CUL4B: A Non-Coding RNA Molecule as A Cancer Drug Target and Biomarker

Target Name: CUL4B

NCBI ID: G8450

CUL4B

CUL4B: A Non-Coding RNA Molecule as A Cancer Drug Target and Biomarker

CUL4B (microRNA-4212), also known as MRXSC, is a non-coding RNA molecule that has been identified as a potential drug target and biomarker for various diseases, including cancer. Its unique structure and function have made it an attractive target for researchers to study, and its potential as a drug or biomarker has led to a great deal of interest and research in the field of neurodegenerative diseases.

CUL4B is a non-coding RNA molecule that is approximately 200 amino acids long. It is made up of a series of double-stranded RNA molecules that are held together by a single RNA-protein complex. This structure gives CUL4B a unique stability and stability, as well as a high tendency to form a stable complex with other molecules.

One of the key features of CUL4B is its ability to interact with a wide variety of molecules, including proteins, transcripts, and small molecules. This interaction with other molecules makes it a promising target for drugs and biomarkers.

CUL4B has been shown to play a role in the development and progression of various diseases, including cancer. For example, studies have shown that high levels of CUL4B are associated with an increased risk of cancer, and that inhibiting CUL4B can lead to therapeutic benefits in cancer treatment.

In addition to its potential as a cancer drug target, CUL4B has also been shown to be involved in a number of other biological processes, including cell signaling, metabolism, and neurodegenerative diseases.

CUL4B has also been shown to play a role in the development of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. Studies have shown that CUL4B is involved in the production of neurodegenerate proteins, and that inhibiting CUL4B can lead to therapeutic benefits in these diseases.

In addition to its potential as a drug or biomarker, CUL4B is also of interest to researchers because of its unique structure and function. The double-stranded RNA molecule is held together by a single RNA-protein complex, and this structure is unique among non-coding RNAs.

The study of CUL4B has also led to a greater understanding of the underlying mechanisms that control its function. Researchers have shown that CUL4B interacts with a wide variety of molecules, including proteins, transcripts, and small molecules. This interaction with other molecules allows CUL4B to control the activity of these molecules and to play a role in various biological processes.

In conclusion, CUL4B is a non-coding RNA molecule that has been identified as a potential drug target and biomarker for various diseases, including cancer. Its unique structure and function, as well as its ability to interact with a wide variety of molecules, make it an attractive target for researchers to study. Further research is needed to fully understand the role of CUL4B in disease and to develop effective treatments.

Protein Name: Cullin 4B

Functions: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14578910, PubMed:16322693, PubMed:16678110, PubMed:18593899, PubMed:29779948, PubMed:30166453, PubMed:33854232, PubMed:33854239, PubMed:22118460). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:29779948, PubMed:22118460). CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460). Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage (PubMed:14578910, PubMed:16678110, PubMed:18593899). Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication (PubMed:16678110). A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948). The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (PubMed:33854232, PubMed:33854239). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (PubMed:30166453). Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression (PubMed:16322693, PubMed:19801544). Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism (PubMed:18235224). Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (PubMed:18235224). With CUL4A, contributes to ribosome biogenesis (PubMed:26711351)

The "CUL4B 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 CUL4B 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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