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Sirtuin 7

SIRT7, Sirtuin 7
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 IV of the sirtuin family. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Sir2, Histone, SIRT6, SIRT3, AGE
Papers on SIRT7
Weight loss is associated with increased NAD(+)/SIRT1 expression but reduced PARP activity in white adipose tissue.
Pietiläinen et al., Helsinki, Finland. In J Clin Endocrinol Metab, Feb 2016
RESULTS: SIRT1, SIRT3, SIRT7 and NAMPT expressions were significantly lower, whereas total PARP activity was increased in obese compared with lean subjects.
Dicer interacts with SIRT7 and regulates H3K18 deacetylation in response to DNA damaging agents.
Tang et al., Wenzhou, China. In Nucleic Acids Res, Jan 2016
Here we showed that the human Dicer protein interacts with SIRT7, an NAD(+)-dependent H3K18Ac (acetylated lysine 18 of histone H3) deacetylase, and holds a proportion of SIRT7 in the cytoplasm.
Protective effects of sirtuins in cardiovascular diseases: from bench to bedside.
Matter et al., Zürich, Switzerland. In Eur Heart J, Jan 2016
Sirtuins (Sirt1-Sirt7) comprise a family of nicotinamide adenine dinucleotide (NAD(+))-dependent enzymes.
Assessing sirtuin expression in endometrial carcinoma and non-neoplastic endometrium.
Jerónimo et al., Porto, Portugal. In Oncotarget, Jan 2016
SIRT1 and SIRT7 protein expression was evaluated by immunohistochemistry using Allred score.
C/EBPα negatively regulates SIRT7 expression via recruiting HDAC3 to the upstream-promoter of hepatocellular carcinoma cells.
Zhang et al., Beijing, China. In Biochim Biophys Acta, Jan 2016
Unlike their lower counterparts that are directly involved in the extending of lifespan, mammalian SIRTs mainly function in metabolism and cellular homeostasis, among them, SIRT7 is the least understood.
The role of sirtuins in cardiac disease.
Sadoshima et al., Newark, United States. In Am J Physiol Heart Circ Physiol, Nov 2015
Sirt6 has also recently been demonstrated to attenuate cardiac hypertrophy, and Sirt7 is known to regulate apoptosis and stress responses in the heart.
Sirtuin regulation in aging and injury.
Raju et al., Augusta, United States. In Biochim Biophys Acta, Nov 2015
Humans encode seven sirtuin isoforms SIRT1-SIRT7 with varying intracellular distribution.
Emerging role of silent information regulator 1 (SIRT1) in hepatocellular carcinoma: a potential therapeutic target.
Li et al., Hefei, China. In Tumour Biol, Jun 2015
SIRT1 (silent information regulator 1), a member of mammalian sirtuin family protein (SIRT1-SIRT7), functions as a conserved nicotinamide adenine dinucleotide (NAD)+-dependent deacetylase to implicate in the modulation of transcriptional silencing and cell survival.
Stem cell aging. A mitochondrial UPR-mediated metabolic checkpoint regulates hematopoietic stem cell aging.
Chen et al., Berkeley, United States. In Science, Apr 2015
Here, we identified a regulatory branch of the mitochondrial unfolded protein response (UPR(mt)), which is mediated by the interplay of SIRT7 and NRF1 and is coupled to cellular energy metabolism and proliferation.
Sirtuin 7 in cell proliferation, stress and disease: Rise of the Seventh Sirtuin!
Ramakrishna et al., Hyderābād, India. In Cell Signal, Mar 2015
Sirtuin 7 is a member of the sirtuin family of proteins.
miR-125b suppresses the proliferation of hepatocellular carcinoma cells by targeting Sirtuin7.
Wang et al., Wuhan, China. In Int J Clin Exp Med, 2014
Furthermore, TargetScan was conducted to predict the target gene of miR-125b and Sirtuin7 (SIRT7) was chosen to a potential target gene.
A SIRT7-dependent acetylation switch of GABPβ1 controls mitochondrial function.
Auwerx et al., Lausanne, Switzerland. In Cell Metab, 2014
Here, we identify Sirt7 as a crucial regulator of mitochondrial homeostasis.
SIRT7 controls hepatic lipid metabolism by regulating the ubiquitin-proteasome pathway.
Yamagata et al., Kumamoto, Japan. In Cell Metab, 2014
However, the physiological functions and molecular mechanisms of SIRT7 are poorly understood.
SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation.
Chua et al., Stanford, United States. In Nature, 2012
work establishes SIRT7 as a highly selective H3K18Ac deacetylase and demonstrates a pivotal role for SIRT7 in chromatin regulation, cellular transformation programs and tumour formation in vivo.
A big step for SIRT7, one giant leap for Sirtuins… in cancer.
Vaquero et al., Barcelona, Spain. In Cancer Cell, 2012
demonstrated that SIRT7 maintains critical features that define cancer cells by removing the acetylation mark on lysine 18 of histone H3.
Functional proteomics establishes the interaction of SIRT7 with chromatin remodeling complexes and expands its role in regulation of RNA polymerase I transcription.
Cristea et al., Princeton, United States. In Mol Cell Proteomics, 2012
SIRT7 plays a crucial role in connecting the function of chromatin remodeling complexes to RNA Pol I machinery during transcription
[Inhibitory role of SirT7 in the growth of P19 cell line].
Shen et al., Beijing, China. In Zhongguo Yi Xue Ke Xue Yuan Xue Bao, 2009
SirT7 plays a dominant role in the growth inhibition of the P19 cells.
Involvement of SIRT7 in resumption of rDNA transcription at the exit from mitosis.
Sirri et al., Paris, France. In J Cell Sci, 2009
associated with NORs during mitosis,interacts with the rDNA transcription factor UBF,phosphorylated via the CDK1-cyclin B pathway during mitosis and dephosphorylated by a phosphatase sensitive to okadaic acid at exit from mitosis
Sirt7-dependent inhibition of cell growth and proliferation might be instrumental to mediate tissue integrity during aging.
Bober et al., Bad Nauheim, Germany. In J Physiol Pharmacol, 2008
Using Sirt7 knockout and overexpressing cells we demonstrate an anti-proliferative role of Sirt7. We also show that Sirt7 expression inversely correlates with the tumorigenic potential of several murine cell lines
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