Target Name: Chaperone
NCBI ID: P18275
Review Report on Chaperone Target / Biomarker Content of Review Report on Chaperone Target / Biomarker
Chaperone
Other Name(s): None

Chaperone Proteins: Drug Targets and Their Role in Disease

Chaperone is a protein that plays a critical role in the proper functioning of various cell processes in the body. It is a component of many different cellular structures, including the endoplasmic reticulum, the mitochondria, and the endosomal system. Chaperones are known to help transport and facilitate the delivery of various molecules to their respective destinations within the cell.

One of the well-known chaperone proteins is HSP70, which is a heat- shock protein that is expressed in high levels in the cells under stress, such as those affected by infection or chemotherapy. HSP70 has been shown to play a role in protecting the cell against oxidative stress and inflammation, and it has also been linked to various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

Another chaperone protein that has received significant attention in recent years is TSP90, which is a member of the TSP family. TSP90 is known to play a role in cell signaling, particularly in the regulation of ion channels and protein kinases. It has been shown to promote the formation of neurotransmitter-dependent action potentials in neurons, which are important for proper brain function. TSP90 has also been linked to various neurological and psychiatric disorders, including epilepsy and schizophrenia.

In addition to its role in cell signaling, chaperone proteins have also been shown to play a role in drug delivery and targeting. For example, the chaperone protein ALYsT is a carrier protein that has been shown to transport small molecules, including drugs, across the endosomal membrane and into the endoplasmic reticulum. ALYsT has been shown to play a critical role in the efficacy of some anti-cancer drugs, such as taxanes and vinca alkaloids.

Another example of a chaperone protein that has been shown to be a drug target is the protein known as CSN2. CSN2 is a component of the endosomal system and has been shown to play a role in the delivery of various molecules, including viruses and cancer cells. It is known to interact with the protein known as p53, which is a well-known tumor suppressor protein. The interaction between CSN2 and p53 has been shown to play a critical role in the regulation of cellular processes, including cell death and apoptosis.

Chaperone proteins have also been shown to be involved in the regulation of cellular processes that are important for the development and progression of various diseases. For example, the chaperone protein HSP70 has been shown to play a role in the development of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. HSP70 has also been shown to interact with the protein known as tau, which is a component of neurofibrillary tangles in these diseases. The interaction between HSP70 and tau has been shown to contribute to the development and progression of these diseases.

In conclusion, chaperone proteins play a critical role in the proper functioning of various cellular processes in the body. Many of these proteins have also been shown to play a role in drug delivery and targeting, and their regulation is closely monitored by researchers. The study of chaperone proteins and their role in disease progression and drug delivery is an active area of research, and continued studies in this field may lead to the development of new therapeutic strategies for the treatment of various diseases.

Protein Name: Chaperone (nonspecified Subtype)

The "Chaperone 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 Chaperone 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

Chaperonin-containing T-complex polypeptde 1 complex (CCT) | CHASERR | CHAT | CHCHD1 | CHCHD10 | CHCHD2 | CHCHD2P6 | CHCHD2P9 | CHCHD3 | CHCHD4 | CHCHD5 | CHCHD6 | CHCHD7 | CHCT1 | CHD1 | CHD1-DT | CHD1L | CHD2 | CHD3 | CHD4 | CHD5 | CHD6 | CHD7 | CHD8 | CHD9 | CHDH | CHEK1 | CHEK2 | CHEK2P2 | Chemokine CXC receptor | Chemokine receptor | CHERP | CHFR | CHFR-DT | CHGA | CHGB | CHI3L1 | CHI3L2 | CHIA | CHIAP1 | CHIAP2 | CHIC1 | CHIC2 | CHID1 | CHIT1 | CHKA | CHKB | CHKB-CPT1B | CHKB-DT | CHL1 | CHL1-AS2 | Chloride channel | CHM | CHML | CHMP1A | CHMP1B | CHMP1B2P | CHMP2A | CHMP2B | CHMP3 | CHMP4A | CHMP4B | CHMP4BP1 | CHMP4C | CHMP5 | CHMP6 | CHMP7 | CHN1 | CHN2 | CHN2-AS1 | CHODL | Cholesterol Epoxide Hydrolase (ChEH) | Cholesterol esterase | Choline transporter-like protein | CHORDC1 | CHORDC1P4 | CHP1 | CHP1P2 | CHP2 | CHPF | CHPF2 | CHPT1 | CHRAC1 | CHRD | CHRDL1 | CHRDL2 | CHRFAM7A | CHRM1 | CHRM2 | CHRM3 | CHRM3-AS2 | CHRM4 | CHRM5 | CHRNA1 | CHRNA10 | CHRNA2 | CHRNA3 | CHRNA4 | CHRNA5 | CHRNA6