Arginine482 to threonine mutation in the breast cancer resistance protein ABCG2 inhibits rhodamine 123 transport while increasing binding.
about
Marine natural products as breast cancer resistance protein inhibitorsRegulation of biotransformation systems and ABC transporters by benznidazole in HepG2 cells: involvement of pregnane X-receptorPygopus2 inhibits the efficacy of paclitaxel-induced apoptosis and induces multidrug resistance in human glioma cells.Combined effects of epileptic seizure and phenobarbital induced overexpression of P-glycoprotein in brain of chemically kindled ratsARRY-334543 reverses multidrug resistance by antagonizing the activity of ATP-binding cassette subfamily G member 2.Role of basic residues within or near the predicted transmembrane helix 2 of the human breast cancer resistance protein in drug transport.Structure and function of the human breast cancer resistance protein (BCRP/ABCG2).Differential drug resistance acquisition to doxorubicin and paclitaxel in breast cancer cells.Role of the breast cancer resistance protein (ABCG2) in drug transport.Nilotinib potentiates anticancer drug sensitivity in murine ABCB1-, ABCG2-, and ABCC10-multidrug resistance xenograft modelsInteractions of attention-deficit/hyperactivity disorder therapeutic agents with the efflux transporter P-glycoproteinHuman ABCG2: structure, function, and its role in multidrug resistance.Telatinib reverses chemotherapeutic multidrug resistance mediated by ABCG2 efflux transporter in vitro and in vivoA cisplatin-resistant head and neck cancer cell line with cytoplasmic p53(mut) exhibits ATP-binding cassette transporter upregulation and high glutathione levels.Masitinib antagonizes ATP-binding cassette subfamily G member 2-mediated multidrug resistance.GW583340 and GW2974, human EGFR and HER-2 inhibitors, reverse ABCG2- and ABCB1-mediated drug resistance.Bafetinib (INNO-406) reverses multidrug resistance by inhibiting the efflux function of ABCB1 and ABCG2 transporters.Modulation of biotransformation systems and ABC transporters by benznidazole in rats.The nature of amino acid 482 of human ABCG2 affects substrate transport and ATP hydrolysis but not substrate binding.Residues contributing to drug transport by ABCG2 are localised to multiple drug-binding pockets.
P2860
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P2860
Arginine482 to threonine mutation in the breast cancer resistance protein ABCG2 inhibits rhodamine 123 transport while increasing binding.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Arginine482 to threonine mutat ...... port while increasing binding.
@en
type
label
Arginine482 to threonine mutat ...... port while increasing binding.
@en
prefLabel
Arginine482 to threonine mutat ...... port while increasing binding.
@en
P2093
P2860
P356
P1433
P1476
Arginine482 to threonine mutat ...... port while increasing binding.
@en
P2093
Elias Georges
Omar Alqawi
Susan Bates
P2860
P304
P356
10.1042/BJ20040355
P407
P577
2004-09-01T00:00:00Z