Heat-Shock Protein 90: An Anti-Tumor Molecule (P5659)

Target Name: Heat shock protein 90

NCBI ID: P5659

Heat shock protein 90

Other Name(s): Heat shock protein 90 | Hsp90

Heat-Shock Protein 90: An Anti-Tumor Molecule

Heat shock protein 90 (HSP90) is a protein that is expressed in various cell types and is involved in a variety of cellular processes. HSP90 is a heat-induced protein that can be soothing to muscles, heart, brain, liver and other organs and tissues, when When cells are stimulated by high temperatures, HSP90 can quickly fold into specific structures to resist heat damage to cells.

HSP90 is a protein with a molecular weight of 90 kDa, and its thermal stability is due to the presence of multiple hydrogen bonds in its secondary structure. The secondary structure of HSP90 includes a core 伪-helix, a transmembrane region, and an N-terminal 伪-helix. In cells, HSP90 usually interacts with other proteins to form a complex, and these interactions further affect the biological functions of HSP90.

The biological functions of HSP90 include regulating spindle assembly and cell division, apoptosis, cell migration, cell adhesion, cell signaling, cell drug resistance, immune response, metabolism, etc. during the cell cycle. HSP90 plays an important role in many biological processes and is a target of many drugs.

Currently, HSP90 has become a popular molecule in many research fields, especially in tumor research. The anti-tumor effect of HSP90 is mainly achieved by affecting the apoptosis and proliferation of tumor cells. The anti-tumor effect of HSP90 is closely related to its expression level in tumors. Many studies have shown that the expression level of HSP90 is positively correlated with tumor invasion, metastasis and treatment response.

In addition, HSP90 is also widely used in drug screening and drug target discovery. Since HSP90 is expressed in various cells, it is a very promising drug target. Many studies have confirmed that HSP90 inhibitors can inhibit the proliferation, apoptosis and metastasis of tumor cells. In addition, HSP90 inhibitors can also inhibit the immune evasion of tumor cells, thereby enhancing the expression of tumor antigens in immune cells and the immunotherapy effect of tumor antigens.

HSP90, as a protein with a molecular weight of 90 kDa, has the property of resisting damage caused by heat in cells. The biological functions of HSP90 include regulating spindle assembly and cell division, apoptosis, cell migration, cell adhesion, cell signaling, cell drug resistance, immune response, metabolism, etc. during the cell cycle. HSP90 has become a popular molecule in many research fields, especially in oncology research. The anti-tumor effect of HSP90 is mainly achieved by affecting the apoptosis and proliferation of tumor cells. In addition, HSP90 is also widely used in drug screening and drug target discovery.

Protein Name: Heat Shock Protein 90 (nonspecified Subtype)

The "Heat shock protein 90 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 Heat shock protein 90 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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