about
The collapsin response mediator protein 1 (CRMP-1) and the promyelocytic leukemia zinc finger protein (PLZF) bind to UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE), the key enzyme of sialic acid biosynthesisDiversity of microbial sialic acid metabolismColloquium paper: uniquely human evolution of sialic acid genetics and biologySialic acids in the brain: gangliosides and polysialic acid in nervous system development, stability, disease, and regenerationGNE is involved in the early development of skeletal and cardiac muscleCrystal Structure of the N-Acetylmannosamine Kinase Domain of GNEGlcNAc 2-epimerase can serve a catabolic role in sialic acid metabolismHereditary inclusion body myopathy: a decade of progressNon-specific accumulation of glycosphingolipids in GNE myopathyMutation in the key enzyme of sialic acid biosynthesis causes severe glomerular proteinuria and is rescued by N-acetylmannosamineDomain-specific characteristics of the bifunctional key enzyme of sialic acid biosynthesis, UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinaseMetabolic manipulation of glycosylation disorders in humans and animal modelsPreclinical assessment of wt GNE gene plasmid for management of hereditary inclusion body myopathy 2 (HIBM2)N-glycolylneuraminic acid deficiency in mice: implications for human biology and evolutionIntravenous immune globulin in hereditary inclusion body myopathy: a pilot studyCell surface sialylation and fucosylation are regulated by L1 via phospholipase Cgamma and cooperate to modulate neurite outgrowth, cell survival and migration.Insights into the evolution of sialic acid catabolism among bacteria.Sialic acid utilisation and synthesis in the neonatal rat revisitedGanglioside GM3 levels are altered in a mouse model of HIBM: GM3 as a cellular marker of the disease.Molecular modeling of the bifunctional enzyme UDP-GlcNAc 2-epimerase/ManNAc kinase and predictions of structural effects of mutations associated with HIBM and sialuria.Effects of altered sialic acid biosynthesis on N-linked glycan branching and cell surface interactionsN-acetyl-D-mannosamine treatment alleviates age-related decline in place-learning ability in dogsMolecular diagnosis of hereditary inclusion body myopathy by linkage analysis and identification of a novel splice site mutation in GNE.An oncogenic protein Golgi phosphoprotein 3 up-regulates cell migration via sialylation.Structure, biological functions and applications of the AB5 toxins.Glycoprotein hyposialylation gives rise to a nephrotic-like syndrome that is prevented by sialic acid administration in GNE V572L point-mutant mice.Sialylation of Thomsen-Friedenreich antigen is a noninvasive blood-based biomarker for GNE myopathy.UDP-GlcNAc 2-Epimerase/ManNAc Kinase (GNE): A Master Regulator of Sialic Acid Synthesis.Perspectives on distal myopathy with rimmed vacuoles or hereditary inclusion body myopathy: contributions from an animal model. Lack of sialic acid, a central determinant in sugar chains, causes myopathy?Specific lectin biomarkers for isolation of human pluripotent stem cells identified through array-based glycomic analysisST3GAL3 mutations impair the development of higher cognitive functions.Mutation update for GNE gene variants associated with GNE myopathy.A proteome signature for intrauterine growth restriction derived from multifactorial analysis of mass spectrometry-based cord blood serum profiling.Evidences for the involvement of cell surface glycans in stem cell pluripotency and differentiation.A preclinical trial of sialic acid metabolites on distal myopathy with rimmed vacuoles/hereditary inclusion body myopathy, a sugar-deficient myopathy: a review.A novel missense mutation in the GNE gene in an Iranian patient with hereditary inclusion body myopathy.The CMP-sialic acid transporter is localized in the medial-trans Golgi and possesses two specific endoplasmic reticulum export motifs in its carboxyl-terminal cytoplasmic tail.Atypical presentation of GNE myopathy with asymmetric hand weakness.Systemic blockade of sialylation in mice with a global inhibitor of sialyltransferases.Transcript analysis of stem cells
P2860
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P2860
description
2002 nî lūn-bûn
@nan
2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Sialylation is essential for early development in mice.
@ast
Sialylation is essential for early development in mice.
@en
Sialylation is essential for early development in mice.
@nl
type
label
Sialylation is essential for early development in mice.
@ast
Sialylation is essential for early development in mice.
@en
Sialylation is essential for early development in mice.
@nl
prefLabel
Sialylation is essential for early development in mice.
@ast
Sialylation is essential for early development in mice.
@en
Sialylation is essential for early development in mice.
@nl
P2093
P2860
P356
P1476
Sialylation is essential for early development in mice.
@en
P2093
Elvira Rohde
Ivan Horak
Klaus-Peter Knobeloch
Lothar Lucka
Martina Schwarzkopf
Nicola Wiechens
Rüdiger Horstkorte
Stephan Hinderlich
Werner Reutter
P2860
P304
P356
10.1073/PNAS.072066199
P407
P577
2002-04-02T00:00:00Z