PDILT: A Protein Targeted for A Variety of Diseases (G204474)

Target Name: PDILT

NCBI ID: G204474

PDILT

Other Name(s): protein disulfide isomerase family A, member 7 | protein disulfide isomerase like, testis expressed | Protein disulfide isomerase like, testis expressed | PDIA7 | PDILT_HUMAN | protein disulfide-isomerase-like protein of the testis | Protein disulfide-isomerase-like protein of the testis | protein disulfide isomerase-like protein of the testis

PDILT: A Protein Targeted for A Variety of Diseases

PDILT (Protein Disulfide Isomerase Family A, Member 7) is a protein that is expressed in various cell types throughout the body. It is a member of the PDI (Protein Disulfide Isomerase) family, which is a group of enzymes that are involved in the regulation of protein structure and function. PDILT is responsible for the conversion of a protein called cathepsin B into a disulfide-capped form, which is important for the proper functioning of many cellular processes.

PDILT has been identified as a potential drug target in a number of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. Its role in these conditions is to regulate the structure and function of proteins that are involved in the development and progression of these diseases. By targeting PDILT and modulating its activity, researchers hope to develop new treatments for a variety of diseases.

One of the key challenges in studying PDILT is its complex structure. As a protein, PDILT is composed of a series of amino acids that are held together by bonds. These bonds are formed by a process called disulfide bond formation, which involves the formation of a covalent bond between two amino acids that are involved in the disulfide isomerase reaction.

PDILT has a highly conserved catalytic core, which is located at the center of the protein and is responsible for the chemical reaction that converts the protein into its disulfide-capped form. This core is known as the active site and is the region of the protein that is most active in catalyzing the disulfide bond formation.

In addition to its conserved catalytic core, PDILT also has a number of unique features that make it an attractive drug target. For example, it is a monomeric protein, which means that it is composed of a single polypeptide chain. This can make it easier to design and develop targeted therapies, as well as to monitor the effectiveness of these therapies.

PDILT also has a number of different isoforms, which are different forms of the protein that are produced by alternative splicing. These isoforms are produced by different mechanisms and may have different functions, which can make it more difficult to study the protein. However, researchers have been able to use techniques such as mass spectrometry to identify and quantify different isoforms of PDILT.

PDILT has also been shown to play a role in a variety of cellular processes, including the regulation of protein stability, cell signaling, and inflammation. For example, studies have shown that PDILT is involved in the regulation of the stability of the protein huntingtin, which is a protein that is involved in the development of neurodegenerative diseases.

In addition to its role in these processes, PDILT is also shown to be involved in the regulation of inflammation. For example, studies have shown that PDILT is involved in the production of reactive oxygen species (ROS), which are molecules that can contribute to the development of oxidative stress and inflammation.

Given its complex structure and variety of functions, PDILT is an attractive target for researchers to study and develop new treatments for a variety of diseases. Researchers are currently working to develop new therapies that can specifically target PDILT and modulate its activity. These therapies may include small molecules, antibodies, and other types of drugs that can be used to treat a range of conditions, including cancer, neurodegenerative diseases, and autoimmune disorders.

In conclusion, PDILT is a protein that is expressed in various cell types throughout the body and is involved in the regulation of protein structure and function. Its complex structure and variety of functions make it an attractive target for researchers to study and develop new treatments for a variety of diseases. As research continues to advance, it is likely that new therapies will be developed that can specifically target PDILT and modulate its activity.

Protein Name: Protein Disulfide Isomerase Like, Testis Expressed

Functions: Probable redox-inactive chaperone involved in spermatogenesis

The "PDILT 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 PDILT comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
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•   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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