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SAMHD1 may play a role in regulation of the innate immune response. Additionally we are shipping SAMHD1 Antibodies (141) and SAMHD1 Proteins (4) and many more products for this protein.
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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.
stereoselective 2' substitutions that reveal nucleotide substrate specificity for SAMHD1, and a novel inhibitory mechanism for the dNTPase activity of SAMHD1, are reported.
Allosteric regulation of SAMHD1 has been uncovered through molecular dynamics simulations.
Cell cycle-associated changes of proteins are induced by activation of the Raf (show RAF1 ELISA Kits)/MEK (show MAP2K1 ELISA Kits)/ERK (show EPHB2 ELISA Kits) kinase cascade, culminating in upregulation of CDK1 (show CDK1 ELISA Kits) with subsequent SAMHD1 T592 phosphorylation and deactivation of its antiviral activity.
SAMHD1 acts as an inhibitor in cutaneous T-cell lymphoma cell growth.
miR (show MLXIP ELISA Kits)-181 is an important regulator of SAMHD1 protein expression in neoplastic CD4 (show CD4 ELISA Kits)+ T-cells, likely through a mechanism of translational inhibition
the mechanisms by which SAMHD1 is phosphorylated and suggest the contribution of cyclin (show PCNA ELISA Kits) binding to SAMHD1 expression and stability in dividing cells.
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.
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.
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
Data suggest that zebrafish may represent a system for studying the relationship between type I interferon (show IFNA ELISA Kits) (IFN) signaling and a loss of deoxynucleoside triphosphate triphosphohydrolase SAMHD1 activity.
These data support a model in which SAMHD1 catalytic activity is regulated through tetramer stabilization by the carboxyl-terminal tail, phosphorylation destabilizing the complexes and inactivating the enzyme. ISF2 may serve to reduce the dNTP pool to very low levels as a means of restricting virus replication.
These observations suggest that heterozygous cancer-associated SAMHD1 mutations increase mutation rates in cancer cells.
SAMHD1 in the mouse blocks retroviral infection at the level of reverse transcription and is regulated through cell cycle-dependent phosphorylation.
phosphorylation of mSAMHD1 at T634 by CDK1 (show CDK1 ELISA Kits)/2 negatively regulates its HIV-1 restriction in differentiated cells, but does not affect its murine leukemia virus restriction in dividing cells.
SAMHD1 restricts HIV-1 replication and regulates interferon (show IFNA ELISA Kits) production in mouse myeloid cells.
Allosteric regulation by dATP and dTTP works similarly in human and mouse SAMHD1.
SAMHD1 decreases dNTP pool in murine cells, restricts retroviral replication and regulates type I IFN production.
SAMHD1 can restrict lentiviruses in vivo and that nucleotide starvation is an evolutionarily conserved antiviral mechanism.
there are several Vpx residues required for SAMHD1 degradation
Vpx targets SAMHD1 for degradation in a viral strategy to control cellular deoxynucleotide levels for efficient replication
This gene may play a role in regulation of the innate immune response. The encoded protein is upregulated in response to viral infection and may be involved in mediation of tumor necrosis factor-alpha proinflammatory responses. Mutations in this gene have been associated with Aicardi-Goutieres syndrome.
SAM domain and HD domain-containing protein 1
, dendritic cell-derived IFNG-induced protein
, deoxynucleoside triphosphate triphosphohydrolase SAMHD1
, monocyte protein 5
, SAM domain- and HD domain-containing protein 1
, IFN-gamma induced
, interferon-gamma-inducible protein Mg11