Results 81 to 90 of about 14,068 (233)

Increasing O-GlcNAcylation level on organ culture of soleus modulates the calcium activation parameters of muscle fibers. [PDF]

open access: yesPLoS ONE, 2012
O-N-acetylglucosaminylation is a reversible post-translational modification which presents a dynamic and highly regulated interplay with phosphorylation.
Caroline Cieniewski-Bernard   +3 more
doaj   +1 more source

Protein O-GlcNAcylation in Metabolic Modulation of Skeletal Muscle: A Bright but Long Way to Go

open access: yesMetabolites, 2022
O-GlcNAcylation is an atypical, dynamic and reversible O-glycosylation that is critical and abundant in metazoan. O-GlcNAcylation coordinates and receives various signaling inputs such as nutrients and stresses, thus spatiotemporally regulating the ...
Yang Liu, Yajie Hu, Shize Li
doaj   +1 more source

Hyperphosphorylation-Induced Tau Oligomers [PDF]

open access: yes, 2013
In normal adult brain the microtubule associated protein (MAP) tau contains 2–3 phosphates per mol of the protein and at this level of phosphorylation it is a soluble cytosolic protein.
Cheng-Xin Gong, Fei Liu, Khalid Iqbal
core   +2 more sources

O‐GlcNAcylation of KAT2A Enhances Bladder Cancer Proliferation by Inhibiting the KAT2A‐TRIM22 Interaction

open access: yesCancer Science, EarlyView.
Lysine acetyltransferase 2A (KAT2A) is a transcriptional coactivator and a member of the Histone Acetyltransferase (HAT) family. While altered KAT2A activity has been implicated in various cancers, its role in bladder cancer (BLCA) remains poorly understood.
Wenjie Yang   +8 more
wiley   +1 more source

Nucleocytoplasmic human O-GlcNAc transferase is sufficient for O-GlcNAcylation of mitochondrial proteins [PDF]

open access: yes, 2016
O-linked N-acetylglucosamine modification (O-GlcNAcylation) is a nutrient-dependent protein post-translational modification (PTM), dynamically and reversibly driven by two enzymes: O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyse the ...
Akimoto   +56 more
core   +3 more sources

Biogenesis of TNF‐α‐insights into proteostasis and inflammation

open access: yesThe FEBS Journal, EarlyView.
TNF‐α biogenesis, trafficking, and signalling are tightly and reciprocally coupled to cellular proteostasis systems, including ER chaperones and endoplasmic reticulum‐associated degradation. This bidirectional crosstalk determines whether TNF‐α responses are adaptive or proteotoxic.
Bailasan Haidar   +3 more
wiley   +1 more source

The Role of O-GlcNAcylation in Immune Cell Activation

open access: yesFrontiers in Endocrinology, 2021
O-GlcNAcylation is a dynamic post-translational modification where the sugar, O-linked β-N-acetylglucosamine (O-GlcNAc) is added to or removed from various cytoplasmic, nuclear, and mitochondrial proteins.
Amy Qiang   +2 more
doaj   +1 more source

Activation of the Transcriptional Function of the NF-κB Protein c-Rel by O-GlcNAc Glycosylation [PDF]

open access: yes, 2013
The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation. The
Baltimore, David   +5 more
core  

DNA Hypomethylation Is One of the Epigenetic Mechanisms Involved in Salt‐Stress Priming in Soybean Seedlings

open access: yesPlant, Cell &Environment, EarlyView.
ABSTRACT Salt‐stress priming enhances the tolerance of plants against subsequent exposure to a similar stress. Priming‐induced transcriptomic reprogramming is mediated by multiple epigenetic mechanisms, the best known of which is histone modifications. However, not much is known about other epigenetic responses.
Wai‐Shing Yung   +7 more
wiley   +1 more source

O-GlcNAcylation reduces proteome solubility and regulates the formation of biomolecular condensates in human cells

open access: yesNature Communications
O-GlcNAcylation plays critical roles in the regulation of protein functions and cellular activities, including protein interactions with other macromolecules.
Senhan Xu   +4 more
doaj   +1 more source

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