Target Name: HSPB1
NCBI ID: G3315
Review Report on HSPB1 Target / Biomarker Content of Review Report on HSPB1 Target / Biomarker
HSPB1
Other Name(s): Heat shock protein family B (small) member 1 | heat shock protein family B (small) member 1 | HspB1 | Stress-responsive protein 27 | heat shock 27kD protein 1 | Heat shock protein beta-1 | estrogen-regulated 24 kDa protein | HSP27 | SRP27 | heat shock 27kDa protein 1 | CMT2F | Heat shock 27kD protein 1 | Hsp25 | heat shock 27 kDa protein | HEL-S-102 | 28 kDa heat shock protein | OTTHUMP00000161096 | DKFZp586P1322 | Estrogen-regulated 24 kDa protein | Epididymis secretory protein Li 102 | HSP28 | stress-responsive protein 27 | putative heat shock protein family B member 1 isoform | HMN2B | HSPB1_HUMAN | Heat shock 27 kDa protein | Heat shock 27kDa protein 1 (HSPB1) | epididymis secretory protein Li 102 | HS.76067 | HSP 27

Heat Shock Protein HSPB1: A Potential Drug Target and Biomarker for Diseases

Heat shock protein (HSP) is a family of proteins that are expressed in high levels in the cells under stress, such as those subjected to heat or radiation. HSPs play a crucial role in protecting the cell from the harmful effects of these stressors by maintaining their structural integrity and facilitating the repair process. The HSPB1 protein is a member of the HSP family and is expressed in a variety of cell types. Its unique structure and function make it an attractive drug target and a potential biomarker for various diseases.

The HSPB1 protein is a 21-kDa protein that is expressed in a variety of tissues and cells, including muscle, heart, brain, and cancer cells. It is highly conserved, with a calculated amino acid sequence of 21.1% identity to the human gene family 1 (HSP70) gene family. HSPB1 is a monomer and has a unique 25% polyglutamylated region at its C-terminus. This region is known as the HSPB1-specific glutamylated domain and is involved in protein-protein interactions, including the interaction with HSP70 and HSP90 proteins.

One of the unique features of HSPB1 is its ability to form a stable complex with HSP70 and HSP90 proteins, making it a potential drug target. These complexes are formed under stress and can be targeted by small molecules, such as drugs, to enhance the formation of these protein-protein interfaces. This interaction between HSPB1 and HSP70/90 proteins is a critical step in the stress response process and is a target for the development of new therapeutic strategies for various diseases.

HSPB1 has also been shown to play a role in the regulation of cellular processes, including cell growth, apoptosis, and inflammation. For example, HSPB1 has been shown to regulate the growth of cancer cells and to play a role in the development of neurodegenerative diseases. Additionally, HSPB1 has been shown to contribute to the regulation of inflammation and immune response.

Another important function of HSPB1 is its role in the regulation of protein homeostasis. HSPB1 is involved in the regulation of protein synthesis, degradation, and storage in the endoplasmic reticulum (ER) and cytoplasm. This is important for maintaining the cellular homeostasis and for the regulation of cellular processes, such as the production of reactive oxygen species (ROS) that can damage cellular components and contribute to the development of diseases.

In conclusion, HSPB1 is a protein that plays a critical role in the regulation of cellular processes and is an attractive drug target due to its unique structure and function. Its ability to form stable interactions with HSP70 and HSP90 proteins makes it a potential target for the development of new therapeutic strategies for various diseases. Additionally, HSPB1's role in the regulation of protein homeostasis makes it an important biomarker for the development of diseases. Further research is needed to fully understand the role of HSPB1 in the development of diseases and to develop new therapeutic strategies.

Protein Name: Heat Shock Protein Family B (small) Member 1

Functions: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state (PubMed:10383393, PubMed:20178975). Plays a role in stress resistance and actin organization (PubMed:19166925). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (PubMed:23728742)

The "HSPB1 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 HSPB1 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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