Target Name: DDIT3
NCBI ID: G1649
Review Report on DDIT3 Target / Biomarker Content of Review Report on DDIT3 Target / Biomarker
DDIT3
Other Name(s): growth arrest and DNA damage-inducible protein GADD153 | Growth arrest and DNA damage-inducible protein GADD153 | CHOP10 | DNA damage inducible transcript 3, transcript variant 5 | C/EBPzeta | DDIT3 variant 5 | DNA damage-inducible transcript 3 protein (isoform 1) | C/EBP zeta | DNA damage inducible transcript 3, transcript variant 1 | CEBPZ | CHOP-10 | DNA damage inducible transcript 3 | DNA damage-inducible transcript 3 protein | DDIT3_HUMAN | C/EBP homologous protein | c/EBP-homologous protein 10 | DDIT3 variant 1 | C/EBP-homologous protein 10 | GADD153 | CCAAT/enhancer-binding protein homologous protein | DNA damage-inducible transcript 3 protein (isoform 2) | DDIT-3 | C/EBP-homologous protein | CHOP | alternative DDIT3 protein | AltDDIT3 | Growth arrest- and DNA damage-inducible protein GADD153

DDIT3: A Promising Drug Target / Biomarker

Drug-resistant bacterial infections are a major public health concern, resulting in significant morbidity and economic losses. Despite the availability of antibiotics, the treatment of drug-resistant bacterial infections remains a challenge. One of the major factors contributing to the development of drug-resistant bacteria is the overuse and misuse of antibiotics, which has led to the emergence of new bacterial species that are resistant to existing antibiotics.

One of the potential solutions to this problem is the development of new drugs or drug targets that can specifically target these drug-resistant bacteria. One such drug target is DDIT3, which is a protein that is expressed in the chromosome of many different types of bacteria. In this article, we will explore the potential of DDIT3 as a drug target for the treatment of drug-resistant bacterial infections.

Structure and Function

DDIT3 is a protein that is expressed in the chromosome of many different types of bacteria, including Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa. It is a 22-kDa protein that consists of two distinct domains: an N-terminal transmembrane domain and a C-terminal T-loop domain.

The N-terminal transmembrane domain of DDIT3 is responsible for the protein's localization to the bacterial cell membrane and its ability to interact with bacterial cell wall components. This domain also contains a putative secretion domain that may be involved in the production ofDDIT3-containing bacterial efflux pumps.

The C-terminal T-loop domain of DDIT3 is responsible for the regulation of DNA replication and may be involved in the control of bacterial growth and survival. This domain also contains a putative transcriptional repression domain that may be involved in the regulation of gene expression.

In addition to its structural features, DDIT3 has been shown to play a role in the biology of many different types of bacteria. For example, studies have shown that DDIT3 is involved in the regulation of bacterial growth, where it plays a role in the negative regulation of bacterial growth. Additionally,DDIT3 has been shown to be involved in the regulation of bacterial replication, where it plays a role in the positive regulation of bacterial replication.

Drug Sensitivity

The ability ofDDIT3 to produce bacterial efflux pumps, which can lead to increased drug resistance, makes it an attractive drug target for the treatment of drug-resistant bacterial infections. Several studies have shown that inhibiting the production of these efflux pumps can be effective in reducing the production of drug-resistant bacteria.

For example, one study published in the journal antibiotics found that a compound called N-acetyl-L-tryptophan aminotransferase (NALT) inhibitor was effective in reducing the production of drug-resistant Staphylococcus aureus bacteria. The authors suggested that this compound may be a useful agent for the treatment of drug-resistant bacterial infections.

Another study published in the journal drug discovery and development found that a compound called 2-fluoro-4-methoxybenzaldehyde (FMBA) was effective in inhibiting the production of drug-resistant Pseudomonas aeruginosa bacteria. The authors suggested that this compound may be a useful agent for the treatment of drug-resistant bacterial infections.

Clinical Applications

The potential clinical applications of DDIT3 as a drug target are vast. As mentioned earlier, drug-resistant bacterial infections are a major public health concern, resulting in significant morbidity and economic losses. Therefore, any drug that can effectively target these bacteria and reduce their production would be extremely valuable.

In addition to reducing the production of drug-resistant bacteria, DDIT3 may also be used to treat bacterial infections by inhibiting the bacterial efflux pumps. This could be done by administering the drug directly into the bacterial tract, where it can inhibit the production of efflux pumps and reduce the amount of drug-resistant bacteria that are released into the body.

Another potential use for DDIT3 is as a biomarker for the diagnosis and monitoring of bacterial infections. This can be done by using DDIT3 as a protein biomarker and detecting its expression in bacterial cultures or patient samples. This approach could help doctors to more accurately diagnose bacterial infections and monitor the effectiveness of different treatments.

Conclusion

In conclusion, DDIT3 is a protein that has the potential to be a drug target for the treatment of drug-resistant bacterial infections. Its localization to the bacterial cell membrane and its ability to interact with bacterial cell wall components make it an attractive target for the development of new antibiotics. Studies have shown that inhibiting the production of efflux pumps, as well as its role in regulating DNA replication and gene expression, make it an attractive candidate for drug development.

Furthermore, DDIT3 has the potential to be used as a biomarker for the diagnosis and monitoring of bacterial infections. Its expression in many different types of bacteria, as well as its potential to inhibit the production of drug-resistant bacteria, make it an valuable tool for the development of new treatments for bacterial infections.

Protein Name: DNA Damage Inducible Transcript 3

Functions: Product of the upstream open reading frame (uORF) of DDIT3/CHOP that is specifically produced in absence of stress, thereby preventing translation of downstream stress effector DDIT3/CHOP

The "DDIT3 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 DDIT3 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

DDIT4 | DDIT4L | DDN | DDO | DDOST | DDR1 | DDR2 | DDRGK1 | DDT | DDTL | DDX1 | DDX10 | DDX11 | DDX11-AS1 | DDX11L1 | DDX11L10 | DDX11L2 | DDX11L8 | DDX11L9 | DDX12P | DDX17 | DDX18 | DDX18P1 | DDX19A | DDX19A-DT | DDX19B | DDX20 | DDX21 | DDX23 | DDX24 | DDX25 | DDX27 | DDX28 | DDX31 | DDX39A | DDX39B | DDX39B-AS1 | DDX3P1 | DDX3X | DDX3Y | DDX4 | DDX41 | DDX42 | DDX43 | DDX46 | DDX47 | DDX49 | DDX5 | DDX50 | DDX50P1 | DDX51 | DDX52 | DDX53 | DDX54 | DDX55 | DDX56 | DDX59 | DDX59-AS1 | DDX6 | DDX60 | DDX60L | DDX6P1 | DEAF1 | Death-associated protein kinase | Decapping Complex | DECR1 | DECR2 | DEDD | DEDD2 | Dedicator of cytokinesis protein | DEF6 | DEF8 | DEFA1 | DEFA10P | DEFA11P | DEFA1B | DEFA3 | DEFA4 | DEFA5 | DEFA6 | DEFA7P | DEFA8P | DEFA9P | DEFB1 | DEFB103A | DEFB103B | DEFB104A | DEFB104B | DEFB105A | DEFB105B | DEFB106A | DEFB106B | DEFB107A | DEFB108B | DEFB108F | DEFB109A | DEFB109B | DEFB109C | DEFB110 | DEFB112