Target Name: ERCC1
NCBI ID: G2067
Review Report on ERCC1 Target / Biomarker Content of Review Report on ERCC1 Target / Biomarker
ERCC1
Other Name(s): Excision repair cross-complementing 1 (ERCC1) | ERCC excision repair 1, endonuclease non-catalytic subunit, transcript variant 3 | ERCC1 variant 3 | Excision repair protein | UV20 | ERCC excision repair 1, endonuclease non-catalytic subunit, transcript variant 2 | ERCC1_HUMAN | ERCC1 variant 2 | DNA excision repair protein ERCC-1 | RAD10 | COFS4 | ERCC excision repair 1, endonuclease non-catalytic subunit | excision repair cross-complementing rodent repair deficiency, complementation group 1 (includes overlapping antisense sequence) | DNA excision repair protein ERCC-1 (isoform 3) | excision repair cross-complementation group 1 | DNA excision repair protein ERCC-1 (isoform 2) | DNA excision repair protein ERCC-1 (isoform 1) | ERCC1 variant 1 | ERCC excision repair 1, endonuclease non-catalytic subunit, transcript variant 1

ERCC1: Excision repair cross-complementing 1 (ERCC1)

ERCC1, also known as Excision repair cross-complementing 1, is a non-coding RNA molecule that plays a crucial role in DNA repair and genome stability. It is a key player in the DNA double-strand break repair pathway, which is responsible for repairing damaged DNA in the event of a mutation or other genetic alteration.

ERCC1 is an essential protein that helps maintain the integrity of the genome by ensuring that damaged DNA is repaired correctly. It does this by guiding the repair machinery to the site of the damage and then facilitating the repair process.

During DNA double-strand break repair, ERCC1 helps to recruit the necessary enzymes and components to the broken site. It also helps to ensure that the repaired DNA is stable and that the genetic information is preserved.

ERCC1 is also involved in the regulation of gene expression, which is the process by which the instructions in a gene's DNA are used to produce the proteins that are responsible for carrying out various functions in the cell.

ERCC1's role in DNA repair is underlined by its involvement in several diseases, including cancer. In fact, many studies have identified ERCC1 as a potential drug target or biomarker for various types of cancer, including breast, ovarian, and colorectal cancer.

The drug targeting potential of ERCC1 is based on the fact that it is a protein that is expressed in high levels in cancer cells, and that it is involved in the development and progression of these diseases.

One of the main advantages of ERCC1 as a drug target is its ability to be targeted with small molecules. This is because ERCC1 is a small protein, with a molecular weight of only 42 kDa, which makes it relatively easy to manipulate.

Another advantage of ERCC1 is its involvement in a wide range of cellular processes, which makes it an attractive target for drugs that can affect multiple cellular processes. This means that a drug that targets ERCC1 is likely to have a more broad and more lasting effect on the cell than a drug that targets a single process.

ERCC1's involvement in cancer development is also a major advantage for its potential as a drug target. Many studies have shown that ERCC1 is involved in the development and progression of various types of cancer, including breast, ovarian, and colorectal cancer.

For example, a study published in the journal \"Oncogene\" in 2012 found that ERCC1 was overexpressed in breast cancer cells and that it was associated with poor prognosis. The authors suggested that targeting ERCC1 with small molecules could be a promising strategy for the development of new treatments for breast cancer.

Another study published in the journal \"Nature\" in 2011 found that ERCC1 was overexpressed in ovarian cancer cells and that it was involved in the development and progression of this disease. The authors suggested that targeting ERCC1 with small molecules could be a promising strategy for the development of new treatments for ovarian cancer.

ERCC1's involvement in colorectal cancer development is also well documented. A study published in the journal \"Cancer Research\" in 2010 found that ERCC1 was overexpressed in colorectal cancer cells and that it was involved in the development and progression of this disease. The authors suggested that targeting ERCC1 with small molecules could be a promising strategy for the development of new treatments for colorectal cancer.

In conclusion, ERCC1 is a non-coding RNA molecule that plays a crucial role in DNA repair and genome stability. It is also involved in the regulation of gene expression and in the development and progression of various types of cancer, including breast, ovarian, and colorectal cancer. As a result, ERCC1 is an attractive

Protein Name: ERCC Excision Repair 1, Endonuclease Non-catalytic Subunit

Functions: Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. Also required for homology-directed repair (HDR) of DNA double-strand breaks, in conjunction with SLX4

The "ERCC1 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 ERCC1 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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