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SLBP encodes a protein that binds to the stem-loop structure in replication-dependent histone mRNAs. Additionally we are shipping SLBP Antibodies (19) and SLBP Proteins (5) and many more products for this protein.
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Although the C-terminal tail of dSLBP does not contact the RNA, phosphorylation of the tail promotes SLBP conformations competent for RNA binding and thereby appears to reduce the entropic penalty for the association.
nuclear retention involves Chk2-mediated inactivation of the Drosophila stem loop binding protein (SLBP), the levels of which are specifically depleted in damaged nuclei following Chk2 phosphorylation, an event that contributes to nuclear fallout.
The nuclear magnetic resonance and kinetic studies presented here provide a framework for understanding how SLBP recognizes histone mRNA and highlight possible structural roles of phosphorylation and proline isomerization in RNA binding proteins
Slbp mutants display genomic instability, including loss of heterozygosity (LOH), increased presence of chromosome breaks, tetraploidy, and changes in position effect variegation (PEV).
Developmental control of histone mRNA and dSLBP synthesis during Drosophila embryogenesis and the role of dSLBP in histone mRNA 3' end processing in vivo.
Phosphorylation of T120 and T230 site of Stem-loop binding protein (SLBP) differentially affects the ability of the protein to restore viability and histone mRNA processing.
characterize the structural and dynamic features of the N-terminal domain of SLBP from Drosophila
electrostatic effect of protein phosphorylation can be partially mimicked by a mutant form of SLBP wherein four C-terminal serines are replaced with glutamic acids
Removal of the phosphoryl group from T230 by either dephosphorylation or mutation results in a 7-fold reduction in the affinity of SLBP for the stem-loop RNA
SLBP is a potentially important cellular regulator of HIV-1, thereby establishing a link between histone metabolism, inflammation, and HIV-1 infection
showed that inhibiting the SLBP mRNA and protein levels were rescued by epigenetic modifiers suggesting that nickel's effects on SLBP may be mediated via epigenetic mechanisms
Cyclin F (show CCNF ELISA Kits)-mediated degradation of SLBP limits H2A.X (show H2AFX ELISA Kits) accumulation and apoptosis upon genotoxic stress in G2 cell cycle checkpoint.
CRL4(WDR23 (show DCAF11 ELISA Kits)) is required for efficient histone mRNA 3' end processing to produce mature histone mRNAs for translation. CRL4(WDR23 (show DCAF11 ELISA Kits)) binds and ubiquitylates SLBP in vitro and in vivo, and this modification activates SLBP function in histone mRNA 3' end processing without affecting its protein levels.
FEM1 proteins are ancient regulators of Stem-Loop Binding Protein.
CRL4-DCAF11 (show DCAF11 ELISA Kits) mediates the degradation of SLBP at the end of S phase and this degradation is essential for the viability of cells.
arsenic, a carcinogenic metal, decreases cellular levels of SLBP by inducing its proteasomal degradation and inhibiting SLBP transcription via epigenetic mechanisms
the S/G2 (show STRN3 ELISA Kits) stable mutant form of SLBP is degraded by proteasome in G1, indicating that indicating that the SLBP degradation in G1 is independent of the previously identified SLBP degradation at S/G2 (show STRN3 ELISA Kits)
C-terminal extension of Lsm4 (show LSM4 ELISA Kits) interacts directly with the histone mRNP, contacting both SLBP and 3'hExo (show ERI1 ELISA Kits).
During maturation, Slbp mRNA becomes polyadenylated and translationally activated. Proteasomal activity is required both to initiate and to sustain translational activation.
SLBP expression and activity differ in mouse oocytes and early embryos compared with somatic cells.
Inhibition of NF kappa B (show NFKB1 ELISA Kits) in TNF alpha (show TNF ELISA Kits)-treated primary mouse hepatocytes is associated with increased S-phase cell cycle retention and decreased stem loop binding protein.
histone synthesis in immature and maturing oocytes is governed by a translational control mechanism that is directly regulated by changes in the amount of SLBP
SLBP is an essential component of the mechanism by which growing oocytes of the mouse accumulate the histones that support early embryonic development.
Maternally encoded Slbp is degraded in 2-cell mouse embryos by the co-ordinated activity of two separately regulated pathways.
SLBP is required for retinal stem cell maintenance. SLBP and Notch (show NOTCH1 ELISA Kits) signaling are required for retinal progenitor cell proliferation and subsequent neurogenesis.
SLBP stimulates histone translation at an early step in the intiaition pathway.
This gene encodes a protein that binds to the stem-loop structure in replication-dependent histone mRNAs. Histone mRNAs do not contain introns or polyadenylation signals, and are processed by endonucleolytic cleavage. The stem-loop structure is essential for efficient processing but this structure also controls the transport, translation and stability of histone mRNAs. Expression of the protein is regulated during the cell cycle, increasing more than 10-fold during the latter part of G1.
histone RNA hairpin-binding protein
, stem loop binding protein
, RNA processing protein
, histone stem-loop binding protein
, stem-loop (histone) binding protein
, RNA binding protein
, histone stem loop binding protein
, hairpin binding protein, histone
, histone binding protein
, histone stem-loop-binding protein
, histone stem-loop-binding protein 1