Xiang-Jiao Yang

Molecular Biology · 2006–2008

A researcher in the Science corpus: 6 papers; trusts 17 researchers and is trusted by 3 researchers here, as inferred from the citation graph.

Subfields

Whom Xiang-Jiao Yang trusts overall

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

  1. G. Blander
  2. C. D. Allis
  3. L. Guarente
  4. E. Seto
  5. S. Berger
  6. Kenneth K. Lee
  7. M. Haigis
  8. W. Hallows
  9. R. Goodman
  10. Yi Tang

Who trusts Xiang-Jiao Yang overall

  1. Zhibin Wang
  2. Bor Luen Tang
  3. E. Seto
  4. Shahin Ramazi
  5. Chongzhi Zang
  6. Andrew J. Bannister
  7. John C. Newman
  8. M. Haberland

Papers from Xiang-Jiao Yang's perspective

Ordered by how strongly the researchers Xiang-Jiao Yang trusts endorse each paper. Same corpus, a different order for every researcher.

  1. Translating the Histone Code (Science)
  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. Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases (Proceedings of the National Academy of Sciences of the United States of America)
  6. The Sir2 family of protein deacetylases. (Annual Review of Biochemistry)
  7. Surfing the p53 network (Nature)
  8. Acetylation: a regulatory modification to rival phosphorylation? (EMBO Journal)
  9. HDAC6 is a microtubule-associated deacetylase (Nature)
  10. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. (Molecules and Cells)

Their papers