NOP58: A Potential Drug Target and Biomarker (G51602)

Target Name: NOP58

NCBI ID: G51602

NOP58: A Potential Drug Target and Biomarker

N-Acetyl-L-Tyrosine (NAT) is a protein that is synthesized in the brain and plays a crucial role in the regulation of neurotransmitter release and neurotransmission. NOP58 is a specific protein that is derived from NAT. It is a 58 amino acid protein with a molecular weight of 61 kDa. NOP58 is expressed in various tissues of the brain including the prefrontal cortex, basal ganglia, and hypothalamus. It is highly conserved across species, which suggests that it may be a universal regulator of neurotransmission.

NOP58 has been shown to play a critical role in the regulation of neuronal excitability and synaptic plasticity. It is involved in the regulation of neurotransmitter release by interacting with the neurotransmitter receptors, which are involved in the regulation of neuronal excitability and synaptic plasticity. NOP58 has been shown to interact with dopamine receptors, which are involved in the regulation of motivation, pleasure, and reward.

NOP58 has also been shown to play a role in the regulation of ion channels, which are involved in the regulation of neuronal excitability and synaptic plasticity. NOP58 has been shown to interact with the ion channel protein, Nav1.2, which is involved in the regulation of neuronal excitability and synaptic plasticity.

NOP58 has been shown to be involved in the regulation of neurotransmitter release in response to different types of stimulation, such as sensory input or psychosocial stress. For example, NOP58 has been shown to be involved in the regulation of dopamine release in response to sensory input. Nop58 has been shown to interact with the dopamine receptor, which is involved in the regulation of motivation, pleasure, and reward.

NOP58 has also been shown to be involved in the regulation of neurotransmission in response to psychosocial stress. For example, NOP58 has been shown to be involved in the regulation of cortisol release in response to psychosocial stress. Nop58 has been shown to interact with the cortisol receptor, which is involved in the regulation of stress response.

In addition to its role in the regulation of neurotransmission, NOP58 has also been shown to play a role in the regulation of cellular processes, such as cell survival and cell proliferation. For example, NOP58 has been shown to be involved in the regulation of cell survival in response to oxidative stress. Nop58 has been shown to interact with the protein, Bcl-2, which is involved in the regulation of cell survival.

NOP58 has also been shown to play a role in the regulation of cellular processes in response to different types of stimulation, such as sensory input or psychosocial stress. For example, Nop58 has been shown to be involved in the regulation of neurotransmission in response to sensory input. Nop58 has been shown to interact with the dopamine receptor, which is involved in the regulation of motivation, pleasure, and reward.

In conclusion, NOP58 is a protein that is derived from NAT and is involved in the regulation of neurotransmission. NOP58 has been shown to play a critical role in the regulation of neuronal excitability and synaptic plasticity, as well as the regulation of cellular processes such as cell survival and proliferation. These properties make NOP58 a potential drug target and biomarker for the treatment of various neurological disorders.

Protein Name: NOP58 Ribonucleoprotein

Functions: Required for 60S ribosomal subunit biogenesis. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such as U3, U8 and U14 snoRNAs. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797)

More Common Targets