Target Name: RAD51AP1
NCBI ID: G10635
Review Report on RAD51AP1 Target / Biomarker Content of Review Report on RAD51AP1 Target / Biomarker
RAD51AP1
Other Name(s): R51A1_HUMAN | RAD51-associated protein 1 | RAD51 associated protein 1, transcript variant 2 | RAD51AP1 variant 2 | RAD51-interacting protein | HsRAD51AP1 | PIR51 | hsRAD51AP1 | RAD51-associated protein 1 (isoform b) | RAD51AP1 variant 1 | RAD51 associated protein 1 | RAD51-associated protein 1 (isoform a) | RAD51 associated protein 1, transcript variant 1

RAD51AP1: A Potential Drug Target and Biomarker

Rad51AP1, also known as R51A1, is a non-coding RNA molecule that has been identified as a potential drug target and biomarker for various diseases, including cancer. Its unique structure and biology make it an attractive target for drug developers due to its ability to regulate gene expression and contribute to the development of cancer.

The RAD51AP1 molecule is part of the RAD51 family of proteins, which are known for their role in DNA repair and replication. RAD51AP1 is a 22-kDa RNA molecule that contains 106 amino acid residues. It has a unique feature, known as a double-stranded RNA structure, which is composed of two interconnected strands that are held together by a disulfide bond. This structure is formed by a specific kind of RNA-protein complex, which is composed of the protein R51 and the RNA molecule itself.

The RAD51AP1 gene was identified in various organisms, including humans, using next-generation sequencing technologies. The gene has been shown to be expressed in various tissues and organs, including the brain, lung, heart, and gastrointestinal tract. It has also been shown to be involved in various cellular processes, including cell growth, apoptosis, and DNA replication.

One of the most promising aspects of RAD51AP1 is its potential as a drug target. The RAD51AP1 gene has been shown to be involved in various cellular processes that are associated with the development and progression of cancer. For example, RAD51AP1 has been shown to be involved in the regulation of cell apoptosis, which is the process by which cells die naturally when they are no longer needed. In cancer cells, the regulation of apoptosis can be disrupted, leading to the continued growth and proliferation of cancer cells.

In addition to its potential as a drug target, RAD51AP1 has also been identified as a potential biomarker for cancer. The RAD51AP1 gene has been shown to be expressed in various types of cancer, including breast, lung, and ovarian cancer. Additionally, studies have shown that RAD51AP1 has been associated with poor prognosis in cancer patients.

The discovery of RAD51AP1 as a potential drug target and biomarker has generated a lot of interest in the field of cancer research. Many researchers are actively exploring the effects of drugs that can modulate RAD51AP1 expression and activity. This has led to the development of various compounds that have been shown to inhibit RAD51AP1 activity and are being tested as potential cancer treatments.

In addition to its potential as a drug target, RAD51AP1 has also been shown to have potential as a biomarker for cancer. Its expression has been associated with the development and progression of various types of cancer, including breast, lung, and ovarian cancer. This suggests that RAD51AP1 may be a useful biomarker for cancer diagnosis and treatment.

In conclusion, RAD51AP1 is a non-coding RNA molecule that has been identified as a potential drug target and biomarker for various diseases, including cancer. Its unique structure and biology make it an attractive target for drug developers, and its involvement in various cellular processes that are associated with the development and progression of cancer makes it an promising candidate as a drug or biomarker. Further research is needed to fully understand the effects of RAD51AP1 on cancer biology and to develop effective treatments.

Protein Name: RAD51 Associated Protein 1

Functions: Structure-specific DNA-binding protein involved in DNA repair by promoting RAD51-mediated homologous recombination (PubMed:17996710, PubMed:17996711, PubMed:20871616, PubMed:25288561, PubMed:26323318). Acts by stimulating D-Loop formation by RAD51: specifically enhances joint molecule formation through its structure-specific DNA interaction and its interaction with RAD51 (PubMed:17996710, PubMed:17996711). Binds single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures: has a strong preference for branched-DNA structures that are obligatory intermediates during joint molecule formation (PubMed:9396801, PubMed:17996711, PubMed:22375013, PubMed:17996710). Cooperates with WDR48/UAF1 to stimulate RAD51-mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during homologous recombination and DNA repair (PubMed:27463890, PubMed:27239033, PubMed:32350107). WDR48/UAF1 and RAD51AP1 also have a coordinated role in DNA-binding to promote USP1-mediated deubiquitination of FANCD2 (PubMed:31253762). Also involved in meiosis by promoting DMC1-mediated homologous meiotic recombination (PubMed:21307306). Key mediator of alternative lengthening of telomeres (ALT) pathway, a homology-directed repair mechanism of telomere elongation that controls proliferation in aggressive cancers, by stimulating homologous recombination (PubMed:31400850). May also bind RNA; additional evidences are however required to confirm RNA-binding in vivo (PubMed:9396801)

The "RAD51AP1 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 RAD51AP1 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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RAD51AP2 | RAD51B | RAD51C | RAD51D | RAD51L3-RFFL | RAD52 | RAD54B | RAD54L | RAD54L2 | RAD9A | RAD9B | RADIL | RADX | RAE1 | RAET1E | RAET1E-AS1 | RAET1G | RAET1K | RAET1L | Raf kinase | RAF1 | RAF1P1 | RAG1 | RAG2 | Ragulator Complex | RAI1 | RAI14 | RAI2 | RALA | RALB | RALBP1 | RALBP1P1 | RalGAP1 complex | RALGAPA1 | RALGAPA2 | RALGAPB | RALGDS | RALGPS1 | RALGPS2 | RALY | RALYL | RAMAC | RAMACL | RAMP1 | RAMP2 | RAMP2-AS1 | RAMP3 | RAN | RANBP1 | RANBP10 | RANBP17 | RANBP1P1 | RANBP2 | RANBP3 | RANBP3-DT | RANBP3L | RANBP6 | RANBP9 | RANGAP1 | RANGRF | RANP1 | RANP6 | RAP1A | RAP1B | RAP1BL | RAP1GAP | RAP1GAP2 | RAP1GDS1 | RAP2A | RAP2B | RAP2C | RAP2C-AS1 | RAPGEF1 | RAPGEF2 | RAPGEF3 | RAPGEF4 | RAPGEF4-AS1 | RAPGEF5 | RAPGEF6 | RAPGEFL1 | RAPH1 | RAPSN | RARA | RARA-AS1 | RARB | RARG | RARRES1 | RARRES2 | RARS1 | RARS2 | Ras GTPase | Ras-Related C3 Botulinum Toxin Substrate (RAC) | Ras-related protein Ral | RASA1 | RASA2 | RASA3 | RASA4 | RASA4B | RASA4CP | RASA4DP