PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33395105-2 2021 RECENT FINDINGS: Defects in ABCG5/G8 result in the accumulation of xenosterols. xenosterols 67-78 ATP binding cassette subfamily G member 5 Homo sapiens 28-33 33807969-1 2021 Sitosterolemia is a lipid disorder characterized by the accumulation of dietary xenosterols in plasma and tissues caused by mutations in either ABCG5 or ABCG8. xenosterols 80-91 ATP binding cassette subfamily G member 5 Homo sapiens 144-149 33807969-2 2021 ABCG5 ABCG8 encodes a pair of ABC half transporters that form a heterodimer (G5G8), which then traffics to the surface of hepatocytes and enterocytes and promotes the secretion of cholesterol and xenosterols into the bile and the intestinal lumen. xenosterols 196-207 ATP binding cassette subfamily G member 5 Homo sapiens 0-5 23926302-1 2013 Sitosterolemia is a rare, autosomal recessive disease caused by mutations in the adenosine triphosphate-binding cassette transporter genes ABCG5 or ABCG8 that result in accumulation of xenosterols in the body. xenosterols 185-196 ATP binding cassette subfamily G member 5 Homo sapiens 139-144 25942705-4 2015 The bulk of this exclusion takes place in the intestine and the heterodimeric transporters ABCG5 and ABCG8 are key to keeping these xenosterols out of our bodies. xenosterols 132-143 ATP binding cassette subfamily G member 5 Homo sapiens 91-96 33141631-4 2021 Biochemical and structural information on ABC sterol transporters is beginning to emerge, with published structures of ABCA1 and ABCG5/G8; these two proteins function in the reverse cholesterol transport pathway and mediate the efflux of cholesterol and xenosterols to high-density lipoprotein and bile-salt micelles, respectively. xenosterols 254-265 ATP binding cassette subfamily G member 5 Homo sapiens 129-134 29728459-0 2018 ABCG5 and ABCG8: more than a defense against xenosterols. xenosterols 45-56 ATP binding cassette subfamily G member 5 Homo sapiens 0-5 29055934-1 2017 Sitosterolemia is an autosomal recessive metabolic disease caused by mutations in ABCG5 or ABCG8 genes which encode for the (ATP)-binding cassette (ABC) transporters that are responsible for the trafficking of xenosterols. xenosterols 210-221 ATP binding cassette subfamily G member 5 Homo sapiens 82-87 29928317-5 2013 Two proteins, ABCG5 and ABCG8, constitute a heterodimeric transporter that facilitates the extrusion of sterols from the cell into the biliary lumen, with a preference for xenosterols. xenosterols 172-183 ATP binding cassette subfamily G member 5 Homo sapiens 14-19 23180829-6 2013 These studies show that xenosterols may have a significant biological impact on normal mammalian physiology and that the Abcg5 or Abcg8 knockout mouse model may prove useful in investigating the role of xenosterols on mammalian physiology. xenosterols 203-214 ATP binding cassette subfamily G member 5 Homo sapiens 121-126