Target Name: PHF10
NCBI ID: G55274
Review Report on PHF10 Target / Biomarker Content of Review Report on PHF10 Target / Biomarker
PHF10
Other Name(s): BRG1-associated factor 45a | PHD finger protein 10, isoform a | PHF10_HUMAN | PHD zinc finger protein XAP135 | SMARCG4 | MGC111009 | PHD finger protein 10, transcript variant 1 | BAF45a | BRG1-associated factor, 45-KD, A | PHF10 variant 1 | FLJ10975 | BAF45A | PHD finger protein 10 | XAP135 | PHD finger protein 10 (isoform a)

PHF10: A Protein Implicated in Cancer and Cell Growth

PHF10 (BRG1-associated factor 45a) is a protein that is expressed in various tissues throughout the body. It is a key regulator of cell growth and has been implicated in a number of diseases, including cancer. In recent years, researchers have been interested in finding potential drug targets or biomarkers for PHF10. In this article, we will explore the potential of PHF10 as a drug target and discuss some of the recent research that has been done in this field.

PHF10 is a protein that is expressed in a wide range of tissues, including the brain, heart, liver, and muscle. It is a key regulator of cell growth and has been shown to play a role in a number of diseases, including cancer. In particular, PHF10 has been shown to be involved in the regulation of cell proliferation, and it has been implicated in the development of many types of cancer, including breast, ovarian, and prostate cancer.

One of the key challenges in studying PHF10 is its complex structure. PHF10 is a protein that consists of multiple domains, including an N-terminus, a T-terminus, and a middle region that contains multiple functional domains. The middle region of PHF10 contains a number of known gene products, including a protein that is involved in cell adhesion and a protein that is involved in cell signaling.

In recent years, researchers have been interested in finding potential drug targets or biomarkers for PHF10. One approach that has been explored for this purpose is the use of small molecules, such as drugs that can modulate the activity of PHF10. In this case, the small molecules are designed to interact with specific domains of PHF10 and are used to either activate or inhibit its activity.

One of the most promising approaches for studying PHF10 is the use of small molecules that can modulate its activity in a specific way. For example, researchers have been interested in finding small molecules that can inhibit the activity of PHF10 in the middle region, where it contains the known gene products that are involved in cell adhesion and signaling. This would allow researchers to study the specific functions of PHF10 and identify new potential drug targets.

Another approach that has been explored for studying PHF10 is the use of RNA interference, a technique that allows researchers to knockdown the expression of specific genes in cells. This has been used to study the role of PHF10 in cell signaling and to identify new potential drug targets. By using RNA interference to knockdown the expression of PHF10, researchers have been able to demonstrate that PHF10 plays a key role in cell signaling and that it is involved in a number of important processes in the cell.

In addition to small molecules and RNA interference, researchers have also been interested in studying PHF10 as a potential biomarker for cancer. This is because PHF10 is often expressed at high levels in cancer cells, and it has been shown to be involved in the regulation of cell growth and the development of cancer. By studying the expression of PHF10 in cancer cells, researchers hope to be able to identify new potential drug targets or biomarkers for this disease.

Overall, PHF10 is a protein that has been shown to play a number of important roles in the regulation of cell growth and the development of cancer. While more research is needed to fully understand its functions and potential drug targets, the recent studies that have been done in this field have provided important insights and have identified a number of promising avenues for future research.

Protein Name: PHD Finger Protein 10

Functions: Involved in transcription activity regulation by chromatin remodeling. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity)

The "PHF10 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 PHF10 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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PHF11 | PHF12 | PHF13 | PHF14 | PHF19 | PHF2 | PHF2-ARID5B complex | PHF20 | PHF20L1 | PHF21A | PHF21B | PHF23 | PHF24 | PHF2P1 | PHF2P2 | PHF3 | PHF5A | PHF6 | PHF7 | PHF8 | PHGDH | PHGR1 | PHIP | PHKA1 | PHKA1-AS1 | PHKA2 | PHKA2-AS1 | PHKB | PHKG1 | PHKG2 | PHLDA1 | PHLDA2 | PHLDA3 | PHLDB1 | PHLDB2 | PHLDB3 | PHLPP1 | PHLPP2 | Phosphatidylinositol 3-kinase (PI3K) | Phosphatidylinositol 3-kinase complex (PIK3C3, PIK3R4) | Phosphatidylinositol 4-Kinase (PI4K) | Phosphatidylinositol 4-Kinase beta (PI4K-beta) | Phosphatidylinositol 4-phosphate 5-kinase | Phosphatidylinositol N-acetylglucosaminyltransferase | Phosphatidylinositol-5-phosphate 4-kinase | PHOSPHO1 | PHOSPHO2 | PHOSPHO2-KLHL23 | Phosphodiesterase | Phosphodiesterase 1 (PDE1) | Phosphodiesterase 6 (PDE6) | Phosphodiesterase 8 (nons | Phosphodiesterase IV (PDE4) | Phosphoglucomutase 5 pseudogene 1 | Phosphoglycerate kinase | Phospholipase A | Phospholipase A2 | Phospholipase A2, Cytosolic | Phospholipase A2, Secretory (sPLA2) | Phospholipase C | Phospholipase D | Phosphorylase kinase | PHOX2A | PHOX2B | PHPT1 | PHRF1 | PHTF1 | PHTF2 | PHYH | PHYHD1 | PHYHIP | PHYHIPL | PHYKPL | PI15 | PI16 | PI3 | PI4K2A | PI4K2B | PI4KA | PI4KAP1 | PI4KAP2 | PI4KB | PIANP | PIAS1 | PIAS2 | PIAS3 | PIAS4 | PIBF1 | PICALM | PICART1 | PICK1 | PICSAR | PID1 | PIDD1 | PIERCE1 | PIERCE2 | PIEZO1 | PIEZO2 | PIF1 | PIFO