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SAMHD1 may play a role in regulation of the innate immune response. Additionally we are shipping SAMHD1 Antibodies (142) and SAMHD1 Kits (5) and many more products for this protein.
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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 (show TP53BP1 Proteins) loss and SAMHD1 overexpression as the primary mechanisms responsible for their resistance to PARPi and Ara (show FOXC1 Proteins)-C, respectively.
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.
The activation of interferon (show IFNA Proteins)-induced genes is controlled by the JAK (show JAK3 Proteins)-STAT (show STAT1 Proteins) system; therefore, JAK (show JAK3 Proteins) inhibitors were successfully used in several cases to treat type 1 interferonopathies. Experience with this treatment modality is continuously growing.
our work genetically separated the ability of SAMHD1 to negatively regulate the type I IFN response from its ability to restrict HIV-1.
MiR (show MLXIP Proteins)-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 (show IFNA Proteins).
SAMHD1 is active in HIV-1 permissive cells, does not modify susceptibility to HIV-1 infection but strongly affects sensitivity to nucleoside inhibitors.
expression of p21 (show CDKN1A Proteins) potentially can contribute to inhibition of HIV-1 replication in monocyte-derived dendritic cells through multiple mechanisms. p21 (show CDKN1A Proteins) decreased size of the intracellular dNTP pool; p21 (show CDKN1A Proteins) prevented SAMHD1 phosphorylation and promoted SAMHD1 dNTPase-independent antiviral activity
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.
Data suggest that zebrafish may represent a system for studying the relationship between type I interferon (show IFNA Proteins) (IFN) signaling and a loss of deoxynucleoside triphosphate triphosphohydrolase SAMHD1 activity.
provide genetic evidence that cell-autonomous control of lentivirus infection in myeloid cells by SAMHD1 limits virus-induced production of interferons and the induction of co-stimulatory markers
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 Proteins)/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 Proteins) 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
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