Target Name: EXOSC1
NCBI ID: G51013
Review Report on EXOSC1 Target / Biomarker Content of Review Report on EXOSC1 Target / Biomarker
EXOSC1
Other Name(s): hCsl4p | Exosomal core protein CSL4 | EXOS1_HUMAN | PCH1F | 3'-5' exoribonuclease CSL4 homolog | RP11-452K12.9 | p13 | Exosome complex component CSL4 | EXOSC1 variant 1 | SKI4 | Csl4p | Ski4p | CSL4 e

EXOSC1: A Potential Drug Target for Cancer and Other Diseases

EXOSC1 (hCsl4p), a protein found in various tissues throughout the body, 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 develop new treatments.

EXOSC1 is a transmembrane protein that is expressed in various tissues, including the brain, heart, liver, and muscle. Its primary function is to regulate the activity of a protein called p21, which is a key regulator of the cell cycle. EXOSC1 helps to keep p21 in a state of inactivity, which is necessary for cell growth and division.

One of the key features of EXOSC1 is its unique structure. It consists of four transmembrane domains and a cytoplasmic tail. The transmembrane domains are responsible for the protein's stability and its ability to interact with other proteins. The cytoplasmic tail is responsible for the protein's stability and its ability to interact with the endoplasmic reticulum.

EXOSC1 has been shown to play a key role in the regulation of cell growth and division. Studies have shown that EXOSC1 helps to keep p21 in a state of inactivity by binding to it and preventing it from interacting with other proteins. This interaction between EXOSC1 and p21 is critical for normal cell growth and division.

In addition to its role in cell growth and division, EXOSC1 has also been shown to play a key role in the regulation of cell survival. Studies have shown that EXOSC1 helps to prevent the loss of p21, which is a key regulator of the cell cycle. This interaction between EXOSC1 and p21 is critical for the regulation of cell survival.

EXOSC1 has also been shown to play a key role in the regulation of inflammation. Studies have shown that EXOSC1 helps to regulate the activity of immune cells, which are responsible for fighting off infections and diseases. This interaction between EXOSC1 and immune cells is critical for the regulation of inflammation.

In conclusion, EXOSC1 is a unique protein that has been shown to play a key role in the regulation of cell growth and division, cell survival, and inflammation. Its unique structure and function make it an attractive target for researchers to study and develop new treatments for a variety of diseases. Further research is needed to fully understand the role of EXOSC1 in the regulation of cell biology and to develop new treatments for diseases that are caused by its dysfunction.

Protein Name: Exosome Component 1

Functions: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC1 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC6 and EXOSC8

The "EXOSC1 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 EXOSC1 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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EXOSC10 | EXOSC10-AS1 | EXOSC2 | EXOSC3 | EXOSC4 | EXOSC5 | EXOSC6 | EXOSC7 | EXOSC8 | EXOSC9 | Exosome Complex | EXPH5 | EXT1 | EXT2 | EXTL1 | EXTL2 | EXTL2P1 | EXTL3 | EXTL3-AS1 | EYA1 | EYA2 | EYA3 | EYA4 | EYS | EZH1 | EZH2 | EZHIP | EZR | F10 | F11 | F11-AS1 | F11R | F12 | F13A1 | F13B | F2 | F2R | F2RL1 | F2RL2 | F2RL3 | F3 | F5 | F7 | F8 | F8A1 | F8A2 | F8A3 | F9 | FA2H | FAAH | FAAH2 | FAAHP1 | FAAP100 | FAAP20 | FAAP24 | FABP1 | FABP12 | FABP2 | FABP3 | FABP4 | FABP5 | FABP5P1 | FABP5P10 | FABP5P11 | FABP5P2 | FABP5P3 | FABP5P7 | FABP6 | FABP7 | FABP7P1 | FABP9 | FACT complex | FADD | FADS1 | FADS2 | FADS2B | FADS3 | FADS6 | FAF1 | FAF2 | FAH | FAHD1 | FAHD2A | FAHD2B | FAHD2CP | FAIM | FAIM2 | FALEC | FAM104A | FAM104B | FAM106A | FAM106C | FAM107A | FAM107B | FAM110A | FAM110B | FAM110C | FAM110D | FAM111A | FAM111A-DT