Target Name: TDG
NCBI ID: G6996
Review Report on TDG Target / Biomarker Content of Review Report on TDG Target / Biomarker
TDG
Other Name(s): G/T mismatch-specific thymine DNA glycosylase (isoform 1) | hTDG | Thymine DNA glycosylase, transcript variant 1 | TDG variant 1 | G/T mismatch-specific thymine DNA glycosylase | TDG_HUMAN | Thymine-DNA glycosylase | thymine DNA glycosylase

TDG: A Potential Drug Target and Biomarker for G/T Mismatch-Specific Thymine DNA Glycosylase (ISO Form 1)

Thymine DNA glycosylase (TDG) is a DNA glycosylase enzyme that removes thymine residues from DNA. Thymine is a nucleotide base that is commonly found in DNA and RNA. It has important roles in various cellular processes, including DNA replication, transcription, and repair. TDG is one of the two known DNA glycosylases that remove thymine residues from DNA in the human body. The other is thymine kinase (TKG), which is involved in DNA repair and transcription.

G/T Mismatch-Specific Thymine DNA Glycosylase (ISO Form 1)

TDG is a member of the thymine glycosylase family, which includes DNA glycosylases that remove thymine residues from DNA. DNA glycosylases are important enzymes that maintain the integrity of DNA. They play a crucial role in DNA replication, transcription, and repair. TDG is specific for G/T mismatch-specific thymine DNA glycosylase (ISO Form 1).

TDG functions as a DNA glycosylase enzyme by removing thymine residues from DNA. It is involved in the repair of DNA damage caused by G/T mismatches. G/T mismatches are a common type of DNA damage that can occur during DNA replication, transcription, or repair. Mismatches can lead to the formation of a thymine dinucleotide, which can cause DNA double-strand breaks.

TDG is involved in the repair of G/T mismatches by removing the thymine residue from the damaged DNA. It does this by catalyzing the conversion of the thymine residue to its active form. This active form of thymine can then be removed from the DNA by a different DNA glycosylase enzyme called thymine kinase (TKG).

TDG is also involved in the transcription of DNA. It is a critical enzyme in the regulation of gene expression. DNA transcription is the process by which the instructions in a DNA template are translated into proteins. TDG plays a crucial role in regulating the accuracy of DNA transcription by removing thymine residues from the RNA produced during transcription.

TDG is a protein that is expressed in various tissues and cells in the human body. It is highly conserved, with a calculated pI of 6.9. TDG is primarily expressed in the cytoplasm of eukaryotic cells and is also found in the nucleus. It is a prokaryotic gene and has a single exon.

Drug Target and Biomarker

TDG is a potential drug target for G/T mismatch-specific thymine DNA glycosylase (ISO Form 1). The development of new therapeutics for DNA damage repair therapies is a major focus of research in the field of genetics. G/T mismatch-specific thymine DNA glycosylase (ISO Form 1) is a key enzyme in the repair of DNA damage caused by G/T mismatches.

The development of inhibitors of TDG could be a useful therapeutic approach for the treatment of various DNA-related diseases. For example, G/T mismatch-specific thymine DNA glycosylase (ISO Form 1) may be a drug target for the treatment of genetic diseases caused by DNA damage. DNA damage can cause a wide range of genetic diseases, including cancer, neurodegenerative diseases, and inherited disorders.

In addition to its potential therapeutic applications, TDG is also a potential biomarker for G/T mismatch-specific thymine DNA glycosylase (ISO Form 1). The development of new diagnostic tests for DNA damage repair disorders is a major focus of research in the field of genetics. G/T mismatch-specific thymine DNA glycosylase (ISO Form 1) may be a useful biomarker for

Protein Name: Thymine DNA Glycosylase

Functions: DNA glycosylase that plays a key role in active DNA demethylation: specifically recognizes and binds 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC) in the context of CpG sites and mediates their excision through base-excision repair (BER) to install an unmethylated cytosine. Cannot remove 5-hydroxymethylcytosine (5hmC). According to an alternative model, involved in DNA demethylation by mediating DNA glycolase activity toward 5-hydroxymethyluracil (5hmU) produced by deamination of 5hmC. Also involved in DNA repair by acting as a thymine-DNA glycosylase that mediates correction of G/T mispairs to G/C pairs: in the DNA of higher eukaryotes, hydrolytic deamination of 5-methylcytosine to thymine leads to the formation of G/T mismatches. Its role in the repair of canonical base damage is however minor compared to its role in DNA demethylation. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and a mispaired thymine. In addition to the G/T, it can remove thymine also from C/T and T/T mispairs in the order G/T >> C/T > T/T. It has no detectable activity on apyrimidinic sites and does not catalyze the removal of thymine from A/T pairs or from single-stranded DNA. It can also remove uracil and 5-bromouracil from mispairs with guanine

The "TDG 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 TDG 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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