Polarized expression of a chimeric protein in which the transmembrane and cytoplasmic domains of the influenza virus hemagglutinin have been replaced by those of the vesicular stomatitis virus G protein.

Polarized expression of a chimeric protein in which the transmembrane and cytoplasmic domains of the influenza virus hemagglutinin have been replaced by those of the vesicular stomatitis virus G protein.

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http://www.wikidata.org/entity/Q37410696

Q37410696

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Intracellular localization of the viral polymerase proteins in cells infected with influenza virus and cells expressing PB1 protein from cloned cDNA A sorting signal for the basolateral delivery of the vesicular stomatitis virus (VSV) G protein lies in its luminal domain: analysis of the targeting of VSV G-influenza hemagglutinin chimeras.The internalization signal and the phosphorylation site of transferrin receptor are distinct from the main basolateral sorting information.Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells.Rotavirus is released from the apical surface of cultured human intestinal cells through nonconventional vesicular transport that bypasses the Golgi apparatus.The M protein of vesicular stomatitis virus associates specifically with the basolateral membranes of polarized epithelial cells independently of the G protein.Distinct transport vesicles mediate the delivery of plasma membrane proteins to the apical and basolateral domains of MDCK cells.The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells.An ion-transporting ATPase encodes multiple apical localization signals.An internal deletion in the cytoplasmic tail reverses the apical localization of human NGF receptor in transfected MDCK cells.An endogenous MDCK lysosomal membrane glycoprotein is targeted basolaterally before delivery to lysosomes.Analysis of the signals for polarized transport of influenza virus (A/WSN/33) neuraminidase and human transferrin receptor, type II transmembrane proteins.Possible involvement of microtubule disruption in bipolar budding of a Sendai virus mutant, F1-R, in epithelial MDCK cells.Cell surface transport, oligomerization, and endocytosis of chimeric type II glycoproteins: role of cytoplasmic and anchor domains Expression of the human immunodeficiency virus envelope glycoprotein is restricted to basolateral surfaces of polarized epithelial cells.Signal processing, glycosylation, and secretion of mutant hemagglutinins of a human influenza virus by Saccharomyces cerevisiae.Syncytium formation by recombinant vaccinia viruses carrying bovine parainfluenza 3 virus envelope protein genes.The transmembrane domain of the respiratory syncytial virus F protein is an orientation-independent apical plasma membrane sorting sequence.A single amino acid change in the cytoplasmic domains of measles virus glycoproteins H and F alters targeting, endocytosis, and cell fusion in polarized Madin-Darby canine kidney cells.TGN38 is maintained in the trans-Golgi network by a tyrosine-containing motif in the cytoplasmic domain Tyrosine-based membrane protein sorting signals are differentially interpreted by polarized Madin-Darby canine kidney and LLC-PK1 epithelial cells.Polarized apical targeting directed by the signal/anchor region of simian virus 5 hemagglutinin-neuraminidase.Regulation of targeting signals in membrane proteins. [review]A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin.Thy-1 expresses two signals for apical localization in epithelial cells.

P2860

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P2860

Polarized expression of a chimeric protein in which the transmembrane and cytoplasmic domains of the influenza virus hemagglutinin have been replaced by those of the vesicular stomatitis virus G protein.

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http://www.wikidata.org/entity/Q37410696

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article científic

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article scientifique

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artigo científico

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bilimsel makale

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scientific article published on December 1986

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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