David S. W. Protter

Molecular Biology · 2015–2017

A researcher in the Science corpus: 3 papers; trusts 11 researchers and is trusted by 8 researchers here, as inferred from the citation graph.

Subfields

Whom David S. W. Protter trusts overall

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

  1. C. Brangwynne
  2. N. Kedersha
  3. Yuan Lin
  4. A. Molliex
  5. Shana Elbaum-Garfinkle
  6. S. Jonas
  7. R. Parker
  8. Paul Anderson
  9. J. Buchan
  10. Oliver D. King

Who trusts David S. W. Protter overall

  1. A. Khong
  2. David W. Sanders
  3. Yongdae Shin
  4. T. Matheny
  5. Joshua R. Wheeler
  6. Saumya Jain
  7. N. Kedersha
  8. C. Brangwynne
  9. R. Parker
  10. Jeong-Mo Choi

Papers from David S. W. Protter's perspective

Ordered by how strongly the researchers David S. W. Protter trusts endorse each paper. Same corpus, a different order for every researcher.

  1. Germline P Granules Are Liquid Droplets That Localize by Controlled Dissolution/Condensation (Science)
  2. Cell-Free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers Within Hydrogels (Cell)
  3. Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies. (Cell)
  4. Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles (Molecules and Cells)
  5. Stress granule assembly is mediated by prion-like aggregation of TIA-1. (Molecular Biology of the Cell)
  6. Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization (Cell)
  7. Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes (Proceedings of the National Academy of Sciences of the United States of America)
  8. A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation. (Cell)
  9. Eukaryotic stress granules: the ins and outs of translation. (Molecules and Cells)
  10. Stress granules and processing bodies are dynamically linked sites of mRNP remodeling (Journal of Cell Biology)

Their papers