Unlocking The Potential of O-Fucosylpeptides (G3955)

Target Name: LFNG

NCBI ID: G3955

LFNG

Other Name(s): O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase | Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe (isoform c) | LFNG variant 3 | LFNG O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase, transcript variant 1 | LFNG O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase, transcript variant 4 | LFNG variant 1 | LFNG_HUMAN | SCDO3 | Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe | Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe (isoform d) | LFNG variant 4 | LFNG O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase | Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe (isoform a) | LFNG O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase, transcript variant 3

Unlocking The Potential of O-Fucosylpeptides

LFNG (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase) is a gene that encodes a protein located in the endoplasmic reticulum (ER) of cells. The ER is a network of organelles responsible for the synthesis, processing, and storage of proteins. The function and regulation of LFNG is not well understood, but it is known to be involved in the synthesis and processing of a type of protein called O-fucosylpeptide.

O-fucosylpeptides are a type of carbohydrate that contain a fucose molecule attached to apeptide side chains. They are found in a variety of organisms, including bacteria, yeast, and animals. O-fucosylpeptides have been shown to have a variety of functions, including modulating protein stability, influencing cellular signaling pathways, and serving as potential drug targets.

The LFNG gene is primarily expressed in the brain, where it is involved in the production of a protein called GLT-2 (glutamic acid decarboxylase 2). GLT-2 is an enzyme that converts glutamic acid, a highly reactive acid that is involved in neurotransmitter synthesis, to gamma-aminobutyric acid (GABA), a neurotransmitter that has inhibitory effects on neurons.

In addition to its role in GLT-2 synthesis, LFNG is also involved in the processing of O-fucosylpeptides. Studies have shown that LFNG can catalyze the transfer of the O-fucosyl group from one amino acid to another, a process known as O- fucosylation. This reaction is critical for the formation of stable O-fucosylpeptides, which have been shown to play important roles in cellular signaling pathways.

The importance of LFNG in the processing of O-fucosylpeptides is suggested by its expression in the brain, where it is known to be involved in the development and maintenance of neural circuits. In addition, LFNG has been shown to play a role in modulating the stability of other proteins, including the neurotransmitter acetylcholine.

The potential implications of LFNG as a drug target are significant. O-fucosylpeptides have been shown to have a variety of functions in cellular signaling pathways, including modulating protein stability and influencing the structure and function of other proteins. As such, LFNG may be a promising target for small molecule inhibitors that can modulate its activity.

In addition to its potential as a drug target, LFNG is also a promising biomarker for a variety of neurological and psychiatric disorders. O-fucosylpeptides have been shown to play important roles in the development and progression of a variety of neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease. As such, LFNG may be a valuable tool for the diagnosis and treatment of these disorders.

Overall, LFNG is a gene that has the potential to be a drug target and biomarker for a variety of neurological and psychiatric disorders. Further research is needed to fully understand its function and regulation in these processes.

Protein Name: LFNG O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase

Functions: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 (By similarity). Decreases the binding of JAG1 to NOTCH2 but not that of DLL1 (PubMed:11346656). Essential mediator of somite segmentation and patterning (By similarity)

The "LFNG Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about LFNG comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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