about
Predicting P-glycoprotein-mediated drug transport based on support vector machine and three-dimensional crystal structure of P-glycoproteinDrug binding in human P-glycoprotein causes conformational changes in both nucleotide-binding domains.Additive effect of multiple pharmacological chaperones on maturation of CFTR processing mutantsVanadate trapping of nucleotide at the ATP-binding sites of human multidrug resistance P-glycoprotein exposes different residues to the drug-binding siteNucleotide sequence and in vitro expression of rubella virus 24S subgenomic messenger RNA encoding the structural proteins E1, E2 and CThe 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 togetherRecent progress in understanding the mechanism of P-glycoprotein-mediated drug efflux.Human P-glycoprotein contains a greasy ball-and-socket joint at the second transmission interface.Identification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switch.Attachment of a 'molecular spring' restores drug-stimulated ATPase activity to P-glycoprotein lacking both Q loop glutamines.The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoproteinTariquidar inhibits P-glycoprotein drug efflux but activates ATPase activity by blocking transition to an open conformation.Cysteines introduced into extracellular loops 1 and 4 of human P-glycoprotein that are close only in the open conformation spontaneously form a disulfide bond that inhibits drug efflux and ATPase activity.Thiorhodamines containing amide and thioamide functionality as inhibitors of the ATP-binding cassette drug transporter P-glycoprotein (ABCB1).Corrector-mediated rescue of misprocessed CFTR mutants can be reduced by the P-glycoprotein drug pump.The W232R suppressor mutation promotes maturation of a truncation mutant lacking both nucleotide-binding domains and restores interdomain assembly and activity of P-glycoprotein processing mutants.The V510D suppressor mutation stabilizes DeltaF508-CFTR at the cell surface.Correctors promote folding of the CFTR in the endoplasmic reticulum.Suppressor mutations in the transmembrane segments of P-glycoprotein promote maturation of processing mutants and disrupt a subset of drug-binding sites.Using a cysteine-less mutant to provide insight into the structure and mechanism of CFTR.The chemical chaperone CFcor-325 repairs folding defects in the transmembrane domains of CFTR-processing mutants.ATP hydrolysis promotes interactions between the extracellular ends of transmembrane segments 1 and 11 of human multidrug resistance P-glycoprotein.The drug-binding pocket of the human multidrug resistance P-glycoprotein is accessible to the aqueous medium.Processing mutations located throughout the human multidrug resistance P-glycoprotein disrupt interactions between the nucleotide binding domains.Substrate-induced conformational changes in the transmembrane segments of human P-glycoprotein. Direct evidence for the substrate-induced fit mechanism for drug binding.Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein.Introduction of the most common cystic fibrosis mutation (Delta F508) into human P-glycoprotein disrupts packing of the transmembrane segments.A salt bridge in intracellular loop 2 is essential for folding of human p-glycoprotein.Cross-linking of human multidrug resistance P-glycoprotein by the substrate, tris-(2-maleimidoethyl)amine, is altered by ATP hydrolysis. Evidence for rotation of a transmembrane helix.Drug-stimulated ATPase activity of human P-glycoprotein is blocked by disulfide cross-linking between the nucleotide-binding sites.The packing of the transmembrane segments of human multidrug resistance P-glycoprotein is revealed by disulfide cross-linking analysis.The transmembrane domains of the human multidrug resistance P-glycoprotein are sufficient to mediate drug binding and trafficking to the cell surface.The glycosylation and orientation in the membrane of the third cytoplasmic loop of human P-glycoprotein is affected by mutations and substrates.Quality control by proteases in the endoplasmic reticulum. Removal of a protease-sensitive site enhances expression of human P-glycoprotein.Mutational analysis of human P-glycoprotein.Superfolding of the partially unfolded core-glycosylated intermediate of human P-glycoprotein into the mature enzyme is promoted by substrate-induced transmembrane domain interactions.Cytoplasmic loop three of cystic fibrosis transmembrane conductance regulator contributes to regulation of chloride channel activity.The minimum functional unit of human P-glycoprotein appears to be a monomer.Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug-stimulated ATPase activities.Cystic fibrosis: channel, catalytic, and folding properties of the CFTR protein.
P50
Q28477346-AC367D8C-DEF1-4AC8-BC1C-83A052847504Q33185124-1CFDCC27-10E6-48F2-ADAB-9C295396072CQ33286071-7F4ADE6D-58D8-4451-A4F3-54BADA863822Q34018799-D7F4523A-41B7-4BA1-A53D-E7D4D619A717Q36123589-82725E29-F253-45CE-AA01-7D31FD555784Q36137412-26649952-89D2-4B01-A5BD-E661542F6AFFQ36386127-EAE8D3ED-6F6C-4394-AA72-58DDA481B46DQ37012424-558E55CC-9D2B-4A68-BF2E-4722F76155B1Q37653308-F86AF8FC-A7BA-47F7-A9B8-0428FDC89387Q38724203-2B6B9A51-9DF9-4DCB-9495-A676FE2F4642Q38873295-CDAFE3E0-3CE2-40F4-AFFD-8DB339DEAEC6Q38933973-05C9087F-780F-432E-9BBC-AD6B93BE757CQ38972586-124C86B2-8A58-429A-ACD4-975BBE3D56DCQ39326387-B922CA33-8973-4C82-B6E4-D69FA8B29D17Q39433623-0878A968-2D31-46AF-B871-B032B6A53E3BQ39616542-6CC8368A-A3A4-45A9-9A2D-159A4BF79678Q39686806-048A7301-9AE4-4527-9637-D80CC48673EEQ39999241-A7EFE2C0-5AD2-41C8-A4B5-0DF55D8FBDE6Q40082401-B720EC81-757F-4099-88BE-F2E5B209DA0DQ40312181-BEFE069A-CFCC-4C6A-B496-AFF85CCE18CEQ40328635-C96EFC03-8E0F-4515-9066-D7D89A84126BQ40393600-57E27231-365A-4ABE-AE5A-AA44272EE253Q40513676-3A5CD997-1E6B-4955-921C-3D014BF3EE07Q40537131-8A15B90E-29C6-4C1D-8B30-C82027B7B02FQ40667534-222A14D1-A724-415E-82C3-A5EC43F49728Q40704865-6C42F097-FBE5-43B6-ADD8-1215FA3BC6E8Q40724271-E915D9A4-8B26-4D02-860D-3D58CE11614DQ40790212-3E98D3B4-D32F-4144-974C-D783D9FBEDC3Q40795985-11E2FD00-ED46-4964-B9F3-4A33FC0E5F81Q40880583-1A068B99-5287-4730-9F1F-8EB99A092228Q40899411-5C041148-1082-4F28-8B5E-191252CEA564Q40934272-C2F00627-44C5-4F2D-9A29-332DC049EFF5Q40959016-294C436D-50F5-4892-A3E3-45DB4901CA68Q40992489-56B5A114-A1CA-4EC3-8C4F-ED85B8885697Q41015222-F6B9316E-B9BA-4F4C-B9EE-E5784736BAC0Q41034671-68E6AFBF-178D-48E2-AB19-A6111DB9AE0BQ41155403-3CB0460F-DD7E-499C-997D-057CF67BDBDCQ41155410-10E8BA89-01A4-49E3-B442-BC7BA42BF76CQ41295094-51443087-2E19-416D-A963-B03A1F5D0558Q41725508-BEEBA4FD-8187-4881-9BB8-73113E190834
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Tip W. Loo
@ast
Tip W. Loo
@en
Tip W. Loo
@es
Tip W. Loo
@nl
Tip W. Loo
@sl
type
label
Tip W. Loo
@ast
Tip W. Loo
@en
Tip W. Loo
@es
Tip W. Loo
@nl
Tip W. Loo
@sl
prefLabel
Tip W. Loo
@ast
Tip W. Loo
@en
Tip W. Loo
@es
Tip W. Loo
@nl
Tip W. Loo
@sl
P106
P1153
7006008593
P31
P496
0000-0003-2108-0188