Yongdae Shin

Molecular Biology · 2016–2018

A researcher in the Science corpus: 3 papers; trusts 13 researchers and is trusted by 2 researchers here, as inferred from the citation graph.

Subfields

Whom Yongdae Shin trusts overall

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

  1. C. Brangwynne
  2. Shana Elbaum-Garfinkle
  3. Peter Tompa
  4. A. Molliex
  5. Anthony A. Hyman
  6. T. Mitchison
  7. Saumya Jain
  8. Salman F. Banani
  9. Fabrizio Chiti
  10. Huaiying Zhang

Who trusts Yongdae Shin overall

  1. S. Alberti
  2. Daniel S. W. Lee
  3. David W. Sanders
  4. Jeong-Mo Choi
  5. C. Brangwynne
  6. Joshua A. Riback
  7. Alex S. Holehouse

Papers from Yongdae Shin's perspective

Ordered by how strongly the researchers Yongdae Shin 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. Phase Transitions in the Assembly of Multi-Valent Signaling Proteins (Nature)
  4. Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles (Molecules and Cells)
  5. 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)
  6. Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization (Cell)
  7. ATPase modulated stress granules contain a diverse proteome and substructure (Cell)
  8. Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies. (Cell)
  9. RNA controls PolyQ protein phase transitions (Molecules and Cells)
  10. A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation. (Cell)

Their papers