Target Name: TBP
NCBI ID: G6908
Review Report on TBP Target / Biomarker Content of Review Report on TBP Target / Biomarker
TBP
Other Name(s): transcription initiation factor TFIID TBP subunit | TATA-box-binding protein (isoform 2) | TF2D | TATA-box factor | TATA-box binding protein N-terminal domain | TATA-box binding protein, transcript variant 2 | TBP variant 2 | SCA17 | TBP1 | GTF2D | TATA-box binding protein, transcript variant 1 | TFIID | TATA-box-binding protein (isoform 1) | TATA box binding protein | TBP_HUMAN | TBP variant 1 | Transcription initiation factor TFIID TBP subunit | TATA-box-binding protein | HDL4 | TATA-box binding protein | TATA-binding factor | TATA sequence-binding protein | GTF2D1

The Transcription Initiation Factor TFIID: A Promising Drug Target and Biomarker

Introduction

The Transcription Initiation Factor (TFIID) is a protein that plays a crucial role in the regulation of gene expression. TFIID is composed of two subunits, TFIID伪 and TFIID尾, which are involved in the formation of a complex that activates the transcription machinery. complex is essential for the initiation of transcription from RNA templates, and it has been implicated in various cellular processes, including cell growth, apoptosis, and inflammation.

Despite its importance, TFIID is still an unexplored drug target and biomarker. The lack of selective small molecules that can inhibit TFIID activity has hindered the study of its potential as a drug. However, recent studies have identified a new class of compounds, called NAD+ -dependent inhibitors, that can inhibit TFIID activity.

The NAD+-dependent inhibitors are a new class of small molecules that have been shown to be effective in various cellular processes, including the inhibition of TFIID activity. The unique feature of these inhibitors is their ability to inhibit TFIID activity without affecting the activity of other transcription factors, such as RNA polymerase II (RPNP) and corepressors.

Targeting TFIID

TFIID is a protein that can be targeted by small molecules due to its unique structure and its involvement in various cellular processes. The TFIID complex is composed of two subunits, TFIID伪 and TFIID尾, which are involved in the formation of a complex that activates the transcription machinery. The TFIID伪 subunit contains a N-terminal domain that is similar to the N-terminal domain of other transcription factors, such as RPNP and corepressors. The TFIID尾 subunit contains a C-terminal domain that is similar to the C-terminal domain of other transcription factors, such as RNA polymerase II (RPNP) and corepressors.

TFIID has been shown to play a role in various cellular processes, including cell growth, apoptosis, and inflammation. The TFIID complex is essential for the initiation of transcription from RNA templates, and it has been implicated in the regulation of gene expression. The TFIID complex can also interact with various transcription factors, including RPNP and corepressors.

In order to target TFIID, researchers have used various strategies, such as the use of small molecules and biochemical assays. The use of small molecules has been shown to be an effective way to inhibit TFIID activity. Researchers have synthesized various small molecules that are capable of inhibiting TFIID伪 and TFIID尾 activity. These small molecules have been shown to be effective in various cellular processes, including the inhibition of cell growth and the inhibition of apoptosis.

The NAD+-dependent inhibitors are a new class of small molecules that have been shown to be effective in inhibiting TFIID activity. These inhibitors are able to inhibit TFIID伪 and TFIID尾 activity without affecting the activity of other transcription factors. NAD+-dependent inhibitors have been shown to be effective in various cellular processes, including the inhibition of cell growth and the inhibition of apoptosis.

Mechanism of Action

The mechanism of action of the NAD+-dependent inhibitors is based on the inhibition of the NAD+-dependent TF-ID3-dependent redox reaction (NAD+-dependent redox reaction). This reaction is

Protein Name: TATA-box Binding Protein

Functions: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473, PubMed:27193682, PubMed:2194289, PubMed:2363050, PubMed:2374612). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473, PubMed:27007846). The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C (PubMed:33795473). TBP forms the TFIID-A module together with TAF3 and TAF5 (PubMed:33795473). TBP is a general transcription factor that functions at the core of the TFIID complex (PubMed:33795473, PubMed:27193682, PubMed:2194289, PubMed:2363050, PubMed:2374612, PubMed:9836642). During assembly of the core PIC on the promoter, as part of TFIID, TBP binds to and also bends promoter DNA, irrespective of whether the promoter contains a TATA box (PubMed:33795473). Component of a BRF2-containing transcription factor complex that regulates transcription mediated by RNA polymerase III (PubMed:26638071). Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC during RNA polymerase I-dependent transcription (PubMed:15970593). The rate of PIC formation probably is primarily dependent on the rate of association of SL1 with the rDNA promoter (PubMed:15970593). SL1 is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA (PubMed:15970593)

The "TBP 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 TBP 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

TBPL1 | TBPL2 | TBR1 | TBRG1 | TBRG4 | TBX1 | TBX10 | TBX15 | TBX18 | TBX18-AS1 | TBX19 | TBX2 | TBX20 | TBX21 | TBX22 | TBX3 | TBX4 | TBX5 | TBX5-AS1 | TBX6 | TBXA2R | TBXAS1 | TBXT | TC2N | TCAF1 | TCAF1P1 | TCAF2 | TCAIM | TCAM1P | TCAP | TCEA1 | TCEA1P2 | TCEA2 | TCEA3 | TCEAL1 | TCEAL2 | TCEAL3 | TCEAL4 | TCEAL5 | TCEAL6 | TCEAL7 | TCEAL8 | TCEAL9 | TCEANC | TCEANC2 | TCERG1 | TCERG1L | TCF12 | TCF12-DT | TCF15 | TCF19 | TCF20 | TCF21 | TCF23 | TCF24 | TCF25 | TCF3 | TCF4 | TCF7 | TCF7L1 | TCF7L2 | TCFL5 | TCHH | TCHHL1 | TCHP | TCIM | TCIRG1 | TCL1A | TCL1B | TCL6 | TCN1 | TCN2 | TCOF1 | TCP1 | TCP10L | TCP10L2 | TCP10L3 | TCP11 | TCP11L1 | TCP11L2 | TCP11X2 | TCTA | TCTE1 | TCTN1 | TCTN2 | TCTN3 | TDG | TDGF1 | TDGF1P3 | TDGP1 | TDH | TDH-AS1 | TDO2 | TDP1 | TDP2 | TDRD1 | TDRD10 | TDRD12 | TDRD15 | TDRD3