Thomas Ried
Geriatrics and Gerontology · 2004–2008
A researcher in the Science corpus: 3 papers; trusts 1 researcher and is trusted by 0 researchers here, as inferred from the citation graph.
Subfields
- Geriatrics and Gerontology — 13 citations into it
Whom Thomas Ried trusts
Their strongest outbound trust, strongest first, inferred from their citations.
- L. Guarente (in Geriatrics and Gerontology)
Papers from Thomas Ried's perspective
Ordered by how strongly the researchers Thomas Ried trusts endorse each paper. Same corpus, a different order for every researcher.
- The language of covalent histone modifications (Nature)
- Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins (Nature)
- Translating the Histone Code (Science)
- Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain (Nature)
- Genomic instability and aging-like phenotype in the absence of mammalian SIRT6. (Cell)
- Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses. (Cell)
- The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. (Proceedings of the National Academy of Sciences of the United States of America)
- Sir2 links chromatin silencing, metabolism, and aging. (Genes & Development)
- Mammalian sirtuins--emerging roles in physiology, aging, and calorie restriction. (Genes & Development)
- SET Domain-containing Protein, G9a, Is a Novel Lysine-preferring Mammalian Histone Methyltransferase with Hyperactivity and Specific Selectivity to Lysines 9 and 27 of Histone H3* (Journal of Biological Chemistry)
Their papers
- From silencing to gene expression: real-time analysis in single cells. (2004) — 756 citations
- SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin (2008) — 1,102 citations
- Impaired DNA damage response, genome instability, and tumorigenesis in SIRT1 mutant mice (2008) — 804 citations