Target Name: H1-3
NCBI ID: G3007
Other Name(s): histone H1c | histone cluster 1 H1 family member d | H1 histone family, member 3 | histone 1, H1d | H1D | histone H1s-2 | MGC138176 | histone cluster 1, H1d | H13_HUMAN | H1s-2 | Histone 1, H1d | H1.3 | Histone H1s-2 | Histone H1.3 | HIST1H1D | H1F3 | H1.3 linker histone, cluster member | Histone H1c

H1-3: A Drug Target / Disease Biomarker

H1-3, also known as heat shock protein 3 (HSP3), is a protein that is expressed in high levels in the cells under stress, such as cells under attack by pathogens or cells that have undergone cellular stress due to various factors. HSP3 is a member of the HSP family of proteins, which are known for their ability to withstand and adapt to various forms of stress.

HSP3 is a cytoplasmic protein that is involved in various cellular processes, including the regulation of cell survival, the response to stimuli, and the regulation of cellular signaling pathways. HSP3 is also involved in the regulation of inflammation, DNA damage repair, and cell cycle progression.

One of the key functions of HSP3 is its ability to interact with various signaling molecules, including cytokines, chemokines, and pro-inflammatory signaling pathways. HSP3 has been shown to play a role in the regulation of cellular responses to stress, including the regulation of cell death and the modulation of cellular signaling pathways.

In addition to its role in cellular stress response, HSP3 is also a potential drug target. HSP3 has been shown to play a role in various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases. HSP3 has also been shown to be a potential biomarker for various diseases, including cancer and neurodegenerative diseases.

One of the potential mechanisms by which HSP3 may be targeted by drugs is its role in the regulation of cellular signaling pathways. HSP3 has been shown to play a role in the regulation of various signaling pathways, including the TGF-β pathway, the PI3K/Akt pathway, and the NF-kappa-B pathway. HSP3 has been shown to interact with various signaling molecules, including Smad4, a transcription factor that is involved in the regulation of cellular signaling pathways.

In addition to its role in cellular signaling pathways, HSP3 is also involved in the regulation of cellular stress response. HSP3 has been shown to play a role in the regulation of cellular stress response, including the regulation of cell death and the modulation of cellular signaling pathways. HSP3 has also been shown to interact with various stress-regulating molecules, including heat shock factor 1 (HSP1), which is involved in the regulation of cellular stress response.

One of the potential applications of HSP3 as a drug target is its potential to modulate cellular signaling pathways and to protect against cellular stress. HSP3 has been shown to play a role in the regulation of cellular signaling pathways that are involved in the regulation of cell survival, the response to stimuli, and the regulation of cellular signaling pathways. By modulating these signaling pathways, HSP3 may have the potential to treat various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

In conclusion, H1-3, or heat shock protein 3, is a protein that is involved in various cellular processes, including the regulation of cell survival, the response to stimuli, and the regulation of cellular signaling pathways. HSP3 is also involved in the regulation of inflammation, DNA damage repair, and cell cycle progression. HSP3 has been shown to play a role in the regulation of cellular responses to stress, including the regulation of cell death and the modulation of cellular signaling pathways. As a result, HSP3 is a potential drug target for the treatment of various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

Protein Name: H1.3 Linker Histone, Cluster Member

Functions: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity)

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