Target Name: TUB
NCBI ID: G7275
Review Report on TUB Target / Biomarker Content of Review Report on TUB Target / Biomarker
TUB
Other Name(s): TUB bipartite transcription factor | TUB bipartite transcription factor, transcript variant 1 | Tubby homolog | Rd5 | TUB variant 2 | TUBBY | Tubby homologue | tubby homologue | RDOB | tubby homolog | rd5 | Tubby protein homolog (isoform a) | tubby bipartite transcription factor | Tubby protein homolog | TUB variant 1 | Tubby protein homolog (isoform b) | TUB_HUMAN | TUB bipartite transcription factor, transcript variant 2

TUB: A Potential Drug Target and Biomarker for Stroke and Other Neural Trauma

Stroke is a leading cause of morbidity and mortality worldwide, affecting millions of individuals each year. The devastating effects of stroke not only impact the individual but also their family members and caregivers. The intricate neural repair process post-stroke is often accompanied by various neurological and cognitive impairments, making it an ongoing challenge for both researchers and clinicians.

TUB (Tubulin-associated protein), a key regulator of microtubules, has been identified as a potential drug target and biomarker for stroke. In this article, we will discuss the current understanding of TUB, its involvement in stroke pathology, and its potential as a therapeutic target.

Understanding TUB

TUB is a protein that plays a crucial role in the regulation of microtubules, which are dynamic cytoskeletal structures that organize and support various cellular processes. Microtubules are essential for cell division, intracellular transport, and the regulation of various cellular processes, including cytoskeletal organization and dynamics, cell signaling, and neurotransmitter release.

TUB is a member of the tubulin gene family, which encodes the protein subunits that make up microtubules. The tubulin protein is composed of several domains, including an alpha-helices domain, a beta-sheet domain, and a C-terminus that contains a glycine residue. The alpha-helices domain is responsible for the protein's stability and functions as a binding site for various ligands, while the beta-sheet domain and C-terminus contribute to the protein's stability and localization to the microtubules.

In addition to its role in regulating microtubules, TUB is also involved in the regulation of various cellular processes, including cell adhesion, migration, and the regulation of ion channels. TUB has been shown to play a critical role in the regulation of neurotransmitter release, particularly in the regulation of synaptic plasticity and learning.

Role in Stroke

Several studies have suggested that TUB may be involved in the pathogenesis of stroke. Stroke is a complex neurodegenerative disorder that is often associated with various cellular and molecular changes, including increased oxidative stress, inflammation, and neurotoxicity.

Research has shown that TUB is involved in the regulation of cellular stress responses, and that its activity may contribute to the increased risk of stroke. Several studies have demonstrated that TUB levels are affected by various stressors, including oxidative stress, inflammation, and neurotoxins. For example, TUB levels have been shown to increase in individuals exposed to environmental toxins, such as lead, cadmium, and arsenic, which are known to cause neurotoxicity.

Furthermore, TUB has been shown to play a critical role in the regulation of microtubule dynamics and stability, which may be relevant to the regulation of stroke. Microtubules are thought to play a crucial role in the regulation of cellular processes that are involved in stroke pathology, including the regulation of blood flow, neurotransmitter release, and inflammation.

Potential Therapeutic Strategies

Given the involvement of TUB in the regulation of various cellular processes and its potential role in stroke pathology, there is growing interest in using TUB as a therapeutic target. Several potential therapeutic strategies have been proposed to target TUB and its activity, including:

1. Small Molecule Antagonists: Small molecules have been shown to be effective in inhibiting the activity of TUB, potentially by binding to specific domains or modulating the levels of endogenous ligands. Several studies have shown that inhibitors of TUB, such as N-[1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-

Protein Name: TUB Bipartite Transcription Factor

Functions: Functions in signal transduction from heterotrimeric G protein-coupled receptors. Binds to membranes containing phosphatidylinositol 4,5-bisphosphate. Can bind DNA (in vitro). May contribute to the regulation of transcription in the nucleus. Could be involved in the hypothalamic regulation of body weight (By similarity). Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages

The "TUB 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 TUB 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

TUBA1A | TUBA1B | TUBA1B-AS1 | TUBA1C | TUBA3C | TUBA3D | TUBA3E | TUBA3FP | TUBA4A | TUBA4B | TUBA8 | TUBAL3 | TUBAP2 | TUBAP7 | TUBB | TUBB1 | TUBB2A | TUBB2B | TUBB2BP1 | TUBB3 | TUBB4A | TUBB4B | TUBB6 | TUBB7P | TUBB8 | TUBB8P2 | TUBB8P7 | TUBBP1 | TUBBP2 | TUBBP3 | TUBBP5 | TUBBP6 | TUBD1 | TUBE1 | TUBG1 | TUBG1P | TUBG2 | TUBGCP2 | TUBGCP3 | TUBGCP4 | TUBGCP5 | TUBGCP6 | Tubulin | TUFM | TUFMP1 | TUFT1 | TUG1 | TULP1 | TULP2 | TULP3 | TULP4 | Tumor Necrosis Factor Receptor Superfamily Member 10 (TRAIL-R) | Tumor-Associated Glycoprotein 72 (TAG-72) | TUNAR | TUSC1 | TUSC2 | TUSC2P1 | TUSC3 | TUSC7 | TUSC8 | TUT1 | TUT4 | TUT7 | TVP23A | TVP23B | TVP23C | TVP23C-CDRT4 | TVP23CP2 | TWF1 | TWF2 | TWIST | TWIST1 | TWIST2 | TWNK | TWSG1 | TWSG1-DT | TXK | TXLNA | TXLNB | TXLNG | TXLNGY | TXN | TXN2 | TXNDC11 | TXNDC12 | TXNDC15 | TXNDC16 | TXNDC17 | TXNDC2 | TXNDC5 | TXNDC8 | TXNDC9 | TXNIP | TXNL1 | TXNL1P1 | TXNL4A | TXNL4B | TXNP6 | TXNRD1 | TXNRD2