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Human Polyclonal BTBD12 Primary Antibody für IP - ABIN440495
Holloway, Mohan, Balmus, Sun, Modzelewski, Borst, Freire, Weiss, Cohen: Mammalian BTBD12 (SLX4) protects against genomic instability during mammalian spermatogenesis. in PLoS genetics 2011
Show all 3 Pubmed References
Human Polyclonal BTBD12 Primary Antibody für WB - ABIN529697
Fregoso, Emerman: Activation of the DNA Damage Response Is a Conserved Function of HIV-1 and HIV-2 Vpr That Is Independent of SLX4 Recruitment. in mBio 2016
Human Polyclonal BTBD12 Primary Antibody für ICC, IF - ABIN440496
Wan, Yin, Horvath, Sarkar, Chen, Wu, Wan, Lu, Gu, Yu, Lue, Chang, Liu, Lei: SLX4 assembles a telomere maintenance toolkit by bridging multiple endonucleases with telomeres. in Cell reports 2013
Loss-of-function mutations in SLX4 may contribute to the development of breast cancer in very rare cases
The BLM (zeige BLM Antikörper)-TOP3A (zeige TOP3A Antikörper)-RMI (BTR (zeige GPR148 Antikörper)) dissolvase complex is required for Alternative lengthening of telomeres-mediated telomere synthesis. BLM (zeige BLM Antikörper) and SLX4 play opposing roles in recombination-dependent replication at human telomeres.
Data suggest that dimeric GEN1 binds with high affinity/selectivity to Holliday junctions, introducing two symmetrical hydrolytic cleavages of phosphodiester backbone; at present, less is known about SLX1-SLX4-MUS81-EME1 resolving enzyme complex. (GEN1 = Holliday junction 5' flap endonuclease; SLX = structure-specific endonuclease subunit; MUS81 = MUS81 endonuclease; EME1 = essential meiotic endonuclease 1) [REVIEW]
These data also indicate that HIV-1 and HIV-2 Vpr activate the DNA damage response through an SLX4-independent mechanism that remains uncharacterized.
The functioning of SLX4 is dependent on its dimerization via an oligomerization motif called the BTB domain.
SLX4-SLX1 Protein-independent Down-regulation of MUS81-EME1 Protein by HIV-1 Viral Protein R (Vpr).
Results identified homozygous mutations in FANCA (zeige FANCA Antikörper) and FANCP/SLX4 genes, both located on chromosome 16, were the affected recessive FA genes in three and one family respectively. Genotyping with short tandem repeat markers and SNP arrays revealed uniparental disomy of the entire mutation-carrying chromosome 16 in all four patients.
SLX4 (FANCP) and XPF (zeige ERCC4 Antikörper) (FANCQ) proteins interact with each other and play a vital role in the Fanconi anemia (zeige PALB2 Antikörper) (FA) DNA repair pathway. Study has revealed that the global minor allele, SLX4(Y546C), is defective in this interaction.
SUMOylation and PARylation cooperate to recruit and stabilize SLX4 at DNA damage sites.
Identification and characterization of MUS81 (zeige MUS81 Antikörper) point mutations that abolish interaction with the SLX4 scaffold protein (zeige HOMER1 Antikörper).
Data shed light on SLX4 recruitment, and they point to the existence of currently unidentified ubiquitylated ligands and E3 ligases that are crucial for ICL repair.
SLX4 is a tumor suppressor, which activates XPF (zeige ERCC4 Antikörper)-ERCC1 (zeige ERCC1 Antikörper) nuclease (zeige DCLRE1C Antikörper) specificity in DNA crosslink repair.
Data indicate that SLX1 and MUS81 (zeige MUS81 Antikörper)-EME1 nucleases act together to resolve Holliday junctions (HJs) in a manner that requires tethering to SLX4.
these data indicate that BTBD12 functions throughout gametogenesis to maintain genome stability, possibly by co-ordinating repair processes and/or by linking DNA repair events to the cell cycle via ATM (zeige ATM Antikörper)
mouse Slx4, a regulator of structure-specific nucleases, disruption phenocopies Fanconi anemia (zeige PALB2 Antikörper)
This gene encodes a structure-specific endonuclease subunit. The encoded protein contains a central BTB domain and it forms a multiprotein complex with the ERCC4(XPF)-ERCC1, MUS81-EME1, and SLX1 endonucleases, and also associates with MSH2/MSH3 mismatch repair complex, telomere binding complex TERF2(TRF2)-TERF2IP(RAP1), the protein kinase PLK1 and the uncharacterized protein C20orf94. The multiprotein complex is required for repair of specific types of DNA lesions and is critical for cellular responses to replication fork failure. The encoded protein acts as a docking platform for the assembly of multiple structure-specific endonucleases.
BTB (POZ) domain containing 12
, SLX4 structure-specific endonuclease subunit homolog
, structure-specific endonuclease subunit SLX4
, BTB/POZ domain-containing protein 12