Nicolas L. Fawzi
Molecular Biology · 2015–2018
A researcher in the Science corpus: 4 papers; trusts 6 researchers and is trusted by 1 researcher here, as inferred from the citation graph.
Subfields
- Molecular Biology — 93 citations into it; #16,721 of 17,773 by trust here, #6,685 by citations
- Materials Chemistry — 5 citations into it
- Spectroscopy — 5 citations into it
Whom Nicolas L. Fawzi trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
Who trusts Nicolas L. Fawzi overall
Papers from Nicolas L. Fawzi's perspective
Ordered by how strongly the researchers Nicolas L. Fawzi trusts endorse each paper. Same corpus, a different order for every researcher.
- Germline P Granules Are Liquid Droplets That Localize by Controlled Dissolution/Condensation (Science)
- Cell-Free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers Within Hydrogels (Cell)
- Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies. (Cell)
- Phase Transitions in the Assembly of Multi-Valent Signaling Proteins (Nature)
- 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)
- Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization (Cell)
- Stress granule assembly is mediated by prion-like aggregation of TIA-1. (Molecular Biology of the Cell)
- Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles (Molecules and Cells)
- Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis (Science)
- A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation. (Cell)
Their papers
- Residue-by-residue view of in vitro FUS granules that bind the C-terminal domain of RNA polymerase II (2015) — 814 citations
- Phosphorylation of the FUS low‐complexity domain disrupts phase separation, aggregation, and toxicity (2017) — 611 citations
- ALS mutations disrupt phase separation mediated by -helical structure in the TDP-43 low complexity C-terminal domain (2016) — 751 citations
- Protein Phase Separation: A New Phase in Cell Biology (2018) — 1,723 citations