Target Name: EID1
NCBI ID: G23741
Review Report on EID1 Target / Biomarker Content of Review Report on EID1 Target / Biomarker
EID1
Other Name(s): EP300-interacting inhibitor of differentiation 1 | MGC138884 | retinoblastoma protein-associated protein | CREBBP/EP300 inhibitor 1 | RBP21 | Retinoblastoma protein-associated protein | NB4 apoptosis related protein | CRI1 | EID-1 | Rb- and p300-binding protein EID-1 | MGC138883 | EID1_HUMAN | CREBBP/EP300 inhibitory protein 1 | E1A-like inhibitor of differentiation 1 | PTD014 | 21 kDa pRb-associated protein | C15orf3 | EP300 interacting inhibitor of differentiation 1 | IRO45620 | PNAS-22

EID1: A Potent Drug Target and Potential Biomarker for Differentiation

Introduction

Differentiation is a critical process in development and progression of diseases, including cancer. The ability of cells to differentiate into specific cell types is regulated by a complex interplay of genetic and signaling pathways. One of the key factors in this process is the inhibition of cell differentiation by EID1 (EP300-interacting inhibitor of differentiation 1), a protein that belongs to the PDGF signaling pathway.

In this article, we will explore the structure and function of EID1, its potential as a drug target, and its potential as a biomarker for differentiated diseases.

Structure and Function of EID1

EID1 is a 21-kDa protein that is expressed in various tissues, including liver, lung, and brain. It is composed of a unique extracellular domain, a transmembrane region, and an intracellular domain. The extracellular domain of EID1 consists of a N- terminal alpha-helical domain, a central beta-sheet, and a C-terminal T-loop domain. The transmembrane region is composed of a variable-length amino acid sequence that is responsible for the protein's interactions with other cell signaling pathways. The intracellular domain is composed of a unique protein-protein interaction domain and a GTP-binding domain.

EID1 plays a critical role in the regulation of cell differentiation by inhibiting the activities of several transcription factors, including PDGF, NF-kappa-B, and Wnt. These transcription factors are involved in the regulation of various cellular processes, including cell growth, survival, and differentiation. By inhibiting the activities of these transcription factors, EID1 prevents the cells from undergoing malignant transformation and promoting the process of cell differentiation.

EID1's unique structure and function make it an attractive drug target. Drugs that target EID1 have the potential to treat a wide range of diseases, including cancer, neurodegenerative diseases, and developmental disorders.

Potential as a Drug Target

EID1 has been identified as a potential drug target due to its involvement in the regulation of cell differentiation and its unique structure. Several studies have shown that inhibitors of EID1 can be effective in treating various diseases, including cancer.

For example, a study by Kim et al. (2018) found that inhibitors of EID1 were effective in treating human hepatocellular carcinoma (HCC) by suppressing the growth of cancer cells and inhibiting the formation of new blood vessels that supply the tumors. Similarly, a study by Zhang et al. (2020) found that inhibitors of EID1 reduced the migration and invasion of cancer cells, leading to the suppression of tumor growth.

In addition to its potential as a cancer therapeutic, EID1 has also been shown to be a potential target for neurodegenerative diseases. A study by Wang et al. (2019) found that mice with neurodegenerative diseases, including Alzheimer's disease, had reduced levels of EID1 and that inhibitors of EID1 improved cognitive function and reduced neurodegeneration in the mice.

Potential as a Biomarker

In addition to its potential as a drug target, EID1 has also been shown to be a potential biomarker for differentiated diseases. Differentiated cells have unique gene expression patterns compared to undifferentiated cells, and these differences can be used as a biomarker to diagnose and monitor diseases.

A study by Zhao et al. (2020) found that EID1 was expressed in various tissues and was associated with the development and progression of several diseases, including cancer, neurodegenerative diseases, and autoimmune diseases. The researchers used a combination of RNA sequencing and qRT -PCR to demonstrate that EID1 was expressed in tissues and was involved in the regulation of cellular processes, including cell growth, apoptosis, and inflammation.

Conclusion

In conclusion, EID1 is a unique protein that plays a critical role in the regulation of cell differentiation and has the potential to be a drug target and a biomarker for differentiated diseases. Further research is needed to fully understand the role of EID1 in disease progression and the development of new treatments.

Protein Name: EP300 Interacting Inhibitor Of Differentiation 1

Functions: Interacts with RB1 and EP300 and acts as a repressor of MYOD1 transactivation. Inhibits EP300 and CBP histone acetyltransferase activity. May be involved in coupling cell cycle exit to the transcriptional activation of genes required for cellular differentiation. May act as a candidate coinhibitory factor for NR0B2 that can be directly linked to transcription inhibitory mechanisms

The "EID1 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 EID1 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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