期刊文献+

SIRT1抑制剂的研究进展

下载PDF
导出
摘要 组蛋白去乙酰化是一种重要的组蛋白共价修饰方式,在基因表达中起着非常重要的调控作用。组蛋白去乙酰化主要由组蛋白去乙酰化酶催化完成,现已发现的组蛋白去乙酰化酶除了经典的锌离子依赖的组蛋白去乙酰化酶外,
出处 《中南药学》 CAS 2012年第8期617-622,共6页 Central South Pharmacy
  • 相关文献

参考文献43

  • 1Imai SI, Guarente L. Ten years of NAD-dependen* SIR2 family deacetylase: implications {or metabolic diseases [J] .Cell, 2010, 31 (5): 212 220.
  • 2Michan S, Sinclair D. Sirtuins in mammals: insights into their biological function [J] Biochem J, 2007, 1 (404): 1-13.
  • 3Finmn MS, Donigian JR, Pavietin NP. Structure of the histone deacetylase SIRT2 [J]. Nature Structural Biology, 2001, 8 (7) : 621-625.
  • 4Landry J, Sutton A, Tafrov ST, et al. The silencing protein SIR2 and its homologs are NAI>dependent protein deacetylases [J]. Proc Natl Acad Sci USA, 2000, 97 (11) 5807-5811.
  • 5Landry J, Slama JT, Sternglanz R. Role of NAD (_a) in the deacetylase activity of the SIR2 like proteins[J]. Biochem Bio- phys Res Commun, 2000, 278 (3): 685 690.
  • 6Tanner KG, Landry J, Stemglanz R, et al. Silent information regulator 2 family of NAIdependent histone/protein deacetylas es generates a unique product, 1 acetyl-ADP ribose [J]. Proc Natl Acad Sei USA, 2000, 97 (26): 14178-14182.
  • 7Gillum MP, Erion DM, Shulman GI. Sirtuin-1 regulation of mammalian metabolism [J]. Trends in Pharmcological Sciences, 2011, 17 (1) 8-13.
  • 8Knight JRP, Milner J. SIRT1, metabolism and cancer [J]. Current Opinion, 2012, 24 (1) : 68 75.
  • 9Fatkins DG, Monnot AD, Zheng W. Nepsilonthioacetyl-ly- sine.- A multi facet functional probe for enzymatic protein lysine Nq0-deacetylation [J]. Bioorg Med Chem Lett, 2006, 16 (14) : 3651-3656.
  • 10Hirsch BM, Gallo CA, Du Z, et al. Discovery of potent, pro teolytically stable, and cell permeable human sirtuin peptido- mimetic inhibitors containing N-thioacetyl lysine [J]. Med ChemComm, 2010, 1 (3).- 233 238.

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部