Evidence for covalent attachment of fatty acids to Sindbis virus glycoproteins. - Wikidata - wikimedia - TriplyDB

Evidence for covalent attachment of fatty acids to Sindbis virus glycoproteins.

Evidence for covalent attachment of fatty acids to Sindbis virus glycoproteins.

http://www.wikidata.org/entity/Q37326763

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Purified membrane and soluble folate binding proteins from cultured KB cells have similar amino acid compositions and molecular weights but differ in fatty acid acylation n-Tetradecanoyl is the NH2-terminal blocking group of the catalytic subunit of cyclic AMP-dependent protein kinase from bovine cardiac muscle Adaptive mutations in Sindbis virus E2 and Ross River virus E1 that allow efficient budding of chimeric viruses Functional characterization of the Sindbis virus E2 glycoprotein by transposon linker-insertion mutagenesis Site-directed mutations in the Sindbis virus E2 glycoprotein identify palmitoylation sites and affect virus budding Effect of actinomycin D and cycloheximide on replication of Sindbis virus in Aedes albopictus (mosquito) cells A structural and functional perspective of alphavirus replication and assembly The alphaviruses: gene expression, replication, and evolution Processing and fatty acid acylation of RAS1 and RAS2 proteins in Saccharomyces cerevisiae.All about that fat: Lipid modification of proteins in Cryptococcus neoformans Fatty acid acylation of lens fiber plasma membrane proteins Nucleotide sequence of the 26S mRNA of Sindbis virus and deduced sequence of the encoded virus structural proteins The peptide hormone ghrelin binds to membrane-mimetics via its octanoyl chain and an adjacent phenylalanine.Dynamic palmitoylation and the role of DHHC proteins in T cell activation and anergy.The human and simian immunodeficiency virus envelope glycoprotein transmembrane subunits are palmitoylated.Two classes of fatty acid acylated proteins exist in eukaryotic cells.Lipoprotein nature of Bacillus licheniformis membrane penicillinase Ankyrin is fatty acid acylated in erythrocytes Synthesis and incorporation of myelin polypeptides into CNS myelin.Mutations in the cytoplasmic domain of the influenza virus hemagglutinin affect different stages of intracellular transport.The presence of cysteine in the cytoplasmic domain of the vesicular stomatitis virus glycoprotein is required for palmitate addition Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion.Acylated proteins in Acholeplasma laidlawii Distribution of virus structural proteins and protein-protein interactions in plasma membrane of baby hamster kidney cells infected with Sindbis or vesicular stomatitis virus.Unique regulatory properties of the type 2a Ca2+ channel beta subunit caused by palmitoylation.Fatty acid acylation of vaccinia virus proteins.Posttranslational processing of p21 ras proteins involves palmitylation of the C-terminal tetrapeptide containing cysteine-186 Myristylation is required for intracellular transport but not for assembly of D-type retrovirus capsids.Myristic acid, a rare fatty acid, is the lipid attached to the transforming protein of Rous sarcoma virus and its cellular homolog.Acylation of the 176R (19-kilodalton) early region 1B protein of human adenovirus type 5.Fatty acid modification of Newcastle disease virus glycoproteins.Fatty acid-acylated proteins in secretory mutants of Saccharomyces cerevisiae Myristic acid is attached to the transforming protein of Rous sarcoma virus during or immediately after synthesis and is present in both soluble and membrane-bound forms of the protein.Chemical approaches for profiling dynamic palmitoylation Fat chance! Getting a grip on a slippery modification.Palmitoylation of Sindbis Virus TF Protein Regulates Its Plasma Membrane Localization and Subsequent Incorporation into Virions.Disentangling the Frames, the State of Research on the Alphavirus 6K and TF Proteins.Acylation of viral and eukaryotic proteins.Protein lipid modifications--More than just a greasy ballast.The covalent modification of eukaryotic proteins with lipid.

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P2860

Evidence for covalent attachment of fatty acids to Sindbis virus glycoproteins.

http://www.wikidata.org/entity/Q37326763

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on April 1979

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Evidence for covalent attachment of fatty acids to Sindbis virus glycoproteins.

@en

Evidence for covalent attachment of fatty acids to Sindbis virus glycoproteins.

@nl

type

label

Evidence for covalent attachment of fatty acids to Sindbis virus glycoproteins.

@en

Evidence for covalent attachment of fatty acids to Sindbis virus glycoproteins.

@nl

prefLabel

Evidence for covalent attachment of fatty acids to Sindbis virus glycoproteins.

@en

Evidence for covalent attachment of fatty acids to Sindbis virus glycoproteins.

@nl

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Proceedings of the National Academy of Sciences of the United States of America

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Evidence for covalent attachment of fatty acids to Sindbis virus glycoproteins.

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Bracha M

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Schlesinger MJ

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Schmidt MF

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P2860

Protein measurement with the Folin phenol reagent

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A simple method for the isolation and purification of total lipides from animal tissues

A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels

Tunicamycin inhibits glycosylation and multiplication of Sindbis and vesicular stomatitis viruses.

Purification and composition of the proteins from Sindbis virus grown in chick and BHK cells.

Enzymatic iodination of Sindbis virus proteins.

Cleavage of a viral envelope precursor during the morphogenesis of Sindbis virus.

Glycoproteins of Sindbis virus: priliminary characterization of the oligosaccharides

Amino-terminal sequence analysis of the structural proteins of Sindbis virus.

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1687-1691

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scholarly article

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10.1073/PNAS.76.4.1687

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4

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287008

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