A. Greenleaf
Molecular Biology · with Phatnani · 2006
A researcher in the Science corpus: 1 paper; trusts 1 researcher and is trusted by 1 researcher here, as inferred from the citation graph.
Subfields
- Molecular Biology — 10 citations into it
Whom A. Greenleaf trusts
Their strongest outbound trust, strongest first, inferred from their citations.
- Patrick Cramer (in Molecular Biology)
Who trusts A. Greenleaf
- J. Manley (in Archeology)
Papers from A. Greenleaf's perspective
Ordered by how strongly the researchers A. Greenleaf trusts endorse each paper. Same corpus, a different order for every researcher.
- Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription. (Genes & Development)
- Methylation of Histone H3 by Set2 in Saccharomyces cerevisiae Is Linked to Transcriptional Elongation by RNA Polymerase II (Molecular and Cellular Biology)
- An extensive network of coupling among gene expression machines (Nature)
- Recognition of RNA polymerase II carboxy-terminal domain by 3′-RNA-processing factors
- Elongation by RNA polymerase II: the short and long of it. (Genes & Development)
- Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex. (Cell)
- Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription. (Cell)
- Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution (Science)
- The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. (Molecules and Cells)
- Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity. (Molecules and Cells)
Their papers
- Phosphorylation and functions of the RNA polymerase II CTD. (2006) — 811 citations