ABCG2 p.Cys603Gly
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PMID: 16367905
[PubMed]
Kage K et al: "Role of Cys-603 in dimer/oligomer formation of the breast cancer resistance protein BCRP/ABCG2."
No.
Sentence
Comment
91
Similar results were found for PA/ C603H, PA/C603R, PA/C603G and PA/C603W cells (data not shown).
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ABCG2 p.Cys603Gly 16367905:91:55
status: VERIFIED
PMID: 16877258
[PubMed]
Wakabayashi K et al: "Human ABC transporter ABCG2 in xenobiotic protection and redox biology."
No.
Sentence
Comment
62
It is important to note that substitution of the amino acid at 603 from Cys to Gly disrupted the ability of homodimer formation.
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ABCG2 p.Cys603Gly 16877258:62:63
status: VERIFIED63 The C603G variant of ABCG2 was a monomer (Fig. 4A), which was unchanged even after reductive treatment with dithiothreitol (DTT) (Fig. 4B).
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ABCG2 p.Cys603Gly 16877258:63:4
status: VERIFIED76 The C603G variant was as active as the wild-type variant in terms of ATP-dependent methotrexate transport and drug resistance profiles to SN-38 and mitoxantrone.
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ABCG2 p.Cys603Gly 16877258:76:4
status: VERIFIED78 Immunoblot detection of ABCG2 (WT) as well as of C603G and C592G/C608G variants expressed in Flp-In-293 cells (A).
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ABCG2 p.Cys603Gly 16877258:78:49
status: VERIFIED80 The effect of DTT treatment on C603G and C592G/C608G variants expressed in Flp-In-293 cells (B).
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ABCG2 p.Cys603Gly 16877258:80:31
status: VERIFIED89 Furthermore, the C603G variant was observed in the plasma membrane.
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ABCG2 p.Cys603Gly 16877258:89:17
status: VERIFIED101 Moreover, the protein level of the C592G/ C603G/C608G variant in Flp-In-293 cells was extremely low (Wakabayashi et al., 2006).
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ABCG2 p.Cys603Gly 16877258:101:42
status: VERIFIED
PMID: 18644784
[PubMed]
Ozvegy-Laczka C et al: "Interaction with the 5D3 monoclonal antibody is regulated by intramolecular rearrangements but not by covalent dimer formation of the human ABCG2 multidrug transporter."
No.
Sentence
Comment
28
Interestingly, mutation of Cys-603 to Ala, Gly, or Ser does not remarkably influence the expression and functionality of the transporter (9-11).
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ABCG2 p.Cys603Gly 18644784:28:27
status: VERIFIED
No.
Sentence
Comment
50
The C603G variant is as active as was the wild-type in terms of ATP-dependent methotrexate (MTX) transport and drug resistance profiles to SN-38 and MTX (Wakabayashi et al. 2006).
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ABCG2 p.Cys603Gly 18668433:50:4
status: VERIFIED51 Furthermore, the C603G variant was observed in the plasma membrane as was the wild-type (Wakabayashi et al. 2006).
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ABCG2 p.Cys603Gly 18668433:51:17
status: VERIFIED
PMID: 19111842
[PubMed]
Wakabayashi-Nakao K et al: "Quality control of human ABCG2 protein in the endoplasmic reticulum: ubiquitination and proteasomal degradation."
No.
Sentence
Comment
886
The C603G variant was as active as was the wild type in terms of ATP-dependent MTX transport and profiles of drug resistance to SN-38 and mitoxantrone [4,7].
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ABCG2 p.Cys603Gly 19111842:886:4
status: NEW887 Furthermore, the C603G variant was observed in the plasma membrane [7].
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ABCG2 p.Cys603Gly 19111842:887:17
status: NEW892 Moreover, the protein level of the C592G/C603G/ C608G variant in Flp-In-293 cells was extremely low [7].
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ABCG2 p.Cys603Gly 19111842:892:41
status: NEW
PMID: 19827267
[PubMed]
Ishikawa T et al: "Human ABC transporter ABCG2 in cancer chemotherapy and pharmacogenomics."
No.
Sentence
Comment
187
The C603G variant was as active as was the wild type in terms of ATP-dependent MTX transport and profiles of drug resistance to SN-38 and mitoxantrone (Mitomo et al., 2003; Wakabayashi et al., 2006a).
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ABCG2 p.Cys603Gly 19827267:187:4
status: VERIFIED
PMID: 21567408
[PubMed]
Nakagawa H et al: "Ubiquitin-mediated proteasomal degradation of ABC transporters: a new aspect of genetic polymorphisms and clinical impacts."
No.
Sentence
Comment
92
In fact, substitution of either Cys592 or Cys608 to Gly resulted in a marked decrease in protein levels of ABCG2 in the plasma membrane of Flp-In-293 cells in vitro.77 Moreover, the C592G/ C603G/C608G variant, in which all of the three Cys residues were substituted to Gly, was expressed at an extremely low level.73 The reduced protein levels could not be ascribed to any instability of mRNA encoding those variants because the mRNA levels of ABCG2 WT and those variants were kept at equal levels by Flp-mediated chromosomal integration of one single copy of ABCG2 complementary DNA (cDNA).73 It is important to note that the C592G/C608G variant formed a homodimer, however its cellular localization was remarkably altered.
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ABCG2 p.Cys603Gly 21567408:92:189
status: NEW