About: Complexity and Diversity of the Mammalian Sialome Revealed by Nidovirus Virolectins

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Complexity and Diversity of the Mammalian Sialome Revealed by Nidovirus Virolectins Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Complexity and Diversity of the Mammalian Sialome Revealed by Nidovirus Virolectins
Creator	Yu, Hai Chen, Xi Padler-Karavani, Vered Varki, Ajit Langereis, Martijn Heesters, Balthasar Bakkers, Mark Boot, Willemijn De Groot, Raoul De Poot, Stefanie Deng, Lingquan Gerwig, Gerrit Huizinga, Eric Hulswit, Ruben Kamerling, Johannis Marie Van Ederen, Anne Van Der Loos, Chris Van Kuppeveld, Frank Van Vliet, Arno Vervoort, Stephin
source	Elsevier; Medline; PMC
abstract	Sialic acids (Sias), 9-carbon-backbone sugars, are among the most complex and versatile molecules of life. As terminal residues of glycans on proteins and lipids, Sias are key elements of glycotopes of both cellular and microbial lectins and thus act as important molecular tags in cell recognition and signaling events. Their functions in such interactions can be regulated by post-synthetic modifications, the most common of which is differential Sia-O-acetylation (O-Ac-Sias). The biology of O-Ac-Sias remains mostly unexplored, largely because of limitations associated with their specific in situ detection. Here, we show that dual-function hemagglutinin-esterase envelope proteins of nidoviruses distinguish between a variety of closely related O-Ac-Sias. By using soluble forms of hemagglutinin-esterases as lectins and sialate-O-acetylesterases, we demonstrate differential expression of distinct O-Ac-sialoglycan populations in an organ-, tissue- and cell-specific fashion. Our findings indicate that programmed Sia-O-acetylation/de-O-acetylation may be critical to key aspects of cell development, homeostasis, and/or function.
has issue date	2015-06-18(xsd:dateTime)
bibo:doi	10.1016/j.celrep.2015.05.044
bibo:pmid	26095364
has license	cc-by-nc-nd
sha1sum (hex)	d733c0afa475ed9c4f57c2540c0353d36cbc58e3
schema:url	https://doi.org/10.1016/j.celrep.2015.05.044
resource representing a document's title	Complexity and Diversity of the Mammalian Sialome Revealed by Nidovirus Virolectins
has PubMed Central identifier	PMC5292239
has PubMed identifier	26095364
schema:publication	Cell Rep
resource representing a document's body	covid:d733c0afa475ed9c4f57c2540c0353d36cbc58e3#body_text
is schema:about of	named entity 'REVEALED' named entity 'DIVERSITY' named entity 'KEY' named entity 'CELL RECOGNITION' named entity 'MAMMALIAN' named entity 'COMPLEXITY' named entity 'ACT' named entity 'MOLECULAR' named entity 'LECTINS' named entity 'TAGS' named entity 'SIALIC ACIDS' named entity 'DIFFERENTIAL' named entity 'BACKBONE' named entity 'CELLULAR' named entity 'SIGNALING' named entity 'LIMITATIONS' named entity 'MOLECULES' named entity 'PROTEINS' named entity 'O-ACETYLATION' named entity 'INTERACTIONS' named entity 'HHS' named entity 'LARGELY' named entity 'COMMON' named entity 'MICROBIAL' named entity 'ACCESS' named entity 'FUNCTIONS' named entity 'EVENTS' named entity 'SIA' named entity 'ASSOCIATED' named entity 'PUBLIC' named entity 'TERMINAL' named entity 'LIPIDS' named entity 'REGULATED' named entity 'ELEMENTS' named entity 'CARBON' named entity 'IMPORTANT' named entity 'THEIR' named entity 'LIFE' named entity 'SUGARS' named entity 'BIOLOGY' named entity 'COMPLEX' named entity 'GLYCANS' named entity 'molecules' named entity 'microbial' named entity 'proteins' named entity 'regulated' named entity 'glycans' named entity 'limitations' named entity 'versatile' named entity 'molecular' named entity 'Complexity' named entity 'Public Access' named entity 'LUN' named entity 'Sia' named entity 'Purkinje cells' named entity 'lectins' named entity 'metastatic' named entity 'Sia' named entity 'hemagglutination' named entity 'biotin' named entity 'Sia' named entity 'IgG2'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software