Target Name: PHAX
NCBI ID: G51808
Review Report on PHAX Target / Biomarker Content of Review Report on PHAX Target / Biomarker
PHAX
Other Name(s): RNUXA | Phosphorylated adapter RNA export protein | PHAX_HUMAN | phosphorylated adapter RNA export protein | phosphorylated adaptor for RNA export | Phosphorylated adaptor for RNA export | RNA U, small nuclear RNA export adaptor (phosphorylation regulated) | RNA U small nuclear RNA export adapter protein | RNA U, small nuclear RNA export adapter (phosphorylation regulated)

PHAX: A Potential Drug Target and Biomarker

PHAX (RNUXA) is a drug target (or biomarker) that has been gaining significant attention in the pharmaceutical industry due to its potential utility as a new treatment option for various diseases. PHAX is a small non-coding RNA molecule that has been shown to play a critical role in various cellular processes, including cell growth, differentiation, and survival.

PHAX has been shown to have a negative impact on cancer cell growth and has been identified as a potential target for cancer treatments. Studies have shown that inhibiting PHAX can cause significant regression in the growth of cancer cells, which could lead to a reduction in the size of tumors and improved overall treatment outcomes.

PHAX has also been shown to be involved in the development and progression of neurodegenerative diseases, such as Alzheimer's and Parkinson's disease. Studies have shown that PHAX levels are significantly decreased in the brains of individuals with Alzheimer's and Parkinson's disease, which could be a potential biomarker for these conditions.

In addition to its potential therapeutic applications, PHAX has also been shown to have a regulatory role in the body. Studies have shown that PHAX is involved in the regulation of various cellular processes, including cell cycle progression, apoptosis (programmed cell death), and inflammation. This suggests that PHAX may play a role in the development and progression of various diseases.

Given the potential utility of PHAX as a drug target and biomarker, there is significant interest in developing compounds that can inhibit its activity. Researchers have been exploring various approaches to inhibiting PHAX, including small molecule inhibitors, RNA-based inhibitors, and protein-based inhibitors.

One approach to inhibiting PHAX is to use small molecule inhibitors. These inhibitors can be designed to specifically target PHAX and have been shown to have a negative impact on its activity. Researchers have been particularly interested in inhibitors that can target the PHAX protein itself, as these inhibitors may have a more targeted and effective impact on the molecule.

Another approach to inhibiting PHAX is to use RNA-based inhibitors. These inhibitors are designed to specifically target PHAX mRNA and have been shown to have a negative impact on its activity. Researchers have been particularly interested in inhibitors that can target PHAX specifically in certain cell types, such as cancer cells or neurodegenerative cells.

Another approach to inhibiting PHAX is to use protein-based inhibitors. These inhibitors are designed to specifically target PHAX protein and have been shown to have a negative impact on its activity. Researchers have been particularly interested in inhibitors that can target PHAX specifically in certain cell types, such as cancer cells or neurodegenerative cells.

While there is still much to be learned about the full potential and utility of PHAX as a drug target and biomarker, it is clear that it has the potential to revolutionize the pharmaceutical industry. Further research is needed to fully understand the activity of PHAX and its potential as a therapeutic agent.

Protein Name: Phosphorylated Adaptor For RNA Export

Functions: A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner (By similarity). Also plays a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Binds also to telomerase RNA

The "PHAX 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 PHAX 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

PHB1 | PHB1P1 | PHB1P19 | PHB1P3 | PHB1P8 | PHB1P9 | PHB2 | PHC1 | PHC1P1 | PHC2 | PHC2-AS1 | PHC3 | Phenylalanyl-tRNA synthetase | PHETA1 | PHETA2 | PHEX | PHEX-AS1 | PHF1 | PHF10 | 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