Target Name: WWOX
NCBI ID: G51741
Review Report on WWOX Target / Biomarker Content of Review Report on WWOX Target / Biomarker
WWOX
Other Name(s): WW domain-containing oxidoreductase (isoform 1) | HHCMA56 | EIEE28 | FOR II protein | WW domain containing oxidoreductase, transcript variant 4 | D16S432E | FRA16D | SCAR12 | WW domain containing oxidoreductase | SDR41C1 | WW domain-containing oxidoreductase (isoform 4) | PRO0128 | Short chain dehydrogenase/reductase family 41C, member 1 | WW domain-containing oxidoreductase (isoform 2) | Putative oxidoreductase | FOR | WW domain containing oxidoreductase, transcript variant 1 | fragile site FRA16D oxidoreductase | WWOX variant 2 | short chain dehydrogenase/reductase family 41C member 1 | Fragile 16D oxido reductase | WWOX variant 1 | WWOX_HUMAN | WOX1 | DEE28 | WW domain-containing oxidoreductase | WWOX variant 4 | WW domain-containing protein WWOX | Short chain dehydrogenase/reductase family 41C member 1 | WW domain containing oxidoreductase, transcript variant 2 | Fragile site FRA16D oxidoreductase

Discovery of WW Domain-Containing Oxidoreductase

World War II (WW) was a global conflict that lasted from 1939 to 1945. It was one of the most significant events in human history and resulted in the death of millions of people. The war effort during this period not only led to significant social, economic, and political changes, but it also led to the development of new technologies and scientific advancements. One of the most significant findings of the post-war era was the discovery of the WW domain-containing oxidoreductase (ISOFORM 1) enzyme.

The WW domain-containing oxidoreductase (ISOFORM 1) is a protein that plays a critical role in the detoxification of harmful substances and antioxidants. This enzyme is found in various organisms, including bacteria, archaea, and eukaryotes. It is a key enzyme in the antioxidant defense system, which is a group of enzymes that protect the cell from damage caused by reactive oxygen species (ROS).

The WW domain-containing oxidoreductase (ISOFORM 1) is a member of the superfamily of oxidoreductases, which are a group of enzymes that remove reactive oxygen species from cellular environments. These enzymes function by reducing the oxidation state of a specific cysteine 鈥嬧?媟esidue, which is a key structural component of proteins. The WW domain-containing oxidoreductase (ISOFORM 1) is unique because it is able to detoxify a wide variety of ROS, including hydrogen peroxide, nitric oxide, and oxygen.

The WW domain-containing oxidoreductase (ISOFORM 1) has been the subject of intense research in recent years due to its potential as a drug target or biomarker. Its unique ability to detoxify ROS makes it an attractive target for the development of new therapeutic strategies for various diseases.

One of the most promising aspects of the WW domain-containing oxidoreductase (ISOFORM 1) is its potential as a drug target. Many diseases are caused by the buildup of ROS in the cell, which can lead to oxidative stress and damage to cellular components. The WW domain-containing oxidoreductase (ISOFORM 1) has the potential to be a therapeutic target for diseases that are characterized by the buildup of ROS. For example, the antioxidant deficient diseases, such as cancer, are caused by the buildup of ROS in the cell and could be treated effectively by increasing the levels of the WW domain-containing oxidoreductase (ISOFORM 1).

In addition to its potential as a drug target, the WW domain-containing oxidoreductase (ISOFORM 1) is also a valuable biomarker for the diagnosis and monitoring of various diseases. Its unique ability to detoxify ROS makes it an attractive target for the development of new diagnostic tools. For example, the WW domain-containing oxidoreductase (ISOFORM 1) can be used as a diagnostic marker for cancer, as it is highly expressed in cancer cells and is sensitive to inhibition by small molecules.

The WW domain-containing oxidoreductase (ISOFORM 1) has also been shown to have a positive correlation with the clinical outcome of many diseases. For example, a study published in the journal Nature Medicine found that patients with advanced cancer who received the chemotherapy drug doxorubicin had higher levels of the WW domain-containing oxidoreductase (ISOFORM 1) compared to those who did not receive the drug. The results of this study suggest that the WW domain-containing oxidoreductase (ISOFORM 1) may be a useful biomarker for monitoring the effectiveness of cancer chemotherapy drugs.

Another promising aspect of the WW domain-containing oxidoreductase (ISOFORM 1) is its potential to be used as a therapeutic agent. The WW domain-containing oxidoreductase (ISOFORM 1) can be used to remove ROS from cellular environments, which may have a positive impact on cellular

Protein Name: WW Domain Containing Oxidoreductase

Functions: Putative oxidoreductase. Acts as a tumor suppressor and plays a role in apoptosis. Required for normal bone development (By similarity). May function synergistically with p53/TP53 to control genotoxic stress-induced cell death. Plays a role in TGFB1 signaling and TGFB1-mediated cell death. May also play a role in tumor necrosis factor (TNF)-mediated cell death. Inhibits Wnt signaling, probably by sequestering DVL2 in the cytoplasm

The "WWOX 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 WWOX 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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