Very high single channel water permeability of aquaporin-4 in baculovirus-infected insect cells and liposomes reconstituted with purified aquaporin-4.
about
The Trafficking of the Water Channel Aquaporin-2 in Renal Principal Cells-a Potential Target for Pharmacological Intervention in Cardiovascular DiseasesMolecular pathophysiology of cerebral edemaAquaporin-4 is expressed in basolateral membranes of proximal tubule S3 segments in mouse kidneyAquaporin-4 dynamics in orthogonal arrays in live cells visualized by quantum dot single particle tracking.Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imagingReconstitution of water channel function of an aquaporin overexpressed and purified from Pichia pastoris.Cloning of an aquaporin-like cDNA and in situ hybridization in adults of the mosquito Aedes aegypti (Diptera: Culicidae).Preparative scale production of functional mouse aquaporin 4 using different cell-free expression modes.Aquaporins: important but elusive drug targets.Structure and function of aquaporin water channels.Aquaporin-4: orthogonal array assembly, CNS functions, and role in neuromyelitis optica.Liquid-vapor oscillations of water in hydrophobic nanoporesAquaporin-4 Mz isoform: brain expression, supramolecular assembly and neuromyelitis optica antibody binding.Clinical update on renal aquaporins.Water permeability of aquaporin-4 channel depends on bilayer composition, thickness, and elasticityLive-cell imaging of aquaporin-4 diffusion and interactions in orthogonal arrays of particles.Neuromyelitis optica IgG does not alter aquaporin-4 water permeability, plasma membrane M1/M23 isoform content, or supramolecular assembly.Peptide-stimulation enhances compartmentalization and the catalytic activity of lung endothelial NOS.The Water Permeability and Pore Entrance Structure of Aquaporin-4 Depend on Lipid Bilayer Thickness.The water permeability of lens aquaporin-0 depends on its lipid bilayer environment.Vasopressin-induced differential stimulation of AQP4 splice variants regulates the in-membrane assembly of orthogonal arrays.Regulation of Na,K-ATPase subunit abundance by translational repression.Expression of aquaporin-4 in fast-twitch fibers of mammalian skeletal muscle.Reversible, temperature-dependent supramolecular assembly of aquaporin-4 orthogonal arrays in live cell membranesSpatial model of convective solute transport in brain extracellular space does not support a "glymphatic" mechanism.Live cell analysis of aquaporin-4 m1/m23 interactions and regulated orthogonal array assembly in glial cells.Molecular cloning, overexpression and characterization of a novel water channel protein from Rhodobacter sphaeroides.Overexpression of aquaporin 4 in articular chondrocytes exacerbates the severity of adjuvant-induced arthritis in rats: an in vivo and in vitro study.Site-directed chemical labeling of extracellular loops in a membrane protein. The topology of the Na,K-ATPase alpha-subunit.Evidences for a leaky scanning mechanism for the synthesis of the shorter M23 protein isoform of aquaporin-4: implication in orthogonal array formation and neuromyelitis optica antibody interaction.Desformylgramicidin: a model channel with an extremely high water permeability.Activation of large conductance sodium channels upon expression of amiloride-sensitive sodium channel in Sf9 insect cells.Large-scale purification of functional recombinant human aquaporin-2.Heterologous expression of Na(+)-K(+)-ATPase in insect cells: intracellular distribution of pump subunits.Characterization of N-glycosylation consensus sequences in the Kv3.1 channel.Mosquito (Aedes aegypti ) aquaporin, present in tracheolar cells, transports water, not glycerol, and forms orthogonal arrays in Xenopus oocyte membranes.The aquaporin-4 water channel as a potential drug target in neurological disorders.Developmental expression and biophysical characterization of a Drosophila melanogaster aquaporin.Enhanced water permeability and tunable ion selectivity in subnanometer carbon nanotube porins.Mercury chloride decreases the water permeability of aquaporin-4-reconstituted proteoliposomes.
P2860
Q26768170-3BB0454B-0F83-492D-835F-7905DA7B634DQ26776371-7D8EB3B3-2E00-4AA5-9162-5F4BD4756EBAQ28507979-BB2B4D5E-0321-4D5C-8E37-806FA42FAECAQ30482870-C21D2EE8-6B1C-49C5-9962-591B88A89699Q30488992-72D6450A-A357-496F-9A40-260AC2613FB4Q30765426-DC8231EE-BCC7-4697-94D2-9DB00407C9CCQ30917363-D8FC620F-2397-4142-B0CF-3F71146BA882Q33707547-DC1C6D59-CE66-4287-A199-C536CD9332A3Q33792739-C006F15C-80C1-41F8-9FCE-8E977023C731Q33822585-A914B3FB-0857-43A4-95CC-B14A65EEA49EQ33892339-A94863EE-0345-4BC9-843E-53AE05BE6F08Q35163023-5C126522-1550-44C4-8A41-E22DC7C25957Q35892159-71E6D792-C58D-4E6B-84DC-63B8AB2BFB84Q36131354-82C8E0E6-4990-43FC-BFD5-02380D339D17Q36379107-5AE92DE5-6072-4102-9CE2-68CF668239C5Q36650364-911DCB6C-815A-4143-BA5A-A54AEFE9EE5AQ36650382-49F6A74A-05F9-4013-B4AB-7E8112535B47Q37013469-A52F21B2-374F-4250-92B8-2AE33B4A83EBQ37094379-7E04E9E2-4E8C-43F0-A756-8B54343F3E27Q37166334-7FC1EC3D-A7F4-4B96-B1DF-78D1098813D3Q37216875-1A7F1D23-21AA-4B9E-A231-28E24DFBFABFQ37371682-3C5AFB6A-3D4C-4AA4-A703-6C1F7BB11FDBQ37384444-6D63C9D4-C249-4DA5-89E1-CBC510CC3211Q37443850-DE7F6C78-F493-4C53-8E79-7194D91361F8Q37457029-CF3F19A5-2002-40DF-9A18-CE9BEB942220Q37467723-6948037B-C0DC-43C2-BDE3-B8F3B487FF35Q37538400-4A895337-650E-4346-811C-DFE5D157C189Q37676735-351FAB6A-D310-4B3F-8F5A-7C5FAD8E9772Q38313317-8F476A9A-CD64-4E17-9F70-9B864A7DBF3EQ39539421-87B7D49D-A04A-474B-A39E-DE7A110BA133Q40173545-0F6B7AE1-267E-4E23-9AE8-D76602B334A1Q40762395-4422C50C-6550-4670-B863-F5942DF021A7Q40782806-241249D4-08CC-4ADD-B90D-CADB667B5EACQ40786470-8EE455B4-14D4-4191-A640-7350085031FBQ42036961-86DC66E7-FB79-4D1A-AAC2-E7C9ABA3B26AQ43041992-DC72D0AF-D0C9-44C9-A2DB-99720AAB3A1DQ46364880-D42AE000-0E32-4247-8574-83B075C0D561Q46412516-7F28CD07-521C-4D31-825C-2DD185EA1BDAQ46496355-17F308F8-5D8E-4F2E-909B-76968E46D3ADQ46826906-3651BD86-3C73-4F44-BC33-20CD5E61405E
P2860
Very high single channel water permeability of aquaporin-4 in baculovirus-infected insect cells and liposomes reconstituted with purified aquaporin-4.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Very high single channel water ...... ted with purified aquaporin-4.
@en
type
label
Very high single channel water ...... ted with purified aquaporin-4.
@en
prefLabel
Very high single channel water ...... ted with purified aquaporin-4.
@en
P2093
P356
P1433
P1476
Very high single channel water ...... ted with purified aquaporin-4.
@en
P2093
P304
P356
10.1021/BI970231R
P407
P577
1997-06-01T00:00:00Z