence the action of di
121 nthesis) to daily PS supplementation in HET (ABCG8 S107X mutation) compared with a healthy control co
122 trate that increased expression of ABCG5 and ABCG8 selectively drives biliary neutral sterol secretio
123 phate binding cassette subfamily G member 8 [ABCG8], sulfotransferase family 2A member 1, cytochrome
124 RA/Ei), colocalizes with the genes Abcg5 and Abcg8 that encode the canalicular cholesterol transporte
125 -binding cassette transporter genes ABCG5 or ABCG8 that result in accumulation of xenosterols in the
126                           To explore whether ABCG8, the sterol efflux (hemi-)transporter, plays a maj
127                    The addition of ABCG5 and ABCG8 to the growing list of LXR target genes further su
128 balance or allelic splicing of the ABCG5 and ABCG8 transcripts in human liver limited the search to c
129 e confirmed a functional defect in the ABCG5/ABCG8 transport system.
130 ing cassette, subfamily G (WHITE), member 8 (ABCG8), two half-transporters that act as a heterodimeri
131                               Both ABCG5 and ABCG8 underwent N-linked glycosylation.
132 ccelerated the degradation of both ABCG5 and ABCG8 via E3 activity-dependent manner.
133 y regulating the expression of Mtp and Abcg5/Abcg8 via Shp and Gata4.
134 To determine the site of action of ABCG5 and ABCG8, we expressed recombinant, epitope-tagged mouse AB
135                               When ABCG5 and ABCG8 were coexpressed, the attached sugars were Endo H-
136      The Endo H-sensitive forms of ABCG5 and ABCG8 were confined to the endoplasmic reticulum (ER), w
137 we quantified the effect of rs4299376 (ABCG5/ABCG8), which affects the intestinal cholesterol absorpt
138 nown but involves the genes ABC1, ABCG5, and ABCG8, which are members of the ATP-binding cassette pro

 
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