Target Name: Selenoprotein
NCBI ID: P48372
Review Report on Selenoprotein Target / Biomarker Content of Review Report on Selenoprotein Target / Biomarker
Selenoprotein
Other Name(s): SELENO | SELP | SEPP

Selenoprotein: A Promising Drug Target and Biomarker

Abstract:

Selenoprotein (nonspecified subtype) (SELENO) is a highly conserved protein that plays a critical role in various cellular processes. Its unique structure and diverse functions have made it an attractive drug target and biomarker. In this article, we will discuss the SELENO protein, its functions, and its potential as a drug target.

Introduction:

Selenoprotein (nonspecified subtype) (SELENO) is a protein that belongs to the family of serine proteases, known as serine proteases. It is a highly conserved protein that has been identified in various organisms, including bacteria, yeast, plants, and animals. SELENO has unique structural features that give it a distinct role in various cellular processes. Its unique features, including a distinct N-terminus, a unique C-terminus, and a conserved catalytic core, have made it an attractive drug target and biomarker.

Functions of Selenoprotein (nonspecified subtype) (SELENO):

SELENO plays a critical role in various cellular processes, including cell signaling, DNA repair, and metabolism. Its functions are achieved through its unique structure and conserved regions.

1. Cell signaling: SELENO is involved in cell signaling by regulating various signaling pathways. It is a key protein in the RhoA-associated GTPase pathway, which regulates cell signaling. SELENO's conserved N-terminus and C-terminus interact with the RhoA protein, which is a key regulator of the RhoA-associated GTPase pathway. This interaction between SELENO and RhoA protein creates a regulatory loop that ensures proper cell signaling.

2. DNA repair: SELENO is involved in DNA repair by regulating the DNA damage response (DDR) pathway. Its conserved N-terminus interacts with the protein NHEJ, which is critical for DNA repair. SELENO's conserved C-terminus interacts with the protein DNA-protein binding domain (DPB), which is involved in DNA repair. This interaction between SELENO and NHEJ and DNA-protein binding domain creates a regulatory loop that ensures proper DNA repair.

3. Metabolism: SELENO is involved in metabolism by regulating various metabolic pathways. Its conserved N-terminus interacts with the protein Pyh, which is involved in metabolism. SELENO's conserved C-terminus interacts with the protein Myh, which is also involved in metabolism. This interaction between SELENO and Pyh and Myh creates a regulatory loop that ensures proper metabolism.

Potential as a drug target:

SELENO's unique structure and diverse functions make it an attractive drug target. Its conserved N-terminus and C-terminus, as well as its unique features, make it a stable protein that can be targeted by small molecules. Several studies have shown that SELENO can be inhibited by small molecules, and these inhibitions have various effects on cellular processes (11-13).

1. Cell signaling: SELENO can be inhibited by small molecules that inhibit the RhoA-associated GTPase pathway. These inhibitors have been shown to have various effects on cellular signaling pathways, including the regulation of cell proliferation, cell migration, and cell adhesion (14-16).

2. DNA repair: SELENO can be inhibited by small molecules that inhibit the DNA damage response (DDR) pathway. These inhibitors have been shown to have various effects on the regulation of DNA repair, including the inhibition of cell

Protein Name: Selenoprotein (nonspecified Subtype)

The "Selenoprotein 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 Selenoprotein 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

More Common Targets

SELENOS | SELENOT | SELENOV | SELENOW | SELL | SELP | SELPLG | SEM1 | SEM1P1 | SEMA3A | SEMA3B | SEMA3B-AS1 | SEMA3C | SEMA3D | SEMA3E | SEMA3F | SEMA3G | SEMA4A | SEMA4B | SEMA4C | SEMA4D | SEMA4F | SEMA4G | SEMA5A | SEMA5A-AS1 | SEMA5B | SEMA6A | SEMA6A-AS1 | SEMA6A-AS2 | SEMA6B | SEMA6C | SEMA6D | SEMA7A | Semenogelin | SEMG1 | SEMG2 | SENCR | SENP1 | SENP2 | SENP3 | SENP3-associated complex | SENP3-EIF4A1 | SENP5 | SENP6 | SENP7 | SENP8 | SEPHS1 | SEPHS1P4 | SEPHS1P6 | SEPHS2 | SEPSECS | SEPSECS-AS1 | SEPT5-GP1BB | SEPTIN1 | SEPTIN10 | SEPTIN11 | SEPTIN12 | SEPTIN14 | SEPTIN2 | SEPTIN3 | SEPTIN4 | SEPTIN4-AS1 | SEPTIN5 | SEPTIN6 | SEPTIN7 | SEPTIN7-DT | SEPTIN7P11 | SEPTIN7P14 | SEPTIN7P2 | SEPTIN7P6 | SEPTIN7P9 | SEPTIN8 | SEPTIN9 | SERAC1 | SERBP1 | SERBP1P3 | SERF1A | SERF1B | SERF2 | SERF2-C15ORF63 | SERGEF | SERHL | SERINC1 | SERINC2 | SERINC3 | SERINC4 | SERINC5 | Serine (or cysteine) proteinase inhibitor clade F | Serine palmitoyltransferase | Serine protease | Serine protease inhibitor | Serine-aspartate repeat-containing protein I-like | SERP1 | SERP2 | SERPINA1 | SERPINA10 | SERPINA11 | SERPINA12 | SERPINA13P | SERPINA2