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The protein encoded by HUS1 is a component of an evolutionarily conserved, genotoxin-activated checkpoint complex that is involved in the cell cycle arrest in response to DNA damage. Additionally we are shipping HUS1 Antibodies (59) and many more products for this protein.
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These results suggest that p21(Waf1/CIP1 (show CDKN1A Proteins)) and Hus1 play crucial roles in the generation and transmission of bystander damage signals after low-dose alpha-particle irradiation.
adenine glycosylase activity, mismatch recognition properties and interaction with protein partners of MUTYH (show MUTYH Proteins) and 5 MAP variants were examined; P502L and R520Q had reduced affinity for PCNA (show PCNA Proteins); only Q324H was found to have reduced affinity for Hus1
Intramolecular binding of the rad9 (show RAD9A Proteins) C-terminus in the checkpoint clamp (show PDZK1 Proteins) Rad9 (show RAD9A Proteins)-Hus1-Rad1 is closely linked with its DNA binding.
these pockets were not required for 9-1-1 chromatin localization or ATR (show ANTXR1 Proteins)-mediated CHK1 (show CHEK1 Proteins) activation but were necessary for interactions between HUS1 and its binding partner MYH (show MUTYH Proteins)
Expression of cell cycle regulatory factors hus1, gadd45a (show GADD45A Proteins), rb1 (show RB1 Proteins), cdkn2a and mre11a (show MRE11A Proteins) correlates with expression of clock gene per2 (show PER2 Proteins) in human colorectal carcinoma tissue.
HUS1 polymorphisms act as risk breast cancer modifiers in the group of non-carriers of BRCA1/2 mutations.
Data show models for the ternary PCNA (show PCNA Proteins)/FEN1 (show FEN1 Proteins)/DNA and Rad9 (show RAD9A Proteins)-Rad1-Hus1 (9-1-1 complex)/FEN1 (show FEN1 Proteins)/DNA assemblies.
The HUS1 is loaded to damaged sites where it serves as a platform for the selective recruitment of checkpoint and repair proteins.
The HUS1 protein interacts with casein kinase 2.
Rad9 (show RAD9A Proteins)-Rad1-Hus1 complex enhances in vitro activity of 8-oxoguanine DNA glycosylase (show OGG1 Proteins).
Whereas Hus1(neo/neo) and Atm(-/-) single mutant mice survived low-dose MMC similar to wild-type controls, Hus1(neo/neo)Atm(-/-) double mutants showed striking MMC hypersensitivity.
Disease severity in a mouse model of ataxia telangiectasia is modulated by the DNA damage checkpoint gene Hus1
HUS1 acts as a component of the canonical 9-1-1 complex during meiotic prophase I to promote DSB repair and further propose that RAD1 (show RAD1 Proteins) and TOPBP1 (show TOPBP1 Proteins) respond to unsynapsed chromatin through an alternative mechanism that does not require RAD9 (show RAD9A Proteins) or HUS1.
requirement for Hus1 in the survival and proliferation of mammary epithelium
Hus1 is required specifically for one of two separable mammalian checkpoint pathways that respond to distinct forms of genome damage during S phase.
Hus1-deficient mouse cells had an impaired S checkpoint after exposure to DNA strand break-inducing agents such as camptothecin or ionizing radiation
we show a requirement for Rad17 and Hus1 to induce G(2) arrest as well as Vpr-induced phosphorylation of histone 2A variant X (H2AX) and formation of nuclear foci containing H2AX and breast cancer susceptibility protein 1
results indicate that the role of Hus1 affecting the sensitivity of cells to IR-induced killing is independent of nonhomologous end-joining but might be linked to homologous recombination repair
Hus1 loss leads to chromosomal instability during DNA replication, triggering increased apoptosis and impaired proliferation through p53 (show TP53 Proteins)-independent mechanisms.
identify differential effects of altered Hus1 gene dosage on genome maintenance during in vitro culture, genotoxic stress responses, embryonic development, and adult homeostasis
The protein encoded by this gene is a component of an evolutionarily conserved, genotoxin-activated checkpoint complex that is involved in the cell cycle arrest in response to DNA damage. This protein forms a heterotrimeric complex with checkpoint proteins RAD9 and RAD1. In response to DNA damage, the trimeric complex interacts with another protein complex consisting of checkpoint protein RAD17 and four small subunits of the replication factor C (RFC), which loads the combined complex onto the chromatin. The DNA damage induced chromatin binding has been shown to depend on the activation of the checkpoint kinase ATM, and is thought to be an early checkpoint signaling event. Alternative splicing results in multiple transcript variants.
, checkpoint protein HUS1
, hus1+-like protein