Target Name: VGF
NCBI ID: G7425
Review Report on VGF Target / Biomarker Content of Review Report on VGF Target / Biomarker
VGF
Other Name(s): VGF nerve growth factor inducible | VGF_HUMAN | SCG7 | Neurosecretory protein VGF | SgVII | neuro-endocrine specific protein VGF | Neuroendocrine regulatory peptide-1 | Neuroendocrine regulatory peptide-2 | VGF-derived peptide TLQP-21 | VGF-derived peptide TLQP-62 | Neuro-endocrine specific protein VGF | NERP-2 | NERP-1 | Antimicrobial peptide VGF[554-577]

Understanding VGF: Potential TherapeuticAgents

VGF (VGF nerve growth factor inducible) is a protein that plays a critical role in the growth and development of tissues, including neural cells. It is a potent regulator of cell proliferation and survival, and has been shown to be involved in a wide range of physiological processes, including embryonic development, tissue repair, and regeneration.

One of the key challenges in studying VGF is its complex structure and function. Despite its importance, little is known about the molecular mechanisms that regulate its activity, or how it interacts with other proteins.

The search for new drug targets and biomarkers has led to the development of VGF as a potential therapeutic agent. Researchers are interested in using VGF as a target for drugs that can promote neural regeneration, repair, or growth, with the hope that these treatments will be effective in treating a variety of neurological and psychiatric disorders.

One approach to studying VGF is through its role as a ligand for protein-protein interactions. This means that VGF can interact with other proteins, known as co-factors, to regulate their activity. One of the most well-studied co-factors for VGF is its interaction with the protein FGF (fibroblast growth factor), which is also a potent regulator of cell proliferation and growth.

Research has shown that VGF and FGF can interact with each other to promote the growth and development of neural cells. This interaction may be important for the development and maintenance of tissues, including the brain.

Another approach to studying VGF is through its role as a negative regulator of the TGF-β pathway. This pathway is a well-studied process that regulates cell proliferation and growth, and is involved in many physiological processes, including embryonic development and tissue repair.

Research has shown that VGF can inhibit the activity of the TGF-β pathway, which may be important for the regulation of cell growth and the prevention of excessive cell proliferation. This interaction between VGF and TGF-β may be important for the development of tissues and organs, including the brain.

In addition to its role in cell proliferation and growth, VGF is also involved in the regulation of cell survival. This may be important for the regulation of stress responses and the prevention of cell death, which are important for maintaining the health and function of tissues.

Research has shown that VGF can interact with the protein p53, which is a well-studied protein that plays a critical role in regulating cell survival. This interaction may be important for the regulation of stress responses and the prevention of cell death, which are important for maintaining the health and function of tissues.

Overall, the role of VGF in cell proliferation, growth, and survival is complex and still not fully understood. Further research is needed to fully understand the molecular mechanisms that regulate its activity, and to determine its potential as a therapeutic agent.

Protein Name: VGF Nerve Growth Factor Inducible

Functions: Secreted polyprotein that is packaged and proteolytically processed by prohormone convertases PCSK1 and PCSK2 in a cell-type-specific manner (By similarity). VGF and peptides derived from its processing play many roles in neurogenesis and neuroplasticity associated with learning, memory, depression and chronic pain (By similarity)

The "VGF 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 VGF 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

More Common Targets

VGLL1 | VGLL2 | VGLL3 | VGLL4 | VHL | VIL1 | VILL | VIM | VIP | VIPAS39 | VIPR1 | VIPR1-AS1 | VIPR2 | VIRMA | VIT | VKORC1 | VKORC1L1 | VLDLR | VLDLR-AS1 | VMA21 | VMAC | VMO1 | VMP1 | VN1R1 | VN1R101P | VN1R108P | VN1R10P | VN1R11P | VN1R12P | VN1R17P | VN1R18P | VN1R2 | VN1R4 | VN1R46P | VN1R5 | VN1R82P | VN1R91P | VN1R96P | VN2R11P | VN2R1P | VN2R3P | VNN1 | VNN2 | VNN3P | Voltage-dependent anion channels (Porins) | Voltage-dependent calcium channel gamma subunit | Voltage-gated K(v) channel | Voltage-Gated Sodium Channel Complex | Volume-Regulated Anion Channel (VRAC) | VOPP1 | VOR Complex | VPREB1 | VPREB3 | VPS11 | VPS13A | VPS13A-AS1 | VPS13B | VPS13C | VPS13C-DT | VPS13D | VPS16 | VPS18 | VPS25 | VPS26A | VPS26AP1 | VPS26B | VPS26C | VPS28 | VPS29 | VPS33A | VPS33B | VPS35 | VPS35L | VPS36 | VPS37A | VPS37B | VPS37C | VPS37D | VPS39 | VPS41 | VPS45 | VPS4A | VPS4B | VPS50 | VPS51 | VPS51P8 | VPS52 | VPS53 | VPS54 | VPS72 | VPS8 | VPS9D1 | VPS9D1-AS1 | VRK1 | VRK2 | VRK3 | VRTN | VSIG1 | VSIG10 | VSIG10L