E. Seto

Molecular Biology · 2000–2016

A researcher in the Science corpus: 9 papers; trusts 27 researchers and is trusted by 10 researchers here, as inferred from the citation graph.

Subfields

Whom E. Seto trusts overall

Their strongest outbound trust, strongest first, inferred from their citations.

  1. S. Imai
  2. L. Guarente
  3. C. D. Allis
  4. Tony Kouzarides
  5. G. Blander
  6. Chunaram Choudhary
  7. Xiang-Jiao Yang
  8. Jessica E. Bolden
  9. Jianyuan Luo
  10. S. Berger

Who trusts E. Seto overall

  1. Xiang-Jiao Yang
  2. J. Audia
  3. Nikolaos G. Frangogiannis
  4. John C. Newman
  5. S. Baylin
  6. Zhibin Wang
  7. PA Marks

Papers from E. Seto's perspective

Ordered by how strongly the researchers E. Seto trusts endorse each paper. Same corpus, a different order for every researcher.

  1. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase (Nature)
  2. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. (Molecules and Cells)
  3. The language of covalent histone modifications (Nature)
  4. Mammalian sirtuins--emerging roles in physiology, aging, and calorie restriction. (Genes & Development)
  5. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. (Molecules and Cells)
  6. Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions (Science)
  7. Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. (Molecules and Cells)
  8. The Sir2 family of protein deacetylases. (Annual Review of Biochemistry)
  9. Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases (Proceedings of the National Academy of Sciences of the United States of America)
  10. The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. (Cell)

Their papers