PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16877258-3 2006 The aim of this review article is to address new aspects of ABCG2 related to redox biology, namely the posttranslational modification (intra- and intermolecular disulfide bond formation) of ABCG2 protein and the transport of porphyrin and chlorophyll metabolites, as well as the high-speed screening and QSAR analysis method to evaluate ABCG2-drug interactions. Disulfides 161-170 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 60-65 25036722-8 2014 Thus, the active form of BCRP, at least a dimer or a larger oligomer is maintained by intramolecular disulfide bridge that involves Cys(603) residues. Disulfides 101-110 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 25-29 19909340-1 2009 The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596. Disulfides 147-156 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 50-55 19909340-1 2009 The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596. Disulfides 147-156 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 57-61 19909340-1 2009 The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596. Disulfides 147-156 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 62-65 19909340-1 2009 The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596. Disulfides 147-156 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 66-70 19909340-2 2009 We have recently reported that the intramolecular disulfide bond is a critical checkpoint for determining the degradation fates of ABCG2. Disulfides 50-59 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 131-136 19111842-1 2009 Human ATP-binding cassette (ABC) transporter ABCG2 (BCRP/MXR/ABCP) is a plasma membrane protein carrying intra- and inter-molecular disulfide bonds and an N-linked glycan. Disulfides 132-141 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 45-50 19111842-1 2009 Human ATP-binding cassette (ABC) transporter ABCG2 (BCRP/MXR/ABCP) is a plasma membrane protein carrying intra- and inter-molecular disulfide bonds and an N-linked glycan. Disulfides 132-141 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 52-56 19111842-1 2009 Human ATP-binding cassette (ABC) transporter ABCG2 (BCRP/MXR/ABCP) is a plasma membrane protein carrying intra- and inter-molecular disulfide bonds and an N-linked glycan. Disulfides 132-141 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 57-60 19111842-1 2009 Human ATP-binding cassette (ABC) transporter ABCG2 (BCRP/MXR/ABCP) is a plasma membrane protein carrying intra- and inter-molecular disulfide bonds and an N-linked glycan. Disulfides 132-141 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 61-65 19111842-2 2009 Both disulfide bond formation and N-glycosylation are critical check points determining the stability and degradation fate of ABCG2 protein in the endoplasmic reticulum (ER). Disulfides 5-14 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 126-131 18430864-0 2008 Effect of cysteine mutagenesis on the function and disulfide bond formation of human ABCG2. Disulfides 51-60 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 85-90 18430864-3 2008 Based on its apparent half size in sequence when compared with other traditional ABC transporters, ABCG2 has been thought to exist and function as a homodimer linked by intermolecular disulfide bonds. Disulfides 184-193 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 99-104 18430864-7 2008 Mapping of the cysteine residues showed that three cysteine residues (Cys284, Cys374, and Cys438) are required concurrently for the function of ABCG2 and potentially for intramolecular disulfide bond formation. Disulfides 185-194 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 144-149 18430864-9 2008 Thus, we conclude that Cys284, Cys374, and Cys438, which may be involved in intramolecular disulfide bond formation, are concurrently required for ABCG2 function, whereas Cys592, Cys603, and Cys608, potentially involved in intermolecular disulfide bond formation, are not required. Disulfides 91-100 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 147-152 18430864-9 2008 Thus, we conclude that Cys284, Cys374, and Cys438, which may be involved in intramolecular disulfide bond formation, are concurrently required for ABCG2 function, whereas Cys592, Cys603, and Cys608, potentially involved in intermolecular disulfide bond formation, are not required. Disulfides 238-247 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 147-152 17686774-0 2007 Intramolecular disulfide bond is a critical check point determining degradative fates of ATP-binding cassette (ABC) transporter ABCG2 protein. Disulfides 15-24 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 128-133 17686774-2 2007 We previously reported that ABCG2 exists in the plasma membrane as a homodimer bound via a disulfide bond at Cys-603. Disulfides 91-100 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 28-33 17686774-3 2007 In the present study, we examined the importance of an intramolecular disulfide bond for stability of the ABCG2 protein. Disulfides 70-79 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 106-111 17686774-8 2007 Ubiquitin-mediated protein degradation is suggested to be involved in degradation of misfolded ABCG2 proteins lacking the intramolecular disulfide bond. Disulfides 137-146 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 95-100 17686774-10 2007 These results strongly suggest that two distinct pathways exist for protein degradation of ABCG2 WT and mutants lacking the intramolecular disulfide bond. Disulfides 139-148 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 91-96 17686774-11 2007 Namely, the WT ABCG2 is degraded in lysosomes, and the misfolded ABCG2 lacking intramolecular disulfide bond undergoes ubiquitin-mediated protein degradation in proteasomes. Disulfides 94-103 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 65-70 18668433-4 2008 This review paper will address the new aspects of ABCG2 in terms of post-translational modifications (i.e., disulfide bond formation, ubiquitination, and endoplasmic reticulum-associated degradation) of ABCG2 protein, high-speed screening, and quantitative structure-activity relationship (QSAR) analysis to evaluate ABCG2-drug interactions, and genetic polymorphisms potentially associated with photosensitivity. Disulfides 108-117 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 50-55 18668433-4 2008 This review paper will address the new aspects of ABCG2 in terms of post-translational modifications (i.e., disulfide bond formation, ubiquitination, and endoplasmic reticulum-associated degradation) of ABCG2 protein, high-speed screening, and quantitative structure-activity relationship (QSAR) analysis to evaluate ABCG2-drug interactions, and genetic polymorphisms potentially associated with photosensitivity. Disulfides 108-117 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 203-208 18668433-4 2008 This review paper will address the new aspects of ABCG2 in terms of post-translational modifications (i.e., disulfide bond formation, ubiquitination, and endoplasmic reticulum-associated degradation) of ABCG2 protein, high-speed screening, and quantitative structure-activity relationship (QSAR) analysis to evaluate ABCG2-drug interactions, and genetic polymorphisms potentially associated with photosensitivity. Disulfides 108-117 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 203-208 16877258-3 2006 The aim of this review article is to address new aspects of ABCG2 related to redox biology, namely the posttranslational modification (intra- and intermolecular disulfide bond formation) of ABCG2 protein and the transport of porphyrin and chlorophyll metabolites, as well as the high-speed screening and QSAR analysis method to evaluate ABCG2-drug interactions. Disulfides 161-170 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 190-195 16877258-3 2006 The aim of this review article is to address new aspects of ABCG2 related to redox biology, namely the posttranslational modification (intra- and intermolecular disulfide bond formation) of ABCG2 protein and the transport of porphyrin and chlorophyll metabolites, as well as the high-speed screening and QSAR analysis method to evaluate ABCG2-drug interactions. Disulfides 161-170 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 190-195 16107343-6 2005 Because the transporter migrated as a dimer in SDS-PAGE, when only Cys-603 was present (C592A-C608A), the data suggest that Cys-603 forms a symmetrical intermolecular disulfide bridge in the ABCG2 homodimer that is not essential for protein expression and function. Disulfides 167-176 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 191-196 16528971-6 2006 These results strongly suggest that Cys603 is prerequisite for homodimer formation of ABCG2 via a disulfide bond. Disulfides 98-107 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 86-91 16107343-10 2005 This supports the conclusion that Cys-592 and Cys-608 form an intramolecular disulfide bridge in ABCG2 that is critical for substrate specificity. Disulfides 77-86 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 97-102 16107343-12 2005 Altogether, our data are consistent with a scenario in which an inter- and an intramolecular disulfide bridge together are of fundamental importance for the structural and functional integrity of ABCG2. Disulfides 93-102 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 196-201 15769853-5 2005 We also obtained evidence that both ABCG2-wt and ABCG2-K86M exist in the cells as disulfide-linked dimers. Disulfides 82-91 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 36-41 16107343-0 2005 Identification of intra- and intermolecular disulfide bridges in the multidrug resistance transporter ABCG2. Disulfides 44-53 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 102-107 16107343-2 2005 ABCG2 is believed to be a functional homodimer that has been proposed to be linked by disulfide bridges. Disulfides 86-95 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 0-5 15769853-5 2005 We also obtained evidence that both ABCG2-wt and ABCG2-K86M exist in the cells as disulfide-linked dimers. Disulfides 82-91 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 49-54 15835752-8 2005 CONCLUSIONS: These results suggest that, although the presence of N-glycan does not affect the localization of BCRP, disulfide bonds and some peptide sequences in both the N- and C-terminals are necessary for the apical expression of BCRP. Disulfides 117-126 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 234-238