Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket.
about
Plant Lessons: Exploring ABCB Functionality Through Structural ModelingMultiple Drug Transport Pathways through Human P-Glycoprotein.Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegansRefined structures of mouse P-glycoproteinCatalytic transitions in the human MDR1 P-glycoprotein drug binding sites.Additive effect of multiple pharmacological chaperones on maturation of CFTR processing mutantsMolecular models of human P-glycoprotein in two different catalytic statesTransmembrane helices 1 and 6 of the human breast cancer resistance protein (BCRP/ABCG2): identification of polar residues important for drug transport.Understanding polyspecificity of multidrug ABC transporters: closing in on the gaps in ABCB1Structural characterization of two metastable ATP-bound states of P-glycoprotein.The ATPase activity of the P-glycoprotein drug pump is highly activated when the N-terminal and central regions of the nucleotide-binding domains are linked closely togetherMolecular model of the outward facing state of the human P-glycoprotein (ABCB1), and comparison to a model of the human MRP5 (ABCC5)Human P-glycoprotein contains a greasy ball-and-socket joint at the second transmission interface.Binding site of ABC transporter homology models confirmed by ABCB1 crystal structureIn silico analysis of the binding of anthelmintics to Caenorhabditis elegansP-glycoprotein 1.Multidrug efflux pumps: drug binding--gates or cavity?Identification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switch.MRP1 expressed on Burkitt's lymphoma cells was depleted by catfish egg lectin through Gb3-glycosphingolipid and enhanced cytotoxic effect of drugs.Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket.Arginines in the first transmembrane segment promote maturation of a P-glycoprotein processing mutant by hydrogen bond interactions with tyrosines in transmembrane segment 11.Substrate-dependent effects of human ABCB1 coding polymorphismsSuppressor mutations in the transmembrane segments of P-glycoprotein promote maturation of processing mutants and disrupt a subset of drug-binding sites.Targeting P-glycoprotein: Investigation of piperine analogs for overcoming drug resistance in cancer.Modulation of drug-stimulated ATPase activity of human MDR1/P-glycoprotein by cholesterolNovel cGMP efflux inhibitors identified by virtual ligand screening (VLS) and confirmed by experimental studies.Locking intracellular helices 2 and 3 together inactivates human P-glycoprotein.Transmembrane helix 12 modulates progression of the ATP catalytic cycle in ABCB1.Inhibition of multidrug resistance by adamantylgb3, a globotriaosylceramide analog.Characterizing the binding interactions between P-glycoprotein and eight known cardiovascular transport substrates.Mapping the Binding Site of the Inhibitor Tariquidar That Stabilizes the First Transmembrane Domain of P-glycoprotein.Structural elucidation of transmembrane domain zero (TMD0) of EcdL: A multidrug resistance-associated protein (MRP) family of ATP-binding cassette transporter protein revealed by atomistic simulation.Residues contributing to drug transport by ABCG2 are localised to multiple drug-binding pockets.Structural model, functional modulation by ivermectin and tissue localization of Haemonchus contortus P-glycoprotein-13.Evidence for the critical role of transmembrane helices 1 and 7 in substrate transport by human P-glycoprotein (ABCB1)
P2860
Q21129220-D796B73B-4045-4C73-A3BB-107DB71D55A8Q27301793-029AD59D-BAA6-45E3-93AE-43E33488B16AQ27673547-30BEE851-6B48-4535-968E-0B6D4DE214AEQ27680445-E8808CF9-2924-424E-B1A8-ACF4D96E2C35Q30518005-FB0FED25-DD81-4257-B305-A84568044E43Q33286071-98143940-4467-4376-ADAD-E36C617D4F95Q33401731-5DB150A1-584B-477C-9BDC-05BF322EF819Q33672739-69D571A6-DF30-41E5-B44D-1C5EE573C101Q35007411-F2428125-FE40-4633-95B4-BB999373057AQ35121898-4846EFAB-8F07-4E3E-BAF4-A5AECF7A18E3Q36137412-186D3728-59E2-4D9E-89E6-C463C830D4F2Q36398058-2C7DCBFF-708E-4235-8D1D-D60E6A2B611AQ37012424-37E17846-1FEA-4045-8635-59167C8339E5Q37355834-500329BE-99AA-49FD-A695-483E0463461EQ37541732-66D6C96A-4FF6-43CD-88B8-50EBF4608F57Q37644558-B488FE4E-DCEE-4593-ADF4-A2BB957BF418Q37653308-738AFF97-4952-414C-96B7-E3FDA35F2B46Q38330317-DD361C63-AFAB-41AB-8066-C92B993FB8D9Q38663320-931EF192-2511-4FC9-BAC4-ACFD40BB6905Q39966104-B22A3CE4-47D9-49F3-A30C-3F8B49DB2E1BQ40011132-6BFF932B-4002-4D13-92B9-1C2E2F564F49Q40082401-E8CF4164-87D1-4831-8F37-497BAAD2CD63Q41368134-3438D04B-93BB-4AEE-B3CB-3D524576E548Q41774328-0A3BFE50-64D0-4EE7-BEE5-3BE03928DA83Q41842363-ABEF2C92-096C-4C1E-9A6B-3AB1414641BBQ41848364-FAE7EDB0-4544-4234-884F-599297C277DEQ42105486-B1F40CB1-BED4-445E-BD24-06F83192B0DFQ42521464-2012EA96-D40C-4C22-9A23-80AB57FD2C0EQ43068236-32BF2F27-3246-469D-859E-FA169FB096ABQ43099273-B1374484-27A6-44F8-B572-A75ACA8294DEQ47777478-168B364F-766C-4110-B578-034A0DF90169Q53694857-246339E5-5DA7-4675-A8DA-CDF29073997DQ53835459-9A593DCF-D2E9-4238-B3E5-8DBD76725B0EQ59126511-8DD55EFE-B81D-480D-865C-A5488B0BFF76
P2860
Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket.
@en
type
label
Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket.
@en
prefLabel
Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket.
@en
P2093
P2860
P356
P1433
P1476
Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket.
@en
P2093
David M Clarke
M Claire Bartlett
P2860
P304
P356
10.1042/BJ20060012
P407
P577
2006-06-01T00:00:00Z