Results 91 to 100 of about 37,468 (260)
Objective To characterize Fc‐glycosylation profiles in patients with anti‐N‐methyl‐D‐aspartate receptor encephalitis (NMDARe) and assess their association with antibody compartmentalization (cerebrospinal fluid [CSF] vs serum), disease triggers (viral, tumor‐related or idiopathic), and 1‐year outcomes.
Laura Marmolejo +16 more
wiley +1 more source
O-GlcNAc and the Epigenetic Regulation of Gene Expression [PDF]
O-GlcNAcylation is an abundant nutrient-driven modification linked to cellular signaling and regulation of gene expression. Utilizing precursors derived from metabolic flux, O-GlcNAc functions as a homeostatic regulator. The enzymes of O-GlcNAc cycling, OGT and O-GlcNAcase, act in mitochondria, the cytoplasm, and the nucleus in association with ...
Brian A, Lewis, John A, Hanover
openaire +2 more sources
O-GlcNAc profiling: from proteins to proteomes [PDF]
O-linked β-D-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) onto serine and threonine residues of proteins is an important post-translational modification (PTM), which is involved in many crucial biological processes including transcription, translation, proteasomal degradation, and signal transduction.
Ma, Junfeng, Hart, Gerald W
openaire +2 more sources
Synergistische Entwicklungsstrategien von Inhibitoren gegen humane UDP‐Galactose‐4‐Epimerase
Die Epimerase GalE ist essenziell für die Biosynthese von krebsrelevanten O‐GalNAc Glykanen. Wir verwenden orthogonales, strukturbasiertes Screening niedermolekularer Fragmente an, um kovalente und nichtkovalente Inhibitoren gegen GalE mit nicht mehr als 22 optimierten Verbindungen zu erhalten.
William M. Browne +22 more
wiley +1 more source
A Synergistic Inhibitor Development Strategy Against Human UDP‐Galactose‐4‐Epimerase
The epimerase GalE is crucial for the biosynthesis of cancer‐relevant O‐GalNAc glycans. Here, we employ orthogonal, structurally enabled small molecule fragment screens to yield both covalent and non‐covalent inhibitors against GalE within no more than 22 elaborated compounds.
William M. Browne +22 more
wiley +1 more source
Epidermal growth factor receptors: function modulation by phosphorylation and glycosylation interplay [PDF]
Post-translational modifications (PTMs) of proteins induce structural and functional changes that are most often transitory and difficult to follow and investigate invivo.
Ahmad, Ishtiaq +6 more
core
Nutrient sensor O-GlcNAc transferase controls cancer lipid metabolism via SREBP-1 regulation [PDF]
Elevated O-GlcNAcylation is associated with disease states such as diabetes and cancer. O-GlcNAc transferase (OGT) is elevated in multiple cancers and inhibition of this enzyme genetically or pharmacologically inhibits oncogenesis.
Bacigalupa, Zachary A. +8 more
core +1 more source
O‐GlcNAc cycling and Epigenetics
The nutrient‐sensing hexosamine signaling pathway terminating in O‐GlcNAc cycling is emerging as a key epigenetic regulator of gene expression in mammals. Mounting evidence suggests that OGlcNAc cycling sits atop a robust regulatory network maintaining higher‐order chromatin structure and epigenetic memory.
John A Hanover +7 more
openaire +1 more source
O-GlcNAc cycling: Implications for neurodegenerative disorders [PDF]
The dynamic post-translational modification of proteins by O-linked N-acetylglucosamine (O-GlcNAc), termed O-GlcNAcylation, is an important mechanism for modulating cellular signaling pathways. O-GlcNAcylation impacts transcription, translation, organelle trafficking, proteasomal degradation and apoptosis.
Brooke D, Lazarus +2 more
openaire +2 more sources
O-GlcNAcase (OGA) is the only enzyme responsible for removing N-acetyl glucosamine (GlcNAc) attached to serine and threonine residues on proteins. This enzyme plays a key role in O-GlcNAc metabolism.
Shanshan Li +13 more
doaj +1 more source

