About: Functional role of evolutionarily highly conserved residues, N-glycosylation level and domains of the Leishmania miltefosine transporter-Cdc50 subunit

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About: Functional role of evolutionarily highly conserved residues, N-glycosylation level and domains of the Leishmania miltefosine transporter-Cdc50 subunit Goto Sponge NotDistinct Permalink

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scientific article published on 01 April 2014

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована у квітні 2014 (uk) im April 2014 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'abril de 2014 (ast) scientific article published on 01 April 2014 (en)
publication date	wds:Q56894082-92FE0A2A-F348-42A3-85CC-3B975B592316
publication date	2014-04-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q56894082-AE2CF02C-2FDF-4C6C-B531-FCB12D303DE1
language of work or name	English
cites work	wds:Q56894082-035C0B58-7501-41F2-AAB9-8F9B4C307469 wds:Q56894082-03E5E67E-FA01-499D-B7D7-611E1F6205B0 wds:Q56894082-044B5860-FBF0-4C40-BCCD-6457C467E88F wds:Q56894082-188561CE-840E-4816-A8F6-1FF12344E003 wds:Q56894082-1D0E9D9A-051E-48E3-B2AB-430F57AE9CCE wds:Q56894082-1FF03297-0A8F-4DA1-8ED1-FF41ECD431B6 wds:Q56894082-20C00329-B586-438C-809B-0C94FC3D657A wds:Q56894082-33FA347E-23ED-4192-91BA-BA5C19AB1B0A wds:Q56894082-39F4CD2B-07EA-44F1-B26D-FACE8B4FAC08 wds:Q56894082-403CDE61-7388-45E3-AEF7-6301BB7B9991 wds:Q56894082-4CC86BDA-5215-45A1-893A-09507C4569FD wds:Q56894082-508AA414-AB8E-4BCA-BDEA-F6B290A3F8AF wds:Q56894082-512641D8-9204-4063-97B9-471FF9C04BD9 wds:Q56894082-57C87E18-F3F1-4382-AFCD-C4D760631619 wds:Q56894082-5A557BC5-799A-43C9-9412-09F6B68B7399 wds:Q56894082-69978968-50B5-4E8F-A9A6-025E2907E8DF wds:Q56894082-7211BBB7-3045-4AED-B525-1200391995EA wds:Q56894082-7BFFCA29-821E-496B-A2BD-915F437AC5C2 wds:Q56894082-7D0C2F57-5139-4D83-8AFD-CD94257B6845 wds:Q56894082-95467032-385D-4ED1-A4AF-98D4944B9419 wds:Q56894082-9893CDA4-F0B6-4B30-8487-3BB98A8DA386 wds:Q56894082-A485B8EE-36CB-420B-BBEC-7BAA1AE1E51E wds:Q56894082-A99AE213-3F18-4537-A200-518ABD5A9D84 wds:Q56894082-AFB9AD4E-C663-4A2B-A605-95FF09D34F4C wds:Q56894082-B0D580E9-E1EB-4D71-898B-5891B87F0D51 wds:Q56894082-B58DD8F5-167B-430E-8BCC-33BA1D2F9123 wds:Q56894082-BFDF21CC-5471-47AB-8A2F-028213384AB9 wds:Q56894082-C64AD9E3-8A25-401E-B386-D0BC60CA5712 wds:Q56894082-CC316B5D-C111-49A4-86AD-AA2F2F5E53D9 wds:Q56894082-DD97802E-3030-4739-89CF-20523BC44442 wds:Q56894082-DF1383BC-379D-4EF9-A06D-777B70C9D40C wds:Q56894082-E2E8F727-2968-431A-8991-4ECBF892FB82 wds:Q56894082-E56589F9-AA85-464C-AAB1-BFCB89B335AF wds:Q56894082-EE1AA01D-F721-42C8-84D8-CC0816181477 wds:Q56894082-F81BD977-E6E5-495A-8454-EE877AA317B1 wds:Q56894082-F8D893B3-AD58-4994-B70E-67CF81259957
cites work	Mammalian P4-ATPases and ABC transporters and their role in phospholipid transport Genome-wide gene expression profiling analysis of Leishmania major and Leishmania infantum developmental stages reveals substantial differences between the two species The Arabidopsis P4-ATPase ALA3 localizes to the golgi and requires a beta-subunit to function in lipid translocation and secretory vesicle formation. Heteromeric interactions required for abundance and subcellular localization of human CDC50 proteins and class 1 P4-ATPases Lem3p is essential for the uptake and potency of alkylphosphocholine drugs, edelfosine and miltefosine A novel membrane protein, Ros3p, is required for phospholipid translocation across the plasma membrane in Saccharomyces cerevisiae Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccharomyces cerevisiae Mapping functional interactions in a heterodimeric phospholipid pump Cdc50p plays a vital role in the ATPase reaction cycle of the putative aminophospholipid transporter Drs2p Crystal structure of the sodium-potassium pump at 2.4 A resolution Functional roles of Na,K-ATPase subunits Mechanisms of experimental resistance of Leishmania to miltefosine: Implications for clinical use. Inactivation of the miltefosine transporter, LdMT, causes miltefosine resistance that is conferred to the amastigote stage of Leishmania donovani and persists in vivo Disruption of the lipid-transporting LdMT-LdRos3 complex in Leishmania donovani affects membrane lipid asymmetry but not host cell invasion Leishmania donovani resistance to miltefosine involves a defective inward translocation of the drug Functions of phospholipid flippases Endocytic recycling in yeast is regulated by putative phospholipid translocases and the Ypt31p/32p-Rcy1p pathway Roles for the Drs2p-Cdc50p complex in protein transport and phosphatidylserine asymmetry of the yeast plasma membrane Phospholipid flippases: building asymmetric membranes and transport vesicles. Critical role of the beta-subunit CDC50A in the stable expression, assembly, subcellular localization, and lipid transport activity of the P4-ATPase ATP8A2 Isolation and characterization of novel mutations in CDC50, the non-catalytic subunit of the Drs2p phospholipid flippase. Low plasma membrane expression of the miltefosine transport complex renders Leishmania braziliensis refractory to the drug Functional cloning of the miltefosine transporter. A novel P-type phospholipid translocase from Leishmania involved in drug resistance Phospholipid translocation and miltefosine potency require both L. donovani miltefosine transporter and the new protein LdRos3 in Leishmania parasites. Pumping lipids with P4-ATPases. Human TMEM30a promotes uptake of antitumor and bioactive choline phospholipids into mammalian cells Inter-subunit interaction of gastric H+,K+-ATPase prevents reverse reaction of the transport cycle Cdc50p, a conserved endosomal membrane protein, controls polarized growth in Saccharomyces cerevisiae The roles of the Na,K-ATPase beta 1 subunit in pump sorting and epithelial integrity CDC50 proteins are critical components of the human class-1 P4-ATPase transport machinery Mechanism and significance of P4 ATPase-catalyzed lipid transport: lessons from a Na+/K+-pump. P4 ATPases: flippases in health and disease Phosphatidylserine stimulation of Drs2p·Cdc50p lipid translocase dephosphorylation is controlled by phosphatidylinositol-4-phosphate. Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P4-ATPase complex reside in the catalytic ALA alpha-subunit Aberrant termination of reproduction-related TMEM30C transcripts in the hominoids. CDC50A plays a key role in the uptake of the anticancer drug perifosine in human carcinoma cells
author name string	wds:Q56894082-3AD23EB9-398A-4342-88FC-70F16CF77353 wds:Q56894082-7E8D9D0B-A3B8-41A0-9760-950E873E1E83
author name string	María P Sánchez-Cañete Sebastián García-Sánchez
rdfs:label	Functional role of evolutionarily highly conserved residues, N-glycosylation level and domains of the Leishmania miltefosine transporter-Cdc50 subunit (en) Functional role of evolutionarily highly conserved residues, N-glycosylation level and domains of the Leishmania miltefosine transporter-Cdc50 subunit (nl)
skos:prefLabel	Functional role of evolutionarily highly conserved residues, N-glycosylation level and domains of the Leishmania miltefosine transporter-Cdc50 subunit (en) Functional role of evolutionarily highly conserved residues, N-glycosylation level and domains of the Leishmania miltefosine transporter-Cdc50 subunit (nl)
name	Functional role of evolutionarily highly conserved residues, N-glycosylation level and domains of the Leishmania miltefosine transporter-Cdc50 subunit (en) Functional role of evolutionarily highly conserved residues, N-glycosylation level and domains of the Leishmania miltefosine transporter-Cdc50 subunit (nl)
author	wds:Q56894082-40624371-956A-43A9-A625-275AD47EAEEC wds:Q56894082-B657DF4B-B9A6-407D-9F68-55A778C02891
author	Francisco Gamarro Santiago Castanys
title	wds:Q56894082-0F67DCAD-2833-416F-802D-6681734D8AE2
title	Functional role of evolutionarily highly conserved residues, N-glycosylation level and domains of the Leishmania miltefosine transporter-Cdc50 subunit (en)
page(s)	wds:Q56894082-8E07C3AC-1DE5-40D3-A0EB-A21B440DC56F
page(s)	83-94

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