about
Expression and in vivo rescue of human ABCC6 disease-causing mutants in mouse liverYeast ARV1 is required for efficient delivery of an early GPI intermediate to the first mannosyltransferase during GPI assembly and controls lipid flow from the endoplasmic reticulum.Molecular docking simulations provide insights in the substrate binding sites and possible substrates of the ABCC6 transporterScreening the expression of ABCB6 in erythrocytes reveals an unexpectedly high frequency of Lan mutations in healthy individualsRole of Hsp90 in biogenesis of the beta-cell ATP-sensitive potassium channel complexTetrameric structure of SUR2B revealed by electron microscopy of oriented single particlesLack of support for a role for RLIP76 (RALBP1) in response to treatment or predisposition to epilepsy.Role of the N-terminal transmembrane domain in the endo-lysosomal targeting and function of the human ABCB6 protein.Abca12-mediated lipid transport and Snap29-dependent trafficking of lamellar granules are crucial for epidermal morphogenesis in a zebrafish model of ichthyosisPhoto-activation of the hydrophobic probe iodonaphthylazide in cells alters membrane protein function leading to cell death.Fungal PDR transporters: Phylogeny, topology, motifs and function.Side population cells from human melanoma tumors reveal diverse mechanisms for chemoresistance.Conserved intramolecular disulfide bond is critical to trafficking and fate of ATP-binding cassette (ABC) transporters ABCB6 and sulfonylurea receptor 1 (SUR1)/ABCC8A novel conserved targeting motif found in ABCA transporters mediates trafficking to early post-Golgi compartments.A-Subclass ATP-Binding Cassette Proteins in Brain Lipid Homeostasis and Neurodegeneration.Impact of mutant β-catenin on ABCB1 expression and therapy response in colon cancer cellsLGR5 rs17109924 is a predictive genetic biomarker for time to recurrence in patients with colon cancer treated with 5-fluorouracil-based adjuvant chemotherapy.New insight into the biochemical mechanisms regulating auxin transport in plants.Drug resistance in cancer - searching for mechanisms, markers and therapeutic agents.Disruption of N-linked glycosylation promotes proteasomal degradation of the human ATP-binding cassette transporter ABCA3.Analysis of pseudoxanthoma elasticum-causing missense mutants of ABCC6 in vivo; pharmacological correction of the mislocalized proteins.Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating.An update on ABCB1 pharmacogenetics: insights from a 3D model into the location and evolutionary conservation of residues corresponding to SNPs associated with drug pharmacokinetics.ABC transporters and their role in nucleoside and nucleotide drug resistance.The biology of the ABCA3 lipid transporter in lung health and disease.Co-expression of human ABCG5 and ABCG8 in insect cells generates an androstan stimulated membrane ATPase activity.Direct evidence that the N-terminal extensions of the TAP complex act as autonomous interaction scaffolds for the assembly of the MHC I peptide-loading complexAnti-diabetic drug binding site in a mammalian KATP channel revealed by Cryo-EM.Identification of a human ABCC10 orthologue in Catharanthus roseus reveals a U12-type intron determinant for the N-terminal domain feature.Mutations in the ABCC8 gene encoding the SUR1 subunit of the KATP channel cause transient neonatal diabetes, permanent neonatal diabetes or permanent diabetes diagnosed outside the neonatal period.Measuring the Conformational Distance of GPCR-related Proteins Using a Joint-based Descriptor.Plant ABC Transporters
P2860
Q27320511-D9051E81-34FE-4E5C-9D56-02F97D4BD401Q27933944-EB223258-8E02-403C-AA86-43896AE70FE4Q28541190-EDD5A1EF-393C-4578-B869-F854308DB8AAQ28544657-D41FFA2E-8189-4C72-95D0-64ABA6C664E8Q28566112-E9F6ACD2-3FFA-41F2-A8A8-30154472FB87Q28569280-36836C1B-DA67-4815-A682-42DD4C2248C2Q30361123-96CF1377-93A8-41B1-A12F-51A5C5610B4AQ30412396-749593FA-DEBF-4059-8A3C-B6AD1E9D42B1Q30429793-96DCA004-D98E-408D-A59D-41026E347573Q33422611-FE088FF0-1062-4D6C-83C8-9D96697F307BQ33624643-E6AAA011-372F-4563-A2AA-256EE98A23CAQ34279342-1FB14F43-8ACA-46A8-A51E-CDDB9C401F09Q34624461-3E353DDE-D369-41D0-9A39-68E42DDB2319Q35114017-42874F79-B7A3-40E2-943B-AFB3D1E6A352Q35801008-F8DF754A-90E5-46E7-B2BC-777BD3503D05Q35892881-A1129B13-0CB7-47CB-86A0-57A5A8DD6E81Q36605121-D83701DD-4B33-4A63-8CEC-81941527CC5BQ36702133-3BBB93CE-A1F9-4C76-9063-D9EDA34D6070Q37008882-11BE4A02-6465-4A95-822B-6D29D9B82B44Q37440530-0D4DB004-C3F0-400E-8B74-7E451A8CA917Q37655761-521CCA18-ABD7-48E7-B317-B0964030D87BQ37691747-A8A33306-3BC9-41F4-9772-A227785760ECQ37882401-2A0C9A8F-70BB-40A2-B7F0-641DC4F644C0Q37979617-84A6AB4C-4C01-41D1-B389-19F5C1176BDBQ39057094-925E05AE-B5A8-4D49-9F2B-17390EF4F828Q40217248-DD430490-6B6A-4FCB-AADD-3BC62936AECFQ41853333-B43C5F1E-D767-4D8D-BEC7-FDE8C20EFC8CQ42637813-3ED9241D-E708-4D49-9E91-C1B9E6A8745EQ42661149-4262965D-2F07-4A89-A73F-F9CA1969346AQ46964181-57BC9D53-D355-4F94-845F-E2382C64DBFFQ47109042-5A0B5FCD-442C-440A-BB8F-2C14139E4E66Q56136135-433C6343-A5F3-405B-8B85-10B78C6555DA
P2860
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
Membrane topology of human ABC proteins.
@ast
Membrane topology of human ABC proteins.
@en
type
label
Membrane topology of human ABC proteins.
@ast
Membrane topology of human ABC proteins.
@en
prefLabel
Membrane topology of human ABC proteins.
@ast
Membrane topology of human ABC proteins.
@en
P2860
P1433
P1476
Membrane topology of human ABC proteins
@en
P2093
András Váradi
Balázs Sarkadi
P2860
P304
P356
10.1016/J.FEBSLET.2005.11.040
P407
P577
2005-12-01T00:00:00Z