Unlocking the Potential of PEF1: A Potential Drug Target and Biomarker

Target Name: PEF1

NCBI ID: G553115

PEF1

Unlocking the Potential of PEF1: A Potential Drug Target and Biomarker

The protein encoded by the penta-EF-hand domain (PEF1) has been identified as a potential drug target and biomarker. PEF1 is a five-domain protein that plays a critical role in the regulation of cell adhesion and migration. It is composed of four transmembrane domains and one cytoplasmic tail.PEF1 has been shown to regulate the activities of several cytoskeleton-associated proteins, including microtubules and actin filaments.

The drug development process for new drugs typically involves the identification of potential drug targets and the validation of those targets using various methods. One of the most promising approaches for drug discovery is the screening of potential drug targets using various screening methods, such as high-throughput screening assays, gene expression profiling, and bioinformatics analysis. One of the main goals of drug discovery is to identify a drug target that is druggable and can modulate the target's activity to achieve the desired therapeutic effect.

PEF1: A Potential Drug Target

PEF1 has been shown to play a critical role in the regulation of cell adhesion and migration. It is composed of four transmembrane domains and one cytoplasmic tail. The four transmembrane domains of PEF1 are named based on their subcellular localization. The first domain is the N-terminus domain, which is involved in the formation of the cytoplasmic tail. The second domain is the C-terminus domain, which is involved in the formation of the cytoplasmic tail and is also known as the C-tail domain. The third domain is the middle domain, which contains the transmembrane region of PEF1. The fourth domain is the C-terminus domain, which is involved in the formation of the cytoplasmic tail and is also known as the C-tail domain.

PEF1 has been shown to regulate the activities of several cytoskeleton-associated proteins, including microtubules and actin filaments. It has been shown to play a critical role in the regulation of cell adhesion and migration. PEF1 has also been shown to be involved in the regulation of cell cycle progression, as well as the regulation of cell survival and proliferation.

PEF1 has been shown to be a potential drug target using various methods. For example, several studies have shown thatPEF1 can be targeted by small molecules, including inhibitors of the interaction between PEF1 and microtubules. Additionally, several studies have shown thatPEF1 can be downregulated by various signaling pathways, including the TGF-β pathway.

PEF1: A Potential Biomarker

PEF1 has also been shown to be a potential biomarker for various diseases, including cancer. It has been shown to be involved in the regulation of cell adhesion and migration, which are critical processes for the development and progression of cancer. Additionally, PEF1 has been shown to be involved in the regulation of cell cycle progression, which is also critical for the development and progression of cancer.

PEF1 has been shown to be expressed in various tissues and cells, including cancer cells, normal tissues, and immune cells. It has also been shown to be involved in the regulation of cellular processes, including cell adhesion, migration, and the regulation of the cell cycle.

Conclusion

PEF1 is a protein that has been identified as a potential drug target and biomarker. It is composed of four transmembrane domains and one cytoplasmic tail. PEF1 has been shown to play a critical role in the regulation of cell adhesion and migration, as well as the regulation of cell cycle progression. It has also been shown to be involved in the regulation of

Protein Name: Penta-EF-hand Domain Containing 1

Functions: Calcium-binding protein that acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium. Together with PDCD6, acts as calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in endoplasmic reticulum (ER)-Golgi transport by regulating the size of COPII coats (PubMed:27716508). In response to cytosolic calcium increase, the heterodimer formed with PDCD6 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification (PubMed:27716508). Its role in the heterodimer formed with PDCD6 is however unclear: some evidence shows that PEF1 and PDCD6 work together and promote association between PDCD6 and SEC31 in presence of calcium (PubMed:27716508). Other reports show that PEF1 dissociates from PDCD6 in presence of calcium, and may act as a negative regulator of PDCD6 (PubMed:11278427). Also acts as a negative regulator of ER-Golgi transport; possibly by inhibiting interaction between PDCD6 and SEC31 (By similarity)

The "PEF1 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 PEF1 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;
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•   related combination drugs;
•   pharmacochemistry experiments;
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•   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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