Sayda M. Elbashir

Molecular Biology · 2001–2020

A researcher in the Science corpus: 7 papers; trusts 2 researchers and is trusted by 29 researchers here, as inferred from the citation graph.

Subfields

Whom Sayda M. Elbashir trusts overall

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

  1. Phillip A. Sharp
  2. Thomas Tuschl
  3. Olivier Voinnet
  4. Scott M. Hammond
  5. Phillip D. Zamore

Who trusts Sayda M. Elbashir overall

  1. Weimin He
  2. Phillip A. Sharp
  3. Thomas Tuschl
  4. David P. Bartel
  5. Phillip D. Zamore
  6. Yoontae Lee
  7. J. Harborth
  8. Yukihide Tomari
  9. Christian B. Matranga
  10. T. Rana

Papers from Sayda M. Elbashir's perspective

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

  1. Transcriptional silencing and promoter methylation triggered by double‐stranded RNA (EMBO Journal)
  2. An RNA-dependent RNA polymerase gene in Arabidopsis is required for posttranscriptional gene silencing mediated by a transgene but not by a virus. (Cell)
  3. Specific interference with gene function by double-stranded RNA in early mouse development (Nature Cell Biology)
  4. Use of double-stranded RNA interference in Drosophila cell lines to dissect signal transduction pathways. (Proceedings of the National Academy of Sciences of the United States of America)
  5. Erratum: EGO-1 is related to RNA-directed RNA polymerase and functions in germ-line development and RNA interference in C. elegans (Current Biology (2000) 10 (169-178))
  6. Expression profiling reveals off-target gene regulation by RNAi
  7. A viral movement protein prevents spread of the gene silencing signal in Nicotiana benthamiana. (Cell)
  8. Cleavage of Scarecrow-like mRNA Targets Directed by a Class of Arabidopsis miRNA (Science)
  9. Cell division: Mitotic kinases as regulators of cell division and its checkpoints (Nature reviews. Molecular cell biology)
  10. Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins. (Annual Review of Biochemistry)

Their papers