Target Name: FHIT
NCBI ID: G2272
Review Report on FHIT Target / Biomarker Content of Review Report on FHIT Target / Biomarker
FHIT
Other Name(s): dinucleosidetriphosphatase | Dinucleosidetriphosphatase | diadenosine 5',5'''-P1,P3-triphosphate hydrolase | Diadenosine 5',5'''-P1,P3-triphosphate hydrolase | Bis(5'-adenosyl)-triphosphatase | AP3A h

FHIT: A Potential Drug Target Or Biomarker for Diseases

FHIT, or dinucleosidetriphosphatase, is a protein that plays a crucial role in cellular signaling and metabolism. It is a key enzyme in the DNA damage repair pathway, which helps to prevent the accumulation of genetic mutations that can cause diseases such as cancer.

FHIT is a member of the nucleotide-binding protein family, which includes enzymes that bind to nucleotides such as DNA and RNA. Its unique function is to add a phosphate group to the dinucleotide triphosphate (dNTP), which is a key component of DNA replication and repair.

In recent years, researchers have become increasingly interested in FHIT as a potential drug target or biomarker for a variety of diseases. Its unique mechanism of action and its involvement in cellular signaling pathways make it an attractive target for drug development.

One of the reasons for the interest in FHIT is its ability to interact with a variety of different nucleotides, which makes it a versatile target for drugs. For example, FHIT has been shown to interact with DNA-protein binding proteins, which are involved in regulates DNA replication and repair. This suggests that FHIT may be a useful target for drugs that target these proteins.

Additionally, FHIT's role in the DNA damage repair pathway has also led to its potential as a biomarker for certain types of cancer. Cancer cells have DNA damage, which can result in the development of certain types of cancer. FHIT's role in repairing DNA damage makes it a potential target for cancer therapies that aim to inhibit its activity.

Another potential mechanism by which FHIT may be involved in the development of certain diseases is its role in cell signaling pathways. FHIT has been shown to play a role in regulating cell proliferation and has been linked to the development of certain types of cancer. Additionally, FHIT has also been shown to interact with proteins involved in cell signaling pathways, which suggests that it may be involved in the regulation of cellular processes that are important for the development of certain diseases.

FHIT is also a good candidate as a drug target because of its high accuracy and specificity. FHIT is a protein that is expressed in all cell types and at high levels in most tissues. This makes it an attractive target for drugs that are able to specifically interact with FHIT and prevent its activity.

In conclusion, FHIT is a protein that has the potential to be a drug target or biomarker for a variety of diseases. Its unique mechanism of action and its involvement in cellular signaling pathways make it an attractive target for drug development. Additionally, FHIT's role in the DNA damage repair pathway and its potential as a biomarker for certain types of cancer make it a valuable tool in the fight against these diseases. Further research is needed to fully understand the potential of FHIT as a drug target or biomarker and to develop effective therapies .

Protein Name: Fragile Histidine Triad Diadenosine Triphosphatase

Functions: Possesses dinucleoside triphosphate hydrolase activity (PubMed:12574506, PubMed:15182206, PubMed:8794732, PubMed:9323207, PubMed:9576908, PubMed:9543008). Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP (PubMed:12574506, PubMed:15182206, PubMed:8794732, PubMed:9323207, PubMed:9576908, PubMed:9543008). Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP (PubMed:8794732). Exhibits adenylylsulfatase activity, hydrolyzing adenosine 5'-phosphosulfate to yield AMP and sulfate (PubMed:18694747). Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (PubMed:18694747). Exhibits adenylylsulfate-ammonia adenylyltransferase, catalyzing the ammonolysis of adenosine 5'-phosphosulfate resulting in the formation of adenosine 5'-phosphoramidate (PubMed:26181368). Also catalyzes the ammonolysis of adenosine 5-phosphorofluoridate and diadenosine triphosphate (PubMed:26181368). Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5 (PubMed:18077326). Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways (PubMed:16407838). Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis (PubMed:15313915). Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake (PubMed:12574506, PubMed:19622739). Functions as tumor suppressor (By similarity)

The "FHIT 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 FHIT 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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