About: Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation

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About: Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation Goto Sponge NotDistinct Permalink

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scientific journal article

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rdf:type	Item
description	artículu científicu espublizáu en 2002 (ast) vědecký článek publikovaný v roce 2002 (cs) 2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована у вересні 2002 (uk) 2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած (hyw) wetenschappelijk artikel (gepubliceerd op 2002/09/06) (nl) vedecký článok (publikovaný 2002/09/06) (sk) مقالة علمية (نشرت في 6-9-2002) (ar) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im September 2002 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en)
publication date	wds:Q28589584-8A25F134-FB2B-4CE5-9E00-61F1C5883134
publication date	2002-09-06 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28589584-89A4DD4F-35F1-44ED-BDF7-371B474ED8EB
language of work or name	English
author name string	wds:Q28589584-383BFF15-57D9-4D5F-93EA-385DEEBC52DB wds:Q28589584-697E72C4-9028-4CB7-8976-0273CE26B660 wds:Q28589584-870A2670-0326-4083-B818-759B4D88A3CB wds:Q28589584-9D992425-7E43-4ADC-8C83-1C869CD5E338
OpenCitations bibliographic resource ID	wds:Q28589584-2B4DACED-8437-4CCD-B46E-975357F7DABF
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/4199688
author name string	Ajit Varki Nissi M. Varki Jamey D. Marth Laura T. Martin
OpenCitations bibliographic resource ID	4199688
rdfs:label	Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation (en) Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation (nl) Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation (ast)
skos:prefLabel	Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation (en) Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation (nl) Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation (ast)
name	Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation (en) Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation (nl) Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation (ast)
title	wds:Q28589584-3D0648FB-657D-4E50-A238-A8548FF3FE67
title	Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation (en)
page(s)	wds:Q28589584-3E431F0C-D5B4-4457-8545-91506B0EC2C1
page(s)	32930–32938
instance of	wds:Q28589584-DAEB385C-9C85-41DB-9B74-ED9665CBC8FF
instance of	scholarly article
main subject	wds:Q28589584-CBB50FB0-0CBA-4D0E-8BBE-E782FCA58BFC wds:Q28589584-F88753D0-F42D-4C20-8480-4E4E3A2B7A95
main subject	ST3 beta-galactoside alpha-2,3-sialyltransferase 1 Beta galactoside alpha 2,6 sialyltransferase 1
PubMed ID	wds:Q28589584-EDD3F73F-EFAF-4A2C-89D5-1D45A941F73C
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12068010
PubMed ID	12068010
published in	wds:Q28589584-5913A9B8-A927-42AF-9F63-0849996992F2
published in	Journal of Biological Chemistry
issue	wds:Q28589584-CD588EBE-DEF4-47B2-BEE1-BE6432AD5BDC
volume	wds:Q28589584-D5BA06D6-222B-4DE2-9C24-6925AA00E619
issue	36
volume	277
DOI	wds:Q28589584-DC04B0E5-A968-45DC-96CE-A1897D47AD41
DOI	http://dx.doi.org/10.1074/JBC.M203362200
DOI	10.1074/JBC.M203362200
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28589584
is cites work of	Sialoadhesin-deficient mice exhibit subtle changes in B- and T-cell populations and reduced immunoglobulin M levels. Regulation of renal outer medullary potassium channel and renal K(+) excretion by Klotho Siglecs and immune regulation B cell antigen receptor signal strength and peripheral B cell development are regulated by a 9-O-acetyl sialic acid esterase Effective replication of human influenza viruses in mice lacking a major α2,6 sialyltransferase Sialic acids in human health and disease Solid-phase glycan isolation for glycomics analysis Functions and Biosynthesis of O-Acetylated Sialic Acids Influenza virus receptor specificity and cell tropism in mouse and human airway epithelial cells Sweet 'n' sour: the impact of differential glycosylation on T cell responses Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1 Structural insight into mammalian sialyltransferases Glycomics: an integrated systems approach to structure-function relationships of glycans ST6Gal-I sialyltransferase confers cisplatin resistance in ovarian tumor cells Structure-based mutagenic analysis of mechanism and substrate specificity in mammalian glycosyltransferases: porcine ST3Gal-I. Anti-inflammatory IgG production requires functional P1 promoter in β-galactoside α2,6-sialyltransferase 1 (ST6Gal-1) gene Terminal N-linked galactose is the primary receptor for adeno-associated virus 9. Role for hepatic and circulatory ST6Gal-1 sialyltransferase in regulating myelopoiesis. Human xeno-autoantibodies against a non-human sialic acid serve as novel serum biomarkers and immunotherapeutics in cancer. Systems-based candidate genes for human response to influenza infection Diversity in cell surface sialic acid presentations: implications for biology and disease Human-specific Regulation of α2–6-linked Sialic Acids Multiple changes in sialic acid biology during human evolution A phenotype survey of 36 mutant mouse strains with gene-targeted defects in glycosyltransferases or glycan-binding proteins Altered granulopoietic profile and exaggerated acute neutrophilic inflammation in mice with targeted deficiency in the sialyltransferase ST6Gal I The Tumor-Associated Glycosyltransferase ST6Gal-I Regulates Stem Cell Transcription Factors and Confers a Cancer Stem Cell Phenotype Heart disease is common in humans and chimpanzees, but is caused by different pathological processes Remodeling of marrow hematopoietic stem and progenitor cells by non-self ST6Gal-1 sialyltransferase Platelets support extracellular sialylation by supplying the sugar donor substrate Endogenous galectin-1 enforces class I-restricted TCR functional fate decisions in thymocytes Deficits in sialylation impair podocyte maturation Sialyltransferase regulates nervous system function in Drosophila Siglecs induce tolerance to cell surface antigens by BIM-dependent deletion of the antigen-reactive B cells Transcriptional profiling of human placentas from pregnancies complicated by preeclampsia reveals disregulation of sialic acid acetylesterase and immune signalling pathways. B-cell-independent sialylation of IgG. Multifaceted Role of Sialylation in Prion Diseases Metabolic Remodeling of Cell-Surface Sialic Acids: Principles, Applications, and Recent Advances Neuraminidase reprograms lung tissue and potentiates lipopolysaccharide-induced acute lung injury in mice Disruption of GM2/GD2 synthase gene resulted in overt expression of 9-O-acetyl GD3 irrespective of Tis21. Elevation of β-galactoside α2,6-sialyltransferase 1 in a fructoseresponsive manner promotes pancreatic cancer metastasis. IgG and leukocytes: Targets of immunomodulatory α2,6 sialic acids

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