Protein Modification by β-N-Acetyl Glucosamine (O-GlcNAc) in Insulin Signaling and Insulin Resistance
Bibliographic record
Abstract
An enzymatic posttranslational modification of proteins at serine or threonine residue by β-N-acetyl glucosamine (GlcNAcylation, also known as O-GlcNAc modification), a product of hexosamine biosynthetic pathway (HBP), has been emerging as a fundamental regulatory mechanism like protein phosphorylation. A significant surge in the information in recent years due to technological advancement has implicated an important role for GlcNAcylation in a wide variety of cellular processes including cell division, metabolism, signal transduction and transcription. Furthermore, GlcNAcylation in proteins has been found to be intimately associated with phosphorylation which is one of the most diverse regulatory mechanisms in the biological system. Therefore, it is likely that altered protein GlcNAcylation may underlie etiology of various diseases including type 2 diabetes. Emerging evidence strongly indicates a role for GlcNAcylation in the development of insulin resistance, a hallmark of type 2 diabetes. Recent findings on protein GlcNAcylation, especially in relation to insulin signaling and insulin resistance have regenerated an immense interest in this field; which was first reported in early nineties. Here we summarize recent development in this area along with unanswered questions and future direction at the end. Some of the recently patented technologies in relation to GlcNAcylation are also summarized in this review. Further investigations in this area are timely and of critical importance with continuous increase in the incidence of type 2 diabetes and diabetes associated complications worldwide. A better understanding of the underlying mechanisms may provide new opportunities for the prevention and treatment of type 2 diabetes. Keywords: Glucose, GlcNAc, GlcNAc transferase, GlcNAc amidase, GlcNAcylation, glycation, hexosamine biosynthetic pathway, insulin resistance, insulin signaling, phosphorylation, posttranslational modification, protein-protein interaction, type 2 diabetes, tyrosine phosphorylation
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How this classification was reachedexpand
Full frame distilled prediction
Teacher imitationNot calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.
Codex and Gemma teacher scores by category
| Category | Codex | Gemma |
|---|---|---|
| Metaresearch | 0.001 | 0.000 |
| Meta-epidemiology (narrow) | 0.000 | 0.000 |
| Meta-epidemiology (broad) | 0.000 | 0.000 |
| Bibliometrics | 0.000 | 0.000 |
| Science and technology studies | 0.000 | 0.000 |
| Scholarly communication | 0.000 | 0.000 |
| Open science | 0.000 | 0.000 |
| Research integrity | 0.000 | 0.001 |
| Insufficient payload (model declined to judge) | 0.000 | 0.000 |
Machine scores (provisional)
The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.
Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.
score_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from itClassification
machine, unvalidatedMachine predicted; a candidate call from one teacher head, not a consensus.
How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".