GNE: The Potential Drug Target and Biomarker (G10020)

Target Name: GNE

NCBI ID: G10020

Content of Review Report on GNE Target / Biomarker

GNE

Other Name(s): Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase, transcript variant 2 | N-acetylmannosamine kinase | UDP-N-acetylglucosamine 2-epimerase (hydrolyzing) | NM | UDP-GlcNAc-2-epimerase | Uridine diphosphate-N-acetylglucosamine-2-epimerase | Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase isoform 4 | GLCNE | Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase | GNE variant 3 | Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase isoform 3 | GNE2 | GNE variant 5 | IBM2 | glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase | GNE variant 4 | UDP-GlcNAc-2-epimerase/ManAc kinase | UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase | ManAc kinase | Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase, transcript variant 1 | DMRV | GNE variant 2 | GLCNE_HUMAN | UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase | N-acylmannosamine kinase | Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase isoform 5 | Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase, transcript variant 5 | GNE variant 1 | Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase, transcript variant 4 | Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase isoform 2 | Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase, transcript variant 3 | Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase isoform 1 | Uae1

GNE: The Potential Drug Target and Biomarker

Glycylated neurotransmitter endpoints (GNEs) are a type of post-synaptic protein that are modified by the addition of a glycyl group to their cytoplasmic domain. GNEs play a crucial role in neural function and communication, and are involved in various neurological disorders, including depression, anxiety, and neurodegenerative diseases. As a result, GNEs have emerged as a promising drug target for the development of new treatments for these disorders.

The GNEs are involved in the release and uptake of neurotransmitters, which are critical for the function of the nervous system. They are also involved in the regulation of intracellular signaling pathways, which are critical for the maintenance of cellular homeostasis. GNEs have been shown to play a role in the regulation of a wide range of physiological processes, including sleep-wake cycles, synaptic plasticity, and neuroprotection.

One of the key challenges in studying GNEs is their complex cellular localization and regulation. GNEs are expressed in a variety of neural tissues and cells, and can be modified by various post-translational modifications, which affect their localization and stability. This makes it difficult to study their function and determine how they contribute to the development of various neurological disorders.

In addition, the regulation of GNEs is often regulated by a complex network of enzymes and factors, which can affect their stability and function. This makes it difficult to identify small, specific molecules that interact with GNEs and determine their function.

Despite these challenges, research into GNEs is ongoing, and there is growing interest in using them as drug targets and biomarkers for a variety of neurological disorders.

One potential drug target for GNEs is the use of small molecules that can modulate their stability and activity. For example, GNEs have been shown to be regulated by various enzymes, including glycylases and phosphatases. By identifying small molecules that can modulate the activity of these enzymes, researchers may be able to develop new treatments for neurological disorders.

Another potential drug target for GNEs is the use of small molecules that can modulate their structure and localization. GNEs are often modified by the addition of a glycyl group, which can affect their stability and localization in the cell. By identifying small molecules that can modify the glycyl group of GNEs, researchers may be able to develop new treatments for neurological disorders.

In addition to drug targets, GNEs may also be useful as biomarkers for the diagnosis and progression of neurological disorders. For example, GNEs have been shown to be altered in various neurological disorders, including Alzheimer's disease, Parkinson's disease, and depression. By identifying changes in the GNEs in these disorders, researchers may be able to develop new diagnostic tests or biomarkers for the diagnosis and progression of these disorders.

Overall, GNEs are a promising drug target and biomarker for the development of new treatments for a variety of neurological disorders. Further research is needed to fully understand their function and develop new treatments based on these insights.

Protein Name: Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine Kinase

Functions: Regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. Plays an essential role in early development (By similarity). Required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells

The "GNE 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 GNE 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.tech.

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