Effects of mutations of ABCA1 in the first extracellular domain on subcellular trafficking and ATP binding/hydrolysis. - Wikidata - wikimedia - TriplyDB

Effects of mutations of ABCA1 in the first extracellular domain on subcellular trafficking and ATP binding/hydrolysis.

Effects of mutations of ABCA1 in the first extracellular domain on subcellular trafficking and ATP binding/hydrolysis.

http://www.wikidata.org/entity/Q38359051

about

Human ABCA7 supports apolipoprotein-mediated release of cellular cholesterol and phospholipid to generate high density lipoprotein Adrenoleukodystrophy: subcellular localization and degradation of adrenoleukodystrophy protein (ALDP/ABCD1) with naturally occurring missense mutations Differential phospholipid substrates and directional transport by ATP-binding cassette proteins ABCA1, ABCA7, and ABCA4 and disease-causing mutants Mammalian P4-ATPases and ABC transporters and their role in phospholipid transport The interaction of ApoA-I and ABCA1 triggers signal transduction pathways to mediate efflux of cellular lipids Phosphorylation of a pest sequence in ABCA1 promotes calpain degradation and is reversed by ApoA-I Unexpected gain of function for the scaffolding protein plectin due to mislocalization in pancreatic cancer.Alpha1-syntrophin modulates turnover of ABCA1.Prediction of disease-related mutations affecting protein localization.ABCA1, ABCG1, and ABCG4 are distributed to distinct membrane meso-domains and disturb detergent-resistant domains on the plasma membrane.HIV-1 protein Nef inhibits activity of ATP-binding cassette transporter A1 by targeting endoplasmic reticulum chaperone calnexin Functional and trafficking defects in ATP binding cassette A3 mutants associated with respiratory distress syndrome.Characterization and classification of ATP-binding cassette transporter ABCA3 mutants in fatal surfactant deficiency.ABCA3-mediated choline-phospholipids uptake into intracellular vesicles in A549 cells.ABCA1 and nascent HDL biogenesis The reverse cholesterol transport system as a potential mediator of luteolysis in the primate corpus luteum A-Subclass ATP-Binding Cassette Proteins in Brain Lipid Homeostasis and Neurodegeneration.ABCG1 and ABCG4 Suppress γ-Secretase Activity and Amyloid β Production.Host HDL biogenesis machinery is recruited to the inclusion of Chlamydia trachomatis-infected cells and regulates chlamydial growth ABCA7, a molecule with unknown function.Mechanisms for cellular cholesterol transport: defects and human disease.Protein kinase C controls vesicular transport and secretion of apolipoprotein E from primary human macrophages.Both STAT3 activation and cholesterol efflux contribute to the anti-inflammatory effect of apoA-I/ABCA1 interaction in macrophages.ABCA1 mutants reveal an interdependency between lipid export function, apoA-I binding activity, and Janus kinase 2 activation.Sphingomyelin depletion impairs anionic phospholipid inward translocation and induces cholesterol efflux.Genetic variation in ABC transporter A1 contributes to HDL cholesterol in the general population.Lipid outward translocation by ABC proteins.ATP-binding cassette proteins involved in glucose and lipid homeostasis.ABC proteins protect the human body and maintain optimal health.Function and regulation of ABCA1--membrane meso-domain organization and reorganization.Oxysterols trigger ABCA1-mediated basolateral surfactant efflux.Genetic and/or non-genetic causes for inter-individual and inter-cellular variability in transporter protein expression: implications for understanding drug efficacy and toxicity.Orthogonal lipid sensors identify transbilayer asymmetry of plasma membrane cholesterol.Liver X receptor beta (LXRbeta) interacts directly with ATP-binding cassette A1 (ABCA1) to promote high density lipoprotein formation during acute cholesterol accumulation.Sodium taurocholate-dependent lipid efflux by ABCA1: effects of W590S mutation on lipid translocation and apolipoprotein A-I dissociation.ATP hydrolysis-dependent conformational changes in the extracellular domain of ABCA1 are associated with apoA-I binding Direct interaction of nuclear liver X receptor-beta with ABCA1 modulates cholesterol efflux.Sphingomyelin-dependence of cholesterol efflux mediated by ABCG1.Enhanced apoA-I-dependent cholesterol efflux by ABCA1 from sphingomyelin-deficient Chinese hamster ovary cells.Purification and ATPase activity of human ABCA1.

P2860

Q24298205-41A3B84E-B08C-4F91-AB97-EB7E6DA6CF89 Q24307632-9C200C01-693A-4295-9E42-E9DADFB0485B Q24337731-8E43DF49-B7C2-4783-96D9-68879892A702 Q26866484-80655D29-385D-4169-8ED8-573B783D1E5F Q27025329-0F81A447-77E2-426D-8344-C9EF1176C56F Q28593742-0ABBA7F3-D912-40D8-AB60-DBB262E1F074 Q30412956-300130DF-8486-47B9-BD68-D76336816A26 Q33196798-6567F778-43AC-4187-B2A1-3465F0884E64 Q33421104-91FA5D94-CC7A-43EE-90D8-E45BD28CAAFF Q34323469-C8D3C0FA-60AC-4062-B69C-E228469843A4 Q34355599-8AC69ED1-73C1-414F-8F0D-EC6F1882E85D Q34484976-94FB8DFA-3443-4B0C-A08A-740B3DC4F518 Q34564474-6BA66F2F-D325-4289-ADF2-9DAA539E4471 Q34638334-728481E7-85E8-474F-888F-6B7383144D9C Q34958342-E2A19856-DF88-4D0E-93C3-1D484E4DE7BC Q35664777-271FA267-FC79-4E87-BF97-DDD3D277D6D2 Q35801008-5A7EE9E8-FF94-4DF9-8269-DE1C502A2317 Q36022428-87E2849F-1C53-4DC1-97A0-5B228539FF13 Q36236662-00BC9924-6664-4293-9EC4-8B06A82E9BC1 Q36352955-EF5BCF8A-78DA-4A5D-B681-39ABDBC477E1 Q36610465-D64587C8-CD52-4CDD-909E-0451EC31BEB5 Q36620898-A36F75F3-A05F-47F2-A6E3-2C83C432D716 Q36843317-63FE8E89-A45C-432A-B5A5-66A978739787 Q37086134-92623B0F-B13C-4B0C-AF6F-912DAF714983 Q37415663-630FE907-8EE9-41C8-BCCD-EF5DEC9D232F Q37591896-171D40CC-D1DC-46A7-8E7E-E0F445DF5420 Q37735992-332A3D36-7984-404F-9371-28BBFB06C136 Q37749201-FCF1B1C5-AEA7-4E00-B480-8C2DA0D1FAD6 Q37851290-E95EADC4-96E1-4E1F-A625-D6339FBC3150 Q37873571-C8C8E83E-7AD0-459E-80A8-23361151BCC3 Q38343286-4F27780E-A19C-4DB4-83FE-00F223E978EB Q38613161-AC2EA7FC-276F-4709-9F37-C870B0B79C0D Q38724298-0309606D-CAD7-480E-B74D-259CF3134855 Q39555610-34592D7B-9FF5-4E4E-9F36-7BFECD9A8DCF Q39885961-03842A69-9E94-432D-905B-4C664795B4E9 Q39935026-2F93D07A-5249-4D82-A507-54CD9E2D3E90 Q39941431-C530FABA-0999-4614-93B3-6374EFE819A4 Q40087053-9C2FFCB5-7114-4F79-9CA8-CD8E4A309DCA Q40149619-4C954E3A-C829-4C72-954C-9D49075669A0 Q40311731-490FC9ED-656D-4D9D-AA1E-9F9C7AAA3668

P2860

Effects of mutations of ABCA1 in the first extracellular domain on subcellular trafficking and ATP binding/hydrolysis.

http://www.wikidata.org/entity/Q38359051

description

2002 nî lūn-bûn

@nan

2002年の論文

@ja

2002年学术文章

@wuu

2002年学术文章

@zh-cn

2002年学术文章

@zh-hans

2002年学术文章

@zh-my

2002年学术文章

@zh-sg

2002年學術文章

@yue

2002年學術文章

@zh

2002年學術文章

@zh-hant

name

Effects of mutations of ABCA1 ...... ng and ATP binding/hydrolysis.

@en

type

label

Effects of mutations of ABCA1 ...... ng and ATP binding/hydrolysis.

@en

prefLabel

Effects of mutations of ABCA1 ...... ng and ATP binding/hydrolysis.

@en

P1433

Q38359051-43034CA2-02AE-417C-A6DE-E6973DCF1428

P1476

Q38359051-E6849108-CB68-4E44-B82C-E8836FCE3D66

P2093

Q38359051-1F7D3D22-33F8-491D-9155-A4443D2AD602

Q38359051-302B3D98-0E0B-447B-B15B-9EA1361DC620

Q38359051-3574425E-C662-4034-A855-E42F33654F8F

Q38359051-5DFB043C-B7C3-4A10-8C5F-86EF5D031EA4

Q38359051-6EFF67C4-B867-4CE4-84CF-B47A97136193

Q38359051-72C5E993-D66B-4A5A-983E-83C8F02C95F2

Q38359051-91BC24E7-0386-4F38-A602-71D49BAE503B

Q38359051-9D866FAF-265E-4CAB-8096-62AE48C21BEE

Q38359051-BB242DD2-7159-4F34-8569-11D6AB6B6D38

Q38359051-CA08FDAD-4E00-40B4-A1DC-E5E708442B83

P2860

Q38359051-01977552-4791-46B5-91B6-302BF109BE52

Q38359051-0244CB09-61A1-46C4-8E3B-9E5D9770DD52

Q38359051-048F6AC6-6FE0-459E-81E8-17DDAAD3D9A0

Q38359051-0BE66307-C816-4013-AE92-CE8CB4C0E6B8

Q38359051-28A0D246-48FD-4F7A-9F40-9D1C9798B90B

Q38359051-2A449797-1FB9-48E4-85FC-83E25924FF29

Q38359051-2F60D4A9-B5FB-48F7-BD72-F10D067FA524

Q38359051-35B8BBC4-4D2F-4685-85F2-4F32668DF176

Q38359051-450DB803-4831-45F3-A780-CF276E9DB531

Q38359051-45B26FAA-FFE4-4963-848C-1BD849AAD882

P304

Q38359051-0C7C1AC0-1183-4B06-B9BD-0AFADEEB3551

P31

Q38359051-40F04902-05EA-401B-BC46-AA2F1860EA96

P356

Q38359051-389F5148-9CCD-4596-87B3-D24B6A3F37FF

P407

Q38359051-7FC8E50B-5234-4F69-AF53-3EFAFC2ACCF6

P433

Q38359051-AD663E62-1E53-4FD7-8299-6249E5DB07E4

P478

Q38359051-547DFDCC-6C31-4660-96C8-53B5988E103E

P50

Q38359051-549F6BCE-5D68-4E56-9C4D-ADC2EF4196D9

P577

Q38359051-6037831C-0DB0-4D13-AC40-B6107FDD3E09

P698

Q38359051-4AD301EB-D818-42C7-9A7B-A8E20A693F1B

P356

P1433

Journal of Biological Chemistry

P1476

Effects of mutations of ABCA1 ...... ng and ATP binding/hydrolysis.

@en

P2093

Arowu R Tanaka

http://www.w3.org/2001/XMLSchema#string

Fumi Kano

http://www.w3.org/2001/XMLSchema#string

Gaku Morinaga

http://www.w3.org/2001/XMLSchema#string

Kei-ichiro Okuhira

http://www.w3.org/2001/XMLSchema#string

Masayuki Murata

http://www.w3.org/2001/XMLSchema#string

Michinori Matsuo

http://www.w3.org/2001/XMLSchema#string

Noriyuki Kioka

http://www.w3.org/2001/XMLSchema#string

Ryo Aoki

http://www.w3.org/2001/XMLSchema#string

Shinji Yokoyama

http://www.w3.org/2001/XMLSchema#string

Sumiko Abe-Dohmae

http://www.w3.org/2001/XMLSchema#string

P2860

Mutations in ABC1 in Tangier disease and familial high-density lipoprotein deficiency

The Tangier disease gene product ABC1 controls the cellular apolipoprotein-mediated lipid removal pathway

Apolipoprotein specificity for lipid efflux by the human ABCAI transporter

Characterization of the ATPase cycle of human ABCA1: implications for its function as a regulator rather than an active transporter

Naturally occurring mutations in the largest extracellular loops of ABCA1 can disrupt its direct interaction with apolipoprotein A-I

Brefeldin A: insights into the control of membrane traffic and organelle structure

Human ATP-binding cassette transporter 1 (ABC1): genomic organization and identification of the genetic defect in the original Tangier disease kindred

The gene encoding ATP-binding cassette transporter 1 is mutated in Tangier disease

Tangier disease is caused by mutations in the gene encoding ATP-binding cassette transporter 1

ABC1 promotes engulfment of apoptotic cells and transbilayer redistribution of phosphatidylserine

P304

8815-8819

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M206885200

http://www.w3.org/2001/XMLSchema#string

P407

P433

10

http://www.w3.org/2001/XMLSchema#string

P478

278

http://www.w3.org/2001/XMLSchema#string

P50

P577

2002-12-31T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

12509412

http://www.w3.org/2001/XMLSchema#string