Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
SIRT5 encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Zusätzlich bieten wir Ihnen Sirtuin 5 Antikörper (180) und Sirtuin 5 Kits (17) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 18 products:
This study showed that SIRT5 supports the anaplerotic entry of glutamine (zeige GFPT1 Proteine) into the TCA cycle in malignant phenotypes of CRC (zeige CALR Proteine) via activating GLUD1 (zeige GLUD1 Proteine).
Results show that SIRT5 binds to, desuccinylates and inhibits PKM2 activity. Increased levels of reactive oxygen species (ROS) decreases succinylation and activity of PKM2 by increasing its binding to SIRT5. Moreover, inhibition of SIRT5 suppresses tumor cell proliferation through desuccinylation of PKM2 K498.
The function of the three mitochondrial sirtuins (SIRT3 (zeige SIRT3 Proteine), SIRT4 (zeige SIRT4 Proteine), SIRT5) and their role in disease are reviewed.
Our study uncovers a SIRT5-dependent mechanism that regulates cellular NADPH (zeige NQO1 Proteine) homeostasis and redox potential by promoting IDH2 (zeige IDH2 Proteine) desuccinylation and G6PD (zeige G6PD Proteine) deglutarylation.
Results demonstrated presence of endogenous SIRT5 in mitochondria of cultured SH-EP cells, identified down-regulation of cellular oxidative stress by SIRT5 as one of the possible mechanisms mediating the anti-apoptotic effect of SIRT5 in SH-EP cells.
Data (including data from studies using knockout mice) suggest that SIRT5 is targeted to protein complexes on the inner mitochondrial membrane via affinity for cardiolipin to promote respiratory chain function, particularly Complex I and Complex II; SIRT5 expression is observed in inner mitochondrial membrane of periportal hepatocytes.
a side chain-to-side chain cyclic pentapeptide harboring a central N(epsilon)-carboxyethyl-thiocarbamoyl-lysine residue behaved as a strong and selective (versus human SIRT1 (zeige SIRT1 Proteine)/2/3/6) inhibitor against human SIRT5-catalyzed deacylation reaction.
Data indicate that compared to non-neoplastic endometria (NNE), endometrial cancer (EC) showed SIRT7 (zeige SIRT7 Proteine) mRNA overexpression, whereas SIRT1 (zeige SIRT1 Proteine), SIRT2 (zeige SIRT2 Proteine), SIRT4 (zeige SIRT4 Proteine) and SIRT5 were underexpressed, and no significant differences were observed for SIRT3 (zeige SIRT3 Proteine) and SIRT6 (zeige SIRT6 Proteine).
Use of a pan-sirtuin (zeige SIRT1 Proteine) inhibitor and shRNA-mediated protein knockdown led us to uncover a role for the NAD(+)-dependent family of sirtuins, and in particular for SIRT2 (zeige SIRT2 Proteine) and SIRT5, in the regulation of the necroptotic cell death program
mutual cooperation between Y102 and R105 residues in promoting the desuccinylation versus deacetylation reaction in SIRT5.
findings reveal a key role for SIRT5 in maintaining cardiac oxidative metabolism under pressure overload to ensure survival
Deletion of Sirt5 in starved mouse embryonic fibroblasts increased levels of mitochondrial dynamics leading to mitochondrial accumulation of the pro-fission Drp1 and to mitochondrial fragmentation.
Our study uncovers a SIRT5-dependent mechanism that regulates cellular NADPH (zeige FDXR Proteine) homeostasis and redox potential by promoting IDH2 (zeige IDH2 Proteine) desuccinylation and G6PD (zeige G6PD Proteine) deglutarylation.
Data show that peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1alpha) overexpression significantly increased the expression of sirtuin 3 (SIRT3 (zeige SIRT3 Proteine)) and sirtuin 5 (SIRT5).
In the cochlea, the expression of SIRT1 (zeige SIRT1 Proteine), 3, and 5 (both mRNA and protein) was decreased in the old mice
These findings establish that regulating heart metabolism and function is a major physiological function of lysine succinylation and SIRT5.
Myocardial ischemic reperfusion injury in Sirt5-/- heart is restored to wild-type levels by pretreatment with dimethyl malonate, a competitive inhibitor of succinate dehydrogenase (SDH (zeige SDHA Proteine)), implicating alteration in SDH (zeige SDS Proteine) activity as causative of the injury.
SIRT5 has a role in cellular metabolism with a multiple enzymatic activities
SIRT3 (zeige SIRT3 Proteine) and SIRT5 regulate the enzyme activity and cardiolipin binding of very long-chain acyl-CoA dehydrogenase (zeige ACADVL Proteine)
Association analysis of individual SIRT5 SNPs and haplotype combinations reveal that the 4 loci are significantly associated with some body measurement and ultrasound traits in Qinchuan cattle.
This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined\; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class III of the sirtuin family. Alternative splicing of this gene results in multiple transcript variants.
NAD-dependent deacetylase sirtuin-5
, NAD-dependent lysine demalonylase and desuccinylase sirtuin-5, mitochondrial
, NAD-dependent protein deacylase sirtuin-5, mitochondrial
, SIR2-like protein 5
, regulatory protein SIR2 homolog 5
, silent mating type information regulation 2, S.cerevisiae, homolog 5
, sir2-like 5
, sirtuin type 5
, Regulatory protein SIR2 homolog 5
, NAD-dependent lysine demalonylase and desuccinylase sirtuin-5A, mitochondrial
, NAD-dependent protein deacylase sirtuin-5A, mitochondrial
, regulatory protein SIR2 homolog 5-a
, sirtuin (silent mating type information regulation 2 homolog) 5
, sirtuin (silent mating type information regulation 2 homolog) 5 (S. cerevisiae)
, sirtuin 5
, nad-dependent deacetylase sirtuin-5