Interaction with the 5D3 monoclonal antibody is regulated by intramolecular rearrangements but not by covalent dimer formation of the human ABCG2 multidrug transporter
about
Disruption of N-linked glycosylation enhances ubiquitin-mediated proteasomal degradation of the human ATP-binding cassette transporter ABCG2Expression levels of the ABCG2 multidrug transporter in human erythrocytes correspond to pharmacologically relevant genetic variationsJump into a New Fold-A Homology Based Model for the ABCG2/BCRP Multidrug TransporterRole of basic residues within or near the predicted transmembrane helix 2 of the human breast cancer resistance protein in drug transport.Fluorescence resonance energy transfer (FRET) analysis demonstrates dimer/oligomer formation of the human breast cancer resistance protein (BCRP/ABCG2) in intact cells.Identification of proline residues in or near the transmembrane helices of the human breast cancer resistance protein (BCRP/ABCG2) that are important for transport activity and substrate specificity.Structure and function of the human breast cancer resistance protein (BCRP/ABCG2).ABCG2 transports and transfers heme to albumin through its large extracellular loopMembrane topology of the human breast cancer resistance protein (BCRP/ABCG2) determined by epitope insertion and immunofluorescence.Interaction of nilotinib, dasatinib and bosutinib with ABCB1 and ABCG2: implications for altered anti-cancer effects and pharmacological propertiesRegulation of the function of the human ABCG2 multidrug transporter by cholesterol and bile acids: effects of mutations in potential substrate and steroid binding sites.The importance of drug transporters in human pluripotent stem cells and in early tissue differentiation.Effects of the lipid environment, cholesterol and bile acids on the function of the purified and reconstituted human ABCG2 protein.Structure-function relationships in ABCG2: insights from molecular dynamics simulations and molecular docking studies.Expression levels of ABCG2 on cord red blood cells and study of fetal anemia associated with anti-Jr(a).
P2860
Q24316869-66EAA890-6796-4101-AD41-714B5015ECD9Q28485221-E7446761-6F41-44F8-B34B-A4A415BEB5F2Q28552715-4D283F8C-6FAD-4930-BC3A-8B00E1D6F9D3Q33890952-84C517B8-54F4-4C47-9CFB-B52EE83E5916Q33980380-FFB56017-20AE-4903-AB63-B0CD3F3FD266Q33997565-7BB633AA-063B-4631-B8E5-AEC8BCC8FC9EQ34176588-B4037229-4687-49DF-938A-D88A5CDC6535Q34236666-BC391A4D-D92C-42C8-838F-7622C41485C9Q34897883-B42BA1ED-DD19-4847-9B43-E02F46BA600FQ37447522-2AA78C38-AF7C-454F-9787-02D3F541D361Q38514267-A6CF04C2-5833-4A2F-B96E-753918EA8D54Q38642449-A4D85109-5BED-42EF-AF19-5DCA47AC00DEQ39233676-2AD45C97-D96A-47B1-B6F6-2B1875A5688CQ45569138-5E5C7EF4-CD32-4939-9025-4C3A87C0E749Q50261032-62639F76-A52E-4459-A1FE-498B5DC6845D
P2860
Interaction with the 5D3 monoclonal antibody is regulated by intramolecular rearrangements but not by covalent dimer formation of the human ABCG2 multidrug transporter
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Interaction with the 5D3 monoc ...... an ABCG2 multidrug transporter
@ast
Interaction with the 5D3 monoc ...... an ABCG2 multidrug transporter
@en
type
label
Interaction with the 5D3 monoc ...... an ABCG2 multidrug transporter
@ast
Interaction with the 5D3 monoc ...... an ABCG2 multidrug transporter
@en
prefLabel
Interaction with the 5D3 monoc ...... an ABCG2 multidrug transporter
@ast
Interaction with the 5D3 monoc ...... an ABCG2 multidrug transporter
@en
P2093
P2860
P356
P1476
Interaction with the 5D3 monoc ...... an ABCG2 multidrug transporter
@en
P2093
András Váradi
Balázs Sarkadi
Brian P Sorrentino
Csilla Hegedus
Csilla Ozvegy-Laczka
György Várady
Katalin Goda
Rozália Laczkó
Tamás Hegedus
P2860
P304
26059-26070
P356
10.1074/JBC.M803230200
P407
P577
2008-07-21T00:00:00Z