Results 11 to 20 of about 37,468 (260)

A Conserved Splicing Silencer Dynamically Regulates O-GlcNAc Transferase Intron Retention and O-GlcNAc Homeostasis [PDF]

open access: yesCell Reports, 2017
Summary: Modification of nucleocytoplasmic proteins with O-GlcNAc regulates a wide variety of cellular processes and has been linked to human diseases.
Sung-Kyun Park   +2 more
exaly   +5 more sources

Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats [PDF]

open access: yesOpen Biology, 2017
O-linked N-acetylglucosamine (O-GlcNAc) is an essential and dynamic post-translational modification found on hundreds of nucleocytoplasmic proteins in metazoa.
Karim Rafie   +2 more
exaly   +2 more sources

Small molecule splicing modulators that disrupt O-GlcNAc homeostasis [PDF]

open access: yesNature Communications
O-Linked N-acetylglucosamine (O-GlcNAc) is a nucleocytoplasmic post-translational modification that is tightly regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
Steven S. Cheng   +10 more
doaj   +2 more sources

O-GlcNAcase Expression is Sensitive to Changes in O-GlcNAc Homeostasis

open access: yesFrontiers in Endocrinology, 2014
O-linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification involving an attachment of a single β-N-acetylglucosamine moiety to serine or threonine residues in nuclear and cytoplasmic proteins.
Zhen Zhang   +2 more
exaly   +3 more sources

O-GlcNAc modification: why so intimately associated with phosphorylation? [PDF]

open access: yesCell Communication and Signaling, 2011
Post-translational modification of proteins at serine and threonine side chains by β-N-acetylglucosamine (O-GlcNAc) mediated by the enzyme β-N-acetylglucosamine transferase has been emerging as a fundamental regulatory mechanism encompassing a wide range
Ande Sudharsana R   +2 more
doaj   +3 more sources

Identification and characterization of O-GlcNAc modifications of a conserved orthopoxvirus core protein [PDF]

open access: yesJournal of Virology
O-GlcNAcylation, a post-translational modification consisting of O-linked N-acetylglucosamine attached to serine and threonine residues, occurs in thousands of cytoplasmic, nuclear, and mitochondrial proteins but has been reported for relatively few ...
Yunliang Zhang, Bernard Moss
doaj   +2 more sources

Functional genomic profiling of O-GlcNAc reveals its context-specific interplay with RNA polymerase II [PDF]

open access: yesGenome Biology
Background How reversible glycosylation of DNA-bound proteins acts on transcription remains scarcely understood. O-linked β-N-acetylglucosamine (O-GlcNAc) is the only known form of glycosylation modifying nuclear proteins, including RNA polymerase II ...
Sofia Rucli   +6 more
doaj   +2 more sources

The post-translational modification O-GlcNAc is a sensor and regulator of metabolism [PDF]

open access: yesOpen Biology
Cells must rapidly adapt to changes in nutrient conditions through responsive signalling cascades to maintain homeostasis. One of these adaptive pathways results in the post-translational modification of proteins by O-GlcNAc.
Murielle M. Morales, Matthew R. Pratt
doaj   +2 more sources

Time-resolved multiomics profiling reveals chromatin O-GlcNAc modification promotes senescence-associated transcriptional program [PDF]

open access: yesNature Communications
O-GlcNAc modification is a key cellular signal, but its role in regulating senescence-associated transcription remains poorly understood. Here, we apply a time-resolved chemical genomics strategy to map dynamic O-GlcNAc chromatin-associated proteins ...
Nana Zhang   +18 more
doaj   +2 more sources

O-GlcNAc impacts mitophagy via the PINK1-dependent pathway [PDF]

open access: yesFrontiers in Aging Neuroscience
BackgroundThe accumulation of dysfunctional mitochondria is an early feature of Alzheimer’s disease (AD). The impaired turnover of damaged mitochondria increases reactive oxygen species production and lowers ATP generation, leading to cellular toxicity ...
Ibtihal M. Alghusen   +16 more
doaj   +2 more sources

Home - About - Disclaimer - Privacy