SAMHD1 Antibody

1. Data show that SAM Domain and HD Domain-Containing Protein 1 (SAMHD1) is specifically targeted by protein phosphatase 2 regulatory subunit Balpha protein (PP2A-B55alpha) holoenzymes during mitotic exit. PMID: 29884836
2. SAMHD1 activity can significantly enhance or decrease the anti-HIV-1 efficacy of nucleotide analogue reverse transcription inhibitors presumably as a result of modulating dNTP pools that compete for recruitment by viral polymerases. PMID: 28220857
3. SAMHD1 is not localized in dot-like structures under DNA double-strand break induction in HeLa cells. PMID: 29614270
4. study considerably extends the picture of pathways involved in molecular pathogenesis of T-PLL and identifies the tumor suppressor gene SAMHD1 with ~20% of T-PLL affected by destructive lesions likely as major player in T-PLL pathogenesis. PMID: 29352181
5. Compared with control cells, infection of SAMHD1-silenced human monocytic cells or primary macrophages with Sendai virus or HIV-1, or treatment with inflammatory stimuli, induces significantly higher levels of NF-kappaB activation and IFN-I induction. SAMHD1 down-regulates innate immune responses to viral infections and inflammatory stimuli. PMID: 29610295
6. SAMHD1 is thus an important player in the replication stress response, which prevents chronic inflammation by limiting the release of single-stranded DNA from stalled replication forks PMID: 29670289
7. Low SAMHD1 expression is associated with HIV-1 infection. PMID: 29084722
8. Multiple domains of SAMHD1(e.g., N-terminus, nuclear localization signal, linker, HD domain, and C-terminus)are essential for Vpx-induced degradation.[review] PMID: 29963825
9. findings indicate a novel role for SAMHD1 in regulating HIV-1 latency, which enhances our understanding of the mechanisms regulating proviral gene expression in CD4(+) T cells. PMID: 29793958
10. results demonstrate that the interaction of CD81 with SAMHD1 controls the metabolic rate of HIV-1 replication by tuning the availability of building blocks for reverse transcription, namely dNTPs PMID: 28871089
11. Immune activation during HIV-1 infection influences SAMHD1 expression and degradation. PMID: 27922067
12. Studies of the phosphomimetic and tetramerization-defective mutants of SAMHD1 reveal poor correlation between tetramerization propensity and dNTPase activity observed in vitro and the ability of the proteins to deplete cellular dNTPs and to restrict retroviral restriction. These results suggest that enzymatic activity of SAMHD1 may be subject to additional cellular regulatory mechanisms that have not yet been elucidated. PMID: 27511536
13. Upregulation of endogenous SAMHD1 expression is attributed to the phosphorylation and nuclear translocation of IRF3. PMID: 27411355
14. Findings define a dNTPase-independent function for SAMHD1 in HR-mediated DSB repair by facilitating CtIP accrual to promote DNA end resection, providing insight into how SAMHD1 promotes genome integrity. PMID: 28834754
15. These results indicate that Vpx, in addition to SAMHD1, overcomes a previously unappreciated restriction for lentiviruses at the level of reverse transcription (RT)that acts independently of dNTP concentrations and is specific to resting CD4 T cells. PMID: 28228523
16. results indicate that the RXL motif is critical for tetramer formation, dNTPase activity, and HIV-1 restriction. These findings help us understand SAMHD1 interactions with other host proteins and the mechanisms regulating SAMHD1 structure and functions in cells. PMID: 29321329
17. These results suggest that SAMHD1 is a relevant restriction factor for HBV and restricts reverse transcription through its dNTPase activity PMID: 27229711
18. SAMHD1 may constitute a promising target to improve a wide range of therapies for both hematological and non-haematological malignancies. PMID: 28436707
19. Study demonstrates a consistent resistance profile to PARPi and a unique cross-resistance profile to non-PARPi drugs in different PARPi-resistant U251 glioblastoma cells and reveals 53BP1 loss and SAMHD1 overexpression as the primary mechanisms responsible for their resistance to PARPi and Ara-C, respectively. PMID: 29274141
20. Study identify three critical cysteine residues of SAMHD1 (Cys341, Cys350, and Cys522) that create a ''redox switch'' through the formation of intrachain disulfide bonds to reversibly inhibit SAMHD1 tetramerization and dNTPase activity. SAMHD1 is oxidized in cells in response to proliferative signals and colocalizes with sites of protein oxidation outside of the nucleus. PMID: 28398823
21. our work genetically separated the ability of SAMHD1 to negatively regulate the type I IFN response from its ability to restrict HIV-1. PMID: 28229507
22. MiR-181a is an important mediator for interferons-induced SAMHD1 expression in astrocytes and microglia, but not for inhibition of HIV-1 infection induced by IFN-alpha. PMID: 27219130
23. SAMHD1 is active in HIV-1 permissive cells, does not modify susceptibility to HIV-1 infection but strongly affects sensitivity to nucleoside inhibitors. PMID: 28359840
24. expression of p21 potentially can contribute to inhibition of HIV-1 replication in monocyte-derived dendritic cells through multiple mechanisms. p21 decreased size of the intracellular dNTP pool; p21 prevented SAMHD1 phosphorylation and promoted SAMHD1 dNTPase-independent antiviral activity PMID: 28931685
25. Studies indicate the ambiguous properties of sterile alpha motif and histidine/aspartic acid domain-containing protein 1 (SAMHD1) as both an inhibitor of uncontrolled proliferation and a resistance factor limiting the efficacy of anticancer treatments. PMID: 28502830
26. stereoselective 2' substitutions that reveal nucleotide substrate specificity for SAMHD1, and a novel inhibitory mechanism for the dNTPase activity of SAMHD1, are reported. PMID: 28046007
27. Allosteric regulation of SAMHD1 has been uncovered through molecular dynamics simulations. PMID: 28321930
28. Cell cycle-associated changes of proteins are induced by activation of the Raf/MEK/ERK kinase cascade, culminating in upregulation of CDK1 with subsequent SAMHD1 T592 phosphorylation and deactivation of its antiviral activity. PMID: 28122869
29. SAMHD1 acts as an inhibitor in cutaneous T-cell lymphoma cell growth. PMID: 27929746
30. miR-181 is an important regulator of SAMHD1 protein expression in neoplastic CD4+ T-cells, likely through a mechanism of translational inhibition PMID: 27889686
31. the mechanisms by which SAMHD1 is phosphorylated and suggest the contribution of cyclin binding to SAMHD1 expression and stability in dividing cells. PMID: 27815502
32. Our findings will facilitate more advanced studies into the role of the SAMHD1 RNase function in the cellular pathogenesis implicated in nucleic acid-triggered inflammatory responses and the anti-retroviral function of SAMHD1. PMID: 27387229
33. Comparison of the wild-type SAMHD1 and the T592D mutant reveals that the phosphomimetic mutation affects the rates of tetramer dissociation, but has no effect on the equilibrium of allosteric activation by deoxynucleotides. PMID: 27566548
34. data suggest an antagonistic regulatory mechanism in which the mutually exclusive oligomeric state requirements for ssNA binding and dNTP hydrolase activity modulate these two functions of SAMHD1 within the cell PMID: 27775344
35. These results indicate that SAMHD1 inhibits HBV replication at the reverse transcription step, most likely through the depletion of cellular dNTPs. PMID: 27179347
36. Our results suggest that SAMHD1, through its dNTPase activity, affects cell proliferation, cell cycle distribution and apoptosis, and emphasize a key role of SAMHD1 in the interplay between cell cycle regulation and HIV-1 infection. PMID: 27183329
37. This study reviewed that Neurologic Phenotypes Associated with Mutations in SAMHD1 in patients with Aicardi-Goutieres Syndrome. PMID: 27643693
38. cytokines play a major role in the reservoir establishment not only by driving homeostatic proliferation but also by increasing susceptibility of CD4+ lymphocytes to HIV-1 infection through SAMHD1 inactivation. PMID: 26923586
39. These observations suggest that heterozygous cancer-associated SAMHD1 mutations increase mutation rates in cancer cells. PMID: 27071091
40. The SAMHD1 restricts HIV-1 infection in non-cycling cells by limiting the pool of deoxyribonucleoside triphosphates, thereby interfering with HIV-1 reverse transcription. PMID: 26733158
41. Studied whether one or more SAMHD1 gene mutations are associated with cerebrovascular disease in the general population using a Chinese stroke cohort. PMID: 26504826
42. SAMHD1 may facilitate some aspects of THP-1 cell differentiation. PMID: 26606981
43. Therefore, our findings revealed that factors in addition to Vpx-SAMHD1 binding influence the efficiency of Vpx-mediated SAMHD1 degradation. PMID: 26779819
44. These results argue against a requirement for additional myeloid-specific host factors for SAMHD1 function but further support the notion that SAMHD1 possesses an additional dNTP-independent function contributing to lentiviral restriction. PMID: 26655245
45. This review summarizes the latest advances in understanding the importance of dNTP metabolism in cancer development and the novel function of SAMHD1 in regulating this process. PMID: 26416562
46. SAMHD1 phosphorylation also ablates restriction and tetramer formation but without affecting triphosphohydrolase steady-state kinetics PMID: 26431200
47. Data suggest that critical role of vpx (Simian immunodeficiency virus vpx protein) in vivo/in vitro is to promote degradation of SAMHD1 in memory CD4+ T-lymphocytes, thereby generating high levels of plasma viremia and induction of immunodeficiency. PMID: 25996507
48. increased SAMHD1 in human astrocytes is in part responsible for the HIV restriction, silencing of which relieves this restriction PMID: 25890101
49. The results presented herein suggest that the RNase activity of SAMHD1 is sufficient to control the replication of retroviruses, but not that of non-retro RNA viruses. PMID: 26032178
50. results prove the importance of SAMHD1 in the regulation of all dNTP pools and suggest that dGK inside mitochondria has the function of recycling the deoxyguanosine derived from endogenous dGTP degraded by SAMHD1 in the nucleus PMID: 26342080

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HGNC: 15925

OMIM: 606754

KEGG: hsa:25939

STRING: 9606.ENSP00000262878

UniGene: Hs.580681