Target Name: EME1
NCBI ID: G146956
Review Report on EME1 Target / Biomarker Content of Review Report on EME1 Target / Biomarker
EME1
Other Name(s): Crossover junction endonuclease EME1 (isoform 1) | SLX2 structure-specific endonuclease subunit homolog A | MMS4L | essential meiotic endonuclease 1 homolog 1 | homolog of yeast EME1 endonuclease | hMMS4 | Crossover junction endonuclease EME1 | EME1 variant 1 | EME1_HUMAN | SLX2A | essential meiotic structure-specific endonuclease 1 | MMS4 homolog | Essential meiotic structure-specific endonuclease 1, transcript variant 1 | Essential meiotic structure-specific endonuclease 1, transcript variant 2 | essential meiotic endonuclease 1 homolog 2 | EME1 variant 2 | Crossover junction endonuclease EME1 (isoform 2) | Homolog of yeast EME1 endonuclease

EME1: A Potential Drug Target and Biomarker

EME1 (Crossover junction endonuclease) is a protein that is expressed in various cell types, including bacteria, archaea, and eukaryotes. It is a type of endonuclease, which is a enzyme that can cleave double-stranded DNA at specific recognition sites. EME1 is also known as isoform 1 and has been identified as a potential drug target or biomarker.

EME1 has been shown to play a role in the regulation of gene expression in various organisms. For example, studies have shown that EME1 can interact with the protein known as RNA polymerase II (RNA-P) and can influence the speed at which RNA-P recognizes and initiates transcription. Additionally, EME1 has been shown to play a role in the regulation of DNA replication, where it can interact with the protein known as DNA replication factor X (DNA-X).

EME1 has also been shown to be involved in the regulation of cell signaling pathways. For example, studies have shown that EME1 can interact with the protein known as PIK3CA, which is a gene that is involved in the regulation of cell signaling pathways. This interaction between EME1 and PIK3CA suggests that EME1 may be a potential drug target for the treatment of various diseases that are characterized by disrupted signaling pathways, such as cancer.

EME1 has also been shown to play a role in the regulation of inflammation. Studies have shown that EME1 can interact with the protein known as nuclear factor kappa B (NF-kappa-B), which is a protein that is involved in the regulation of inflammation. This interaction between EME1 and NF-kappa-B suggests that EME1 may be a potential drug target for the treatment of various inflammatory diseases.

In addition to its potential as a drug target, EME1 has also been shown to have potential as a biomarker. Studies have shown that EME1 can be expressed and purified from various cell types, including cancer cells, and can be used as a protein biomarker for the detection and diagnosis of various diseases. For example, EME1 has been shown to be expressed in various types of cancer, including breast cancer, and has been used as a protein biomarker for the detection of these cancers.

In conclusion, EME1 is a protein that has been shown to play a role in the regulation of various cellular processes, including gene expression, DNA replication, and cell signaling pathways. It has also been shown to play a role in the regulation of inflammation and has potential as a drug target or biomarker. Further research is needed to fully understand the role of EME1 in these processes and to determine its potential as a therapeutic agent.

Protein Name: Essential Meiotic Structure-specific Endonuclease 1

Functions: Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks

The "EME1 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 EME1 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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EME2 | EMG1 | EMID1 | EMILIN1 | EMILIN2 | EML1 | EML2 | EML2-AS1 | EML3 | EML4 | EML4-AS1 | EML5 | EML6 | EMP1 | EMP2 | EMP2P1 | EMP3 | EMSLR | EMSY | EMX1 | EMX2 | EMX2OS | EN1 | EN2 | ENAH | ENAM | ENC1 | ENDOD1 | ENDOG | Endogenous Retrovirus group K Env polyprotein (ERVK) | Endogenous retrovirus group K member 25 Pol protein-like, transcript variant X1 | EndoGlyx-1 | Endoplasmic reticulum collagen prolyl 3-hydroxylation complex | Endothelin receptor | Endothelin-Converting Enzymes (ECE) | Endothiapepsin | ENDOU | ENDOV | ENG | ENGASE | ENHO | ENKD1 | ENKUR | ENO1 | ENO1-AS1 | ENO1P1 | ENO1P4 | ENO2 | ENO3 | ENO4 | ENOPH1 | eNoSC Complex | ENOSF1 | ENOX1 | ENOX1-AS2 | ENOX2 | ENPEP | ENPP1 | ENPP2 | ENPP3 | ENPP4 | ENPP5 | ENPP6 | ENPP7 | ENPP7P10 | ENPP7P12 | ENPP7P7 | ENSA | ENSAP2 | ENTHD1 | ENTPD1 | ENTPD1-AS1 | ENTPD2 | ENTPD3 | ENTPD3-AS1 | ENTPD4 | ENTPD5 | ENTPD6 | ENTPD7 | ENTPD8 | ENTR1 | ENTREP1 | ENTREP2 | ENTREP3 | env | ENY2 | EOGT | EOLA1 | EOLA1-DT | EOLA2 | EOLA2-DT | EOMES | EP300 | EP300-AS1 | EP400 | EP400P1 | EPAS1 | EPB41 | EPB41L1 | EPB41L1-AS1