Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells.
about
The Diverse Forms of Lactose Intolerance and the Putative Linkage to Several CancersTargeting of pseudorabies virus structural proteins to axons requires association of the viral Us9 protein with lipid raftsCharacterization of neuraminidases from the highly pathogenic avian H5N1 and 2009 pandemic H1N1 influenza A viruses.Polar residues and their positional context dictate the transmembrane domain interactions of influenza A neuraminidases.Human cytomegalovirus glycoprotein B contains autonomous determinants for vectorial targeting to apical membranes of polarized epithelial cells.Influenza virus assembly and lipid raft microdomains: a role for the cytoplasmic tails of the spike glycoproteins.Trafficking to the apical and basolateral membranes in polarized epithelial cellsCarbohydrate-mediated Golgi to cell surface transport and apical targeting of membrane proteins.Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 proteinPlasma membrane rafts play a critical role in HIV-1 assembly and release.Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Parvovirus infection of cells by using variants of the feline transferrin receptor altering clathrin-mediated endocytosis, membrane domain localization, and capsid-binding domains.Polarized sorting and trafficking in epithelial cellsAsymmetric requirement for cholesterol in receptor-bearing but not envelope-bearing membranes for fusion mediated by ecotropic murine leukemia virusIndependent segregation of human immunodeficiency virus type 1 Gag protein complexes and lipid rafts.The evolutionary pattern of glycosylation sites in influenza virus (H5N1) hemagglutinin and neuraminidase.The cytoplasmic tail of the influenza A virus M2 protein plays a role in viral assembly.Raft-mediated trafficking of apical resident proteins occurs in both direct and transcytotic pathways in polarized hepatic cells: role of distinct lipid microdomainsReovirus FAST protein transmembrane domains function in a modular, primary sequence-independent manner to mediate cell-cell membrane fusion.Rafts promote assembly and atypical targeting of a nonenveloped virus, rotavirus, in Caco-2 cellsA comprehensive map of the influenza A virus replication cycleAP1B sorts basolateral proteins in recycling and biosynthetic routes of MDCK cells.Residues in the hendra virus fusion protein transmembrane domain are critical for endocytic recyclingAssociation of influenza virus NP and M1 proteins with cellular cytoskeletal elements in influenza virus-infected cells.Rotavirus is released from the apical surface of cultured human intestinal cells through nonconventional vesicular transport that bypasses the Golgi apparatus.Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cellsCaveolin transfection results in caveolae formation but not apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins in epithelial cells.A transmembrane segment determines the steady-state localization of an ion-transporting adenosine triphosphataseRaft association of SNAP receptors acting in apical trafficking in Madin-Darby canine kidney cells.Mapping the sequence mutations of the 2009 H1N1 influenza A virus neuraminidase relative to drug and antibody binding sites.Role of the terminal domains in sodium channel localization.Taking the scenic route: biosynthetic traffic to the plasma membrane in polarized epithelial cellsThe basolateral targeting signal of CD147 (EMMPRIN) consists of a single leucine and is not recognized by retinal pigment epithelium.Specific nucleoprotein residues affect influenza virus morphology.Role of lipids on entry and exit of bluetongue virus, a complex non-enveloped virusGlycosylation increases the thermostability of human aquaporin 10 protein.Detergent-insoluble GPI-anchored proteins are apically sorted in fischer rat thyroid cells, but interference with cholesterol or sphingolipids differentially affects detergent insolubility and apical sorting.Structural and functional analysis of endosomal compartments in epithelial cells.Influenza A virus hemagglutinin and neuraminidase mutually accelerate their apical targeting through clustering of lipid rafts.Palmitoylation is required for intracellular trafficking of influenza B virus NB protein and efficient influenza B virus growth in vitro.
P2860
Q26783628-50612CCD-B3F8-477A-9E61-D33A658D7AB8Q27318720-C64A7069-E2FA-4A7A-B2B5-9E8185D04674Q30398292-B0EF25C6-523F-47B3-8CA8-9260A859BD14Q30427691-2654BD0C-DF08-4D61-9E3C-B8ECFA62D4B8Q32041819-AE17A8A5-1E22-4057-8C2B-7D1AD4F5C3BDQ33804501-56B952D8-C3A9-4BD6-A513-2FFF815527BEQ33814910-3E44BF76-9BFB-449E-BAE4-8CC7FB7EEC5CQ33888566-60D50471-6C66-405F-A7AB-E4E9E9D778A7Q33914921-6971F02E-3AA3-4B09-ABB1-EF96C5091B61Q33950207-700042AB-D75D-483D-97AC-7A8FA8E54098Q34102261-1AE3E8AF-CD5C-4D47-8030-764AD5DA0A9DQ34150166-08319ED9-4E8E-49DF-874E-8C6722FBCC02Q34270230-925310E1-401A-4CCD-81A8-81929AD43AE4Q34341238-9C4F39F8-7766-4075-B015-62C75826FE28Q34466295-DB976827-4B64-4E7F-9236-36009CCF0BC6Q34469957-9C66BB76-6505-4BC8-8EDC-34F1515C5372Q34648238-208917BB-2496-4FD0-ACA4-AB9AFFDC52B5Q34764402-0A7B0CFD-E8B4-4052-9E91-9E7A7A4029FBQ34917410-7A0C4301-D65F-442A-A442-1CD584044172Q34998942-B4AD43BB-6F05-46F7-80D5-AD574D51F932Q35006697-BB2CC131-54FE-4A06-B56D-D46EFA1C683EQ35616362-CDF6A644-C5DD-44A6-9A58-1216871223E7Q35826217-703AA4DE-EBA8-403A-B79E-FDF42F0B3345Q35880794-5C49E043-83DB-46C6-8264-825CBEB2C87EQ35898075-14FB3EDD-9A3B-4858-841A-B9CF063F4C90Q36256212-A8EAC789-2C35-425F-9CC4-A6C0F466C625Q36274909-F124A878-C28C-4AD5-83B8-A2807F42BE39Q36316378-77A21E21-07C3-4318-AF2D-D3DA79A44BBCQ36450084-94864ECA-FFE2-4AFE-B9D7-9132B3904561Q37215150-7A6D6D9E-8003-4B29-A061-88BCF72FD8D4Q37448824-08B4AF73-0FED-4D5A-82EE-97214F67210DQ37488634-07483254-D641-4EB5-B897-BBA089B10652Q37497050-A04B7048-7D2C-4E8B-A7F1-3F8228DDA887Q37547146-D142C199-18AE-4494-8ED5-83886895F635Q37945206-FFA37F8D-AA03-481C-B19B-F082ABF5E036Q38418857-6982128E-4BAB-4D1B-959B-0C042CE15964Q38478806-75AD3E94-41CB-40E5-8C9F-9793C8EECD11Q38584800-FAE77855-B4C7-44DC-B9AA-ACBA78D2A85DQ38981236-287B34C8-AE9C-4C73-AE3C-8CF3F65DDA54Q39222038-6831711A-C103-4951-92AC-623031DFEA78
P2860
Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Transmembrane domain of influe ...... ignal in polarized MDCK cells.
@ast
Transmembrane domain of influe ...... ignal in polarized MDCK cells.
@en
type
label
Transmembrane domain of influe ...... ignal in polarized MDCK cells.
@ast
Transmembrane domain of influe ...... ignal in polarized MDCK cells.
@en
prefLabel
Transmembrane domain of influe ...... ignal in polarized MDCK cells.
@ast
Transmembrane domain of influe ...... ignal in polarized MDCK cells.
@en
P2093
P2860
P1433
P1476
Transmembrane domain of influe ...... signal in polarized MDCK cells
@en
P2093
C M Sanderson
R T Avalos
P2860
P304
P407
P577
1996-09-01T00:00:00Z