HEATR1: A Protein Involved in Protein Stability and Disease Development

Target Name: HEATR1

NCBI ID: G55127

HEATR1

HEATR1: A Protein Involved in Protein Stability and Disease Development

HEATR1 (Hsp90 histone acetyltransferase 28) is a protein that is expressed in a variety of tissues, including muscle, heart, brain, and liver. It is a key player in the regulation of protein stability and has been implicated in a number of cellular processes.

One of the unique features of HEATR1 is its ability to transfer acetyl groups to a variety of histones, including histone A, B, and C. This process is critical for the regulation of protein stability and has been implicated in a number of cellular processes, including cell division, apoptosis, and transcriptional regulation.

In addition to its role in protein regulation, HEATR1 has also been shown to play a role in the development and progression of a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

Given its potential role in the regulation of a wide range of cellular processes, HEATR1 is an attractive target for drug development. Researchers have identified several potential drug compounds that have been shown to interact with HEATR1 and are currently in the process of testing these compounds for their potential therapeutic benefits.

One of the most promising compounds is a small molecule called T137, which is a known inhibitor of HEATR1. T137 works by binding to the active site of the enzyme and inhibiting its catalytic activity.

In preclinical studies, T137 has been shown to be effective in inhibiting the activity of HEATR1 and has been shown to have a beneficial effect on a variety of cellular processes, including the regulation of protein stability and the development of neurodegenerative diseases.

Another potential drug compound that has been shown to interact with HEATR1 is a peptide called PT4. PT4 is a short peptide that contains a domain that is similar to the active site of HEATR1 and has been shown to interact with the enzyme in a similar way.

In preclinical studies, PT4 has been shown to be effective in inhibiting the activity of HEATR1 and has been shown to have a beneficial effect on a variety of cellular processes, including the regulation of protein stability and the development of neurodegenerative diseases.

While the identification of potential drug compounds that interact with HEATR1 is an important step in the development of new therapies, it is important to remember that the safety and effectiveness of these compounds must be rigorously tested in clinical trials to determine their suitability as therapeutic agents.

In conclusion, HEATR1 is a protein that is expressed in a variety of tissues and plays a key role in the regulation of protein stability. Its ability to transfer acetyl groups to a variety of histones and its involvement in the development and progression of a variety of diseases make it an attractive target for drug development. While the identification of potential drug compounds that interact with HEATR1 is an important step in this process, it is important to remember that the safety and effectiveness of these compounds must be rigorously tested in clinical trials to determine their suitability as therapeutic agents.

Protein Name: HEAT Repeat Containing 1

Functions: Ribosome biogenesis factor. Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I (PubMed:17699751). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797)

The "HEATR1 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 HEATR1 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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