Robert B. Best
Molecular Biology · 2005–2021
A researcher in the Science corpus: 9 papers; trusts 1 researcher and is trusted by 9 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 121 citations into it; #4,347 of 17,773 by trust here, #3,737 by citations
Whom Robert B. Best trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
Who trusts Robert B. Best overall
- Paul Robustelli
- Stefano Piana
- Justin A. Lemkul
- K. Lindorff‐Larsen
- Zhuoran Qiao
- David E. Shaw
- John D. Chodera
- Lim Heo
- Tatu Pantsar
- Michael Feig
Papers from Robert B. Best's perspective
Ordered by how strongly the researchers Robert B. Best 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)
- 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 Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles (Molecules and Cells)
- Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization (Cell)
- Comparison of simple potential functions for simulating liquid water
- Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies. (Cell)
- A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation. (Cell)
- The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics (Proceedings of the National Academy of Sciences of the United States of America)
- Sequence Determinants of Intracellular Phase Separation by Complex Coacervation of a Disordered Protein (Molecules and Cells)
- Polymer physics of intracellular phase transitions (Nature Physics)
Their papers
- Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone φ, ψ and side-chain χ1 and χ2 dihedral angles (2012) — 4,191 citations
- Optimized molecular dynamics force fields applied to the helix-coil transition of polypeptides. (2009) — 811 citations
- Simultaneous determination of protein structure and dynamics (2005) — 683 citations
- Extreme disorder in an ultra-high-affinity protein complex (2018) — 588 citations
- Phosphorylation of the FUS low‐complexity domain disrupts phase separation, aggregation, and toxicity (2017) — 611 citations
- Sequence determinants of protein phase behavior from a coarse-grained model (2017) — 573 citations
- Native contacts determine protein folding mechanisms in atomistic simulations (2013) — 628 citations
- Martini 3: A General Purpose Force Field for Coarse-Grained Molecular Dynamics (2021) — 1,229 citations
- The Polarizable Atomic Multipole-based AMOEBA Force Field for Proteins. (2013) — 619 citations