Target Name: DDX25
NCBI ID: G29118
Review Report on DDX25 Target / Biomarker Content of Review Report on DDX25 Target / Biomarker
DDX25
Other Name(s): DEAD (Asp-Glu-Ala-Asp) box helicase 25 | DEAD box protein 25 | ATP-dependent RNA helicase DDX25 | DEAD-box helicase 25 | DDX25_HUMAN | GRTH | gonadotropin-regulated testicular RNA helicase | DDX25 variant 1 | ATP-dependent RNA helicase DDX25 (isoform 1) | DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 25 | epididymis secretory sperm binding protein | DEAD (Asp-Glu-Ala-Asp) box polypeptide 25 | Gonadotropin-regulated testicular RNA helicase

Discovering The Helicase Protein: Potential Drug Target Or Biomarker

Helicase is a protein that plays a crucial role in DNA replication and repair. It is an enzyme that unwinds double-stranded DNA and separates the two complementary strands. The protein encoded by the gene DEAD (Asp-Glu-Ala-Asp) box is a member of the family of DNA-protein interactions, known as theHelicase family 25 (HEC25)1. In this article, we discuss the Helicase protein encoded by DEAD and its potential as a drug target or biomarker.

Structure and Function

The DEAD (Asp-Glu-Ala-Asp) box is a 23 amino acid protein that is located at the top of the double helix. It is composed of two distinct domains: a catalytic domain and a structural domain. The catalytic domain is responsible for the protein's catalytic activity, while the structural domain interacts with DNA and plays a role in the protein's stability2.

The DEAD protein has a unique structure that is composed of a distinct N-terminal region, a catalytic domain, and a C-terminal region3. The N-terminal region is a 12 amino acid residue long and is located at the top of the double helix. It contains a single alpha-helical structure that is responsible for the protein's stability4. The catalytic domain is located at the N-terminus of the protein and consists of a single alpha-helix structure. catalytic activity and is composed of three amino acid residues5. The C-terminal region is located at the bottom of the double helix and consists of a series of beta-strands that are responsible for the protein's stability6.

The DEAD protein has a unique structure that is composed of a catalytic domain and a structural domain. The catalytic domain is responsible for the protein's catalytic activity, while the structural domain interacts with DNA and plays a role in the protein's stability.

Expression and function

The DEAD protein is expressed in a variety of organisms, including bacteria, archaea, and eukaryotes7. It is involved in the replication of DNA in eukaryotic cells8. The DEAD protein has been shown to play a role in the regulation of DNA replication in eukaryotic cells9.

In addition to its role in DNA replication, the DEAD protein has also been shown to play a role in the regulation of cell growth and differentiation10. It has been shown to play a role in the regulation of cell adhesion11.

Drug targeting

The DEAD protein has been shown to be a potential drug target in a variety of diseases12. The DEAD protein is known to be involved in a variety of cellular processes, including DNA replication, cell growth, and cell adhesion. As such, it is a potential target for drugs that are designed to inhibit these processes13.

One class of drugs that have been shown to interact with the DEAD protein is small molecules14. These drugs are designed to inhibit the activity of the DEAD protein and have been shown to be effective in a variety of diseases, including cancer15.

Another class of drugs that have been shown to interact with the DEAD protein are inhibitors of DNA replication16. These drugs work by inhibiting the activity of the DEAD protein, which is responsible for unwinding double-stranded DNA and separating the two complementary strands17.

Biomarker

The DEAD protein has been shown to be a potential biomarker for a variety of diseases18. The DEAD protein is expressed in a variety of tissues and cells, including blood cells, tissue

Protein Name: DEAD-box Helicase 25

Functions: ATP-dependent RNA helicase. Required for mRNA export and translation regulation during spermatid development (By similarity)

The "DDX25 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 DDX25 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

DDX27 | DDX28 | DDX31 | DDX39A | DDX39B | DDX39B-AS1 | DDX3P1 | DDX3X | DDX3Y | DDX4 | DDX41 | DDX42 | DDX43 | DDX46 | DDX47 | DDX49 | DDX5 | DDX50 | DDX50P1 | DDX51 | DDX52 | DDX53 | DDX54 | DDX55 | DDX56 | DDX59 | DDX59-AS1 | DDX6 | DDX60 | DDX60L | DDX6P1 | DEAF1 | Death-associated protein kinase | Decapping Complex | DECR1 | DECR2 | DEDD | DEDD2 | Dedicator of cytokinesis protein | DEF6 | DEF8 | DEFA1 | DEFA10P | DEFA11P | DEFA1B | DEFA3 | DEFA4 | DEFA5 | DEFA6 | DEFA7P | DEFA8P | DEFA9P | DEFB1 | DEFB103A | DEFB103B | DEFB104A | DEFB104B | DEFB105A | DEFB105B | DEFB106A | DEFB106B | DEFB107A | DEFB108B | DEFB108F | DEFB109A | DEFB109B | DEFB109C | DEFB110 | DEFB112 | DEFB113 | DEFB114 | DEFB115 | DEFB116 | DEFB118 | DEFB119 | DEFB121 | DEFB122 | DEFB123 | DEFB124 | DEFB125 | DEFB126 | DEFB127 | DEFB128 | DEFB129 | DEFB130A | DEFB131A | DEFB131B | DEFB132 | DEFB133 | DEFB134 | DEFB135 | DEFB136 | DEFB4A | DEFB4B | Defensin | DEFT1P | DEFT1P2 | DEGS1 | DEGS2 | DEK