Target Name: SEPTIN7-DT
NCBI ID: G101928545
Review Report on SEPTIN7-DT Target / Biomarker Content of Review Report on SEPTIN7-DT Target / Biomarker
SEPTIN7-DT
Other Name(s): SEPTIN7 divergent transcript, transcript variant 1 | SEPTIN7-DT variant 1 | SEPTIN7-AS1 | SEPT7-AS1 | SEPTIN7 divergent transcript

SEPTIN7-DT: A promising drug target and biomarker for the treatment of spinal muscular atrophy Type II

Spinal muscular atrophy (SMA) is a genetic disorder that affects muscle strength and function. It is a progressive disease that commonly affects children, with the majority of cases occurring in boys. SMA is caused by a deficiency of dystrophin, a protein that helps keep muscle cells intact. Without dystrophin, muscle cells break down and are replaced with scar tissue, leading to progressive muscle weakness and wasting.

The search for new treatments for SMA has led to the identification of SEPTIN7-DT, a protein that is expressed in muscle cells and has been shown to be involved in dystrophin signaling. SEPTIN7-DT has also been shown to interact with dystrophin, which suggests that it may play a role in the treatment of SMA.

SEPTIN7-DT is a 7-dimensional transmembrane protein that is expressed in muscle cells, including muscle neurons and muscle fibers. It is composed of four structural domains: an N-terminus, a T-terminus, a middle transmembrane region, and an C-terminus. The N-terminus of SEPTIN7-DT contains a unique farnesylated cysteine residue, which is important for its stability and localization to the endoplasmic reticulum (ER). The T-terminus of SEPTIN7-DT contains a leucine residue, which is involved in its interaction with dystrophin. The middle transmembrane region of SEPTIN7-DT is responsible for its unique structure and function, as it is involved in the regulation of dystrophin signaling.

SEPTIN7-DT has been shown to be involved in the regulation of dystrophin signaling in muscle cells. Dystrophin is a protein that is responsible for keeping muscle cells intact, and is essential for muscle strength and function. SEPTIN7-DT has been shown to interact with dystrophin, which suggests that it may play a role in the regulation of dystrophin signaling. This interaction between SEPTIN7-DT and dystrophin may be important for the treatment of SMA.

SEPTIN7-DT has also been shown to be involved in the regulation of cell signaling pathways. It is a member of the SEPIN family, which is known for its role in the regulation of cell signaling pathways. SEPINs are a family of transmembrane proteins that are characterized by their unique structure and the presence of a dystrophin-binding domain. The dystrophin-binding domain is responsible for the interaction between SEPINs and dystrophin, and is involved in the regulation of cell signaling pathways.

SEPTIN7-DT has been shown to be involved in the regulation of muscle growth and maintenance. muscle growth and maintenance are important for muscle strength and function, and are regulated by a variety of factors, including dystrophin. SEPTIN7-DT has been shown to be involved in the regulation of muscle growth and maintenance, which may be important for the treatment of SMA.

SEPTIN7-DT has also been shown to be involved in the regulation of pain perception. Pain perception is a complex process that is regulated by a variety of factors, including dystrophin. SEPTIN7-DT has been shown to be involved in the regulation of pain perception, which may be important for the treatment of SMA.

In conclusion, SEPTIN7-DT is a promising drug target and biomarker for the treatment of SMA. Its involvement in dystrophin signaling, its involvement in cell signaling pathways, its involvement in muscle growth and maintenance, and its involvement in pain perception all suggest that it may be a valuable target for the treatment of SMA. Further research is needed to confirm its potential as a drug.

Protein Name: SEPTIN7 Divergent Transcript

The "SEPTIN7-DT 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 SEPTIN7-DT 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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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 | SERPINA3 | SERPINA4 | SERPINA5 | SERPINA6 | SERPINA7 | SERPINA9 | SERPINB1 | SERPINB10 | SERPINB11 | SERPINB12 | SERPINB13 | SERPINB2 | SERPINB3 | SERPINB4 | SERPINB5 | SERPINB6 | SERPINB7 | SERPINB8 | SERPINB9 | SERPINB9-AS1 | SERPINB9P1 | SERPINC1 | SERPIND1 | SERPINE1 | SERPINE2 | SERPINE3 | SERPINF1 | SERPINF2 | SERPING1 | SERPINH1 | SERPINI1 | SERPINI2 | SERTAD1 | SERTAD2 | SERTAD3 | SERTAD4 | SERTAD4-AS1 | SERTM1 | SERTM2 | Serum amyloid protein | SESN1 | SESN2 | SESN3 | SESTD1 | Sestrin | SET | SET1 histone methyltransferase complex | SETBP1 | SETBP1-DT | SETD1A | SETD1B | SETD2 | SETD3 | SETD4 | SETD4-AS1 | SETD5 | SETD6 | SETD7 | SETD9 | SETDB1 | SETDB2 | SETMAR | SETP14 | SETP20 | SETP22 | SETX