Target Name: NONO
NCBI ID: G4841
Review Report on NONO Target / Biomarker Content of Review Report on NONO Target / Biomarker
NONO
Other Name(s): NMT55 | OTTHUMP00000023506 | MRXS34 | PPP1R114 | Non-POU domain-containing octamer-binding protein | Non-POU domain containing octamer binding, transcript variant 2 | Non-POU domain-containing octamer-binding protein (isoform 1) | protein phosphatase 1, regulatory subunit 114 | NRB54 | non-POU domain containing octamer binding | OTTHUMP00000023508 | NONO_HUMAN | NONO variant 1 | p54(nrb) | Non-POU domain containing octamer binding, transcript variant 1 | P54 | NONO variant 2 | NonO protein | OTTHUMP00000023507 | non-POU domain-containing octamer (ATGCAAAT) binding protein | P54NRB | p54nrb | 55 kDa nuclear protein | Non-POU domain-containing octamer (ATGCAAAT) binding protein | 54 kDa nuclear RNA- and DNA-binding protein | DNA-binding p52/p100 complex, 52 kDa subunit

NONO: A Potential Drug Target and Biomarker for Myeloma

NONO (NMT55) is a non-coding RNA molecule that has been identified as a potential drug target and biomarker. It is a key regulator of the myeloid-specific gene expression, and its levels have been shown to be reduced in multiple myeloma samples compared to healthy myeloid cells.

Myeloma is a type of cancer that arises from a single clone of white blood cells called a myeloma cell. This cancer is characterized by the uncontrolled growth and proliferation of these myeloma cells, which can lead to a variety of serious health complications such as bone pain, fatigue, and shortness of breath.

NONO has been shown to play a key role in the regulation of myeloma cell growth and proliferation. It is a non-coding RNA molecule that is expressed in the myeloid cells, and it has been shown to regulate the expression of genes involved in cell growth, differentiation, and survival.

One of the most promising aspects of NONO is its potential as a drug target. NONO has been shown to interact with a variety of signaling pathways, including TGF-β, NF-kappa-B, and PI3K/AKT. These signaling pathways are involved in the regulation of cell growth, differentiation, and survival, and targeting them with drugs has been shown to be effective in treating a variety of diseases.

In addition to its potential as a drug target, NONO has also been shown to be a potential biomarker for the diagnosis and prognosis of myeloma. Its levels have been shown to be reduced in myeloma samples compared to healthy myeloid cells, and its levels have been used as a biomarker in a variety of clinical trials.

NONO is also a good candidate as a potential therapeutic target for the treatment of myeloma, it may also be a good biomarker for the monitoring of the disease progression and the response to the treatment.

In conclusion, NONO is a non-coding RNA molecule that has been identified as a potential drug target and biomarker in myeloma. Its levels have been shown to be reduced in myeloma samples compared to healthy myeloid cells, and it has been shown to play a key role in the regulation of myeloma cell growth and proliferation. Further studies are needed to fully understand the potential of NONO as a drug target and biomarker for the treatment of myeloma.

Protein Name: Non-POU Domain Containing Octamer Binding

Functions: DNA- and RNA binding protein, involved in several nuclear processes (PubMed:11525732, PubMed:12403470, PubMed:26571461). Binds the conventional octamer sequence in double-stranded DNA (PubMed:11525732, PubMed:12403470, PubMed:26571461). Also binds single-stranded DNA and RNA at a site independent of the duplex site (PubMed:11525732, PubMed:12403470, PubMed:26571461). Involved in pre-mRNA splicing, probably as a heterodimer with SFPQ (PubMed:11525732, PubMed:12403470, PubMed:26571461). Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b (PubMed:12403470). Together with PSPC1, required for the formation of nuclear paraspeckles (PubMed:22416126). The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs (PubMed:11525732). The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1 (PubMed:10858305). The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends (PubMed:15590677). In vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex (PubMed:15590677). NONO is involved in transcriptional regulation. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity (PubMed:11897684). NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription (By similarity). Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer (By similarity). Important for the functional organization of GABAergic synapses (By similarity). Plays a specific and important role in the regulation of synaptic RNAs and GPHN/gephyrin scaffold structure, through the regulation of GABRA2 transcript (By similarity). Plays a key role during neuronal differentiation by recruiting TET1 to genomic loci and thereby regulating 5-hydroxymethylcytosine levels (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728, PubMed:30270045). Promotes activation of the cGAS-STING pathway in response to HIV-2 infection: acts by interacting with HIV-2 Capsid protein p24, thereby promoting detection of viral DNA by CGAS, leading to CGAS-mediated inmmune activation (PubMed:30270045). In contrast, the weak interaction with HIV-1 Capsid protein p24 does not allow activation of the cGAS-STING pathway (PubMed:30270045)

The "NONO 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 NONO 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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