PPID: A Drug Target / Disease Biomarker (G5481)

Target Name: PPID

NCBI ID: G5481

PPID

PPID: A Drug Target / Disease Biomarker

PPID, also known as Programmed Protein-Protein Interactions, is a protein that plays a crucial role in regulating protein-protein interactions (PPIs) in the body. PPIs are the interactions between two or more proteins that work together to carry out various functions in the cell. They are often referred to as biomarkers because they can be used to diagnose and treat diseases. As a result, targeting PPIs has become an attractive field of research in recent years.

PPID is a protein that is expressed in most tissues of the body and is involved in the regulation of a wide range of cellular processes. It is a key player in the formation of various cellular structures, such as the cytoskeleton, and is involved in the regulation of cell adhesion, migration, and the cytoskeleton. PPID is also involved in the regulation of cell survival, and is a predictor of cancer risk.

One of the unique features of PPID is its ability to interact with other proteins. This interaction is regulated by a variety of factors, including the concentration of PPID in the cell, the presence of other proteins, and the specific sequence of the PPID protein. This makes PPID an attractive target for drug development, as researchers can use various techniques to alter its concentration or activity.

One of the main challenges in studying PPID is its complex structure. PPIDs are highly stable and have a large number of different isoforms. This makes it difficult to study the interactions between PPIDs and other proteins. However, researchers have made significant progress in understanding the structure and function of PPIDs.

One of the most well-studied PPIDs is the protein known as PDGF-BB. PDGF-BB is a cell-signaling protein that is involved in the regulation of cell growth, differentiation, and survival. It is a potent regulator of PPID interactions and has been shown to play a role in a wide range of diseases, including cancer, neurodegenerative diseases, and developmental disorders.

Research has also shown that PPIDs are involved in many different cellular processes, including cell adhesion, migration, and the regulation of cell death. This makes them an attractive target for drug development, as a variety of compounds have been shown to alter the activity of PPIDs.

One of the most promising new approaches to studying PPID is the use of computational tools. By using techniques such as molecular dynamics simulations and site-directed mutagenesis, researchers can study the structure and function of PPIDs in great detail. This has allowed researchers to gain new insights into the regulation of PPID interactions and has led to the development of new drug targets.

In addition to its role in regulating PPID interactions, PPID is also a potential biomarker for a wide range of diseases. Its high stability and the fact that it is involved in many different cellular processes make it an attractive candidate for use as a diagnostic or therapeutic target. For example, studies have shown that PPID levels are often elevated in a variety of cancer types, and that targeting PPIDs may be an effective way to treat these diseases.

Overall, PPID is a protein that has the potential to be a drug target or biomarker. Its structure and function are still being fully understood, and the use of computational tools to study its properties has led to new insights into its regulation. Further research is needed to fully understand the potential of PPID as a drug target or biomarker and to develop effective treatments for the diverse range of diseases that it is involved in.

Protein Name: Peptidylprolyl Isomerase D

Functions: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:11350175, PubMed:20676357). Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. Promotes cell viability in anaplastic lymphoma kinase-positive anaplastic large-cell lymphoma (ALK+ ALCL) cell lines

The "PPID 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 PPID 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