Quantitative proteome‐based systematic identification of SIRT7 substrates

No abstract is available for this paper.

• Publication year

  2017

• Venue

  Proteomics

• Publication date

  2017-07-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1002/pmic.201600395PMID 28556401
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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  2014influential reference
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  2012influential reference
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  2012influential reference
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• Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription.

  2006cited by this paper
• Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins.

  2005cited by this paper
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  2004cited by this paper
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  2001cited by this paper
• Functional significance of histone deacetylase diversity.

  2001cited by this paper
• The human histone deacetylase family.

  2001cited by this paper
• Histone acetylation and transcriptional regulatory mechanisms.

  1998cited by this paper
• Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro.

  1996cited by this paper
• Studies of the DNA binding properties of histone H4 amino terminus. Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 "tail" to DNA.

  1993cited by this paper
• A positive role for histone acetylation in transcription factor access to nucleosomal DNA.

  1993cited by this paper
• Histone acetylation reduces nucleosome core particle linking number change.

  1989cited by this paper
• ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS.

  1964cited by this paper

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• SIRT7: a sentinel of genome stability

  2021cites this paper
• Sirtuins, melatonin, and the relevance of circadian oscillators

  2021cites this paper
• Epigenetics in NAFLD/NASH: Targets and Therapy.

  2021cites this paper
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  2020cites this paper
• Papel pleiotrópico y homeostático de las Sirtuinas en la función biológica humana.

  2020cites this paper
• Chapter 8: Sirtuins in avian biology

  2020cites this paper
• The yin and yang faces of the mitochondrial deacetylase sirtuin 3 in age-related disorders.

  2019cites this paper
• Current trends in protein acetylation analysis

  2019influential citation
• Quantitative Proteomics for Analyses of Multiple Samples in Parallel with Chemical Perturbation

  2019cites this paper
• Deep learning based prediction of reversible HAT/HDAC-specific lysine acetylation

  2019cites this paper
• Mammalian Sirtuins SIRT4 and SIRT7.

  2018cites this paper
• Chemical Probes in Sirtuin Research.

  2018cites this paper
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  2018cites this paper
• Advances in Cellular Characterization of the Sirtuin Isoform, SIRT7

  2018cites this paper
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  2018cites this paper
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