Stefano Piana

Molecular Biology · 2010–2018

A researcher in the Science corpus: 8 papers; trusts 10 researchers and is trusted by 18 researchers here, as inferred from the citation graph.

Subfields

• Molecular Biology — 51 citations into it; #2,054 of 17,773 by trust here, #1,914 by citations
• Materials Chemistry — 45 citations into it; #1,180 of 11,513 by trust here, #2,107 by citations
• Atomic and Molecular Physics, and Optics — 10 citations into it

Whom Stefano Piana trusts overall

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

1. K. Lindorff‐Larsen
2. Robert B. Best
3. Alexander D. MacKerell
4. W. L. Jorgensen
5. David E. Shaw
6. Gerhard Hummer
7. John L. Klepeis
8. Ron O. Dror
9. Binchen Mao
10. K. Bowers

Who trusts Stefano Piana overall

1. Paul Robustelli
2. David E. Shaw
3. David W. Borhani
4. K. Lindorff‐Larsen
5. Maher M. Kassem
6. Michael Feig
7. Ron O. Dror
8. Siva Dasetty
9. Robin Pearce
10. Scott A. Hollingsworth

Papers from Stefano Piana's perspective

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

1. Comparison of simple potential functions for simulating liquid water
2. A point‐charge force field for molecular mechanics simulations of proteins based on condensed‐phase quantum mechanical calculations (Journal of Computational Chemistry)
3. Simultaneous determination of protein structure and dynamics (Nature)
4. GPU-Accelerated Molecular Modeling Coming Of Age (Journal of Molecular Graphics and Modelling)
5. Markov models of molecular kinetics: generation and validation.
6. Long-timescale molecular dynamics simulations of protein structure and function. (Current Opinion in Structural Biology)
7. All-atom empirical potential for molecular modeling and dynamics studies of proteins.
8. Water dispersion interactions strongly influence simulated structural properties of disordered protein states. (Journal of Physical Chemistry B)
9. CHARMM36m: An Improved Force Field for Folded and Intrinsically Disordered Proteins
10. Protein NMR Structures Refined with Rosetta Have Higher Accuracy Relative to Corresponding X-ray Crystal Structures

Their papers

• How Fast-Folding Proteins Fold (2011) — 1,934 citations
• Supporting Online Material Materials and Methods Figs. S1 to S10 Table S1 References Movies S1 to S3 Atomic-level Characterization of the Structural Dynamics of Proteins — 1,242 citations
• Improved side-chain torsion potentials for the Amber ff99SB protein force field (2010) — 5,790 citations
• Developing a molecular dynamics force field for both folded and disordered protein states (2018) — 920 citations
• Systematic Validation of Protein Force Fields against Experimental Data (2012) — 659 citations
• Assessing the accuracy of physical models used in protein-folding simulations: quantitative evidence from long molecular dynamics simulations. (2014) — 449 citations
• How robust are protein folding simulations with respect to force field parameterization? (2011) — 809 citations
• Water dispersion interactions strongly influence simulated structural properties of disordered protein states. (2015) — 773 citations