K. Lindorff‐Larsen

Molecular Biology · 2005–2021

A researcher in the Science corpus: 12 papers; trusts 9 researchers and is trusted by 16 researchers here, as inferred from the citation graph.

Subfields

• Molecular Biology — 114 citations into it; #2,243 of 17,773 by trust here, #1,491 by citations
• Materials Chemistry — 66 citations into it; #1,308 of 11,513 by trust here, #1,756 by citations
• Computational Biology & Bioinformatics — 37 citations into it

Whom K. Lindorff‐Larsen trusts overall

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

1. Stefano Piana
2. W. L. Jorgensen
3. Alexander D. MacKerell
4. Robert B. Best
5. Viktor Hornak
6. John E. Stone
7. David E. Shaw
8. Jeffry D. Madura
9. Gerhard Hummer
10. Michael Feig

Who trusts K. Lindorff‐Larsen overall

1. Paul Robustelli
2. Stefano Piana
3. David E. Shaw
4. David W. Borhani
5. Robin Pearce
6. Maher M. Kassem
7. Ron O. Dror
8. Michael Feig
9. Frank No'e
10. Douglas L. Theobald

Papers from K. Lindorff‐Larsen's perspective

Ordered by how strongly the researchers K. Lindorff‐Larsen 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. GPU-Accelerated Molecular Modeling Coming Of Age (Journal of Molecular Graphics and Modelling)
4. Simultaneous determination of protein structure and dynamics (Nature)
5. Markov models of molecular kinetics: generation and validation.
6. Comparative protein modelling by satisfaction of spatial restraints.
7. HHblits: lightning-fast iterative protein sequence searching by HMM-HMM alignment
8. Long-timescale molecular dynamics simulations of protein structure and function. (Current Opinion in Structural Biology)
9. Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations.
10. How Fast-Folding Proteins Fold (Science)

Their papers

• How Fast-Folding Proteins Fold (2011) — 1,934 citations
• Structure of a functional amyloid protein subunit computed using sequence variation. (2015) — 99 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
• Systematic Validation of Protein Force Fields against Experimental Data (2012) — 659 citations
• A structural biology community assessment of AlphaFold2 applications (2021) — 578 citations
• Simultaneous determination of protein structure and dynamics (2005) — 683 citations
• How robust are protein folding simulations with respect to force field parameterization? (2011) — 809 citations
• Long-timescale molecular dynamics simulations of protein structure and function. (2009) — 744 citations
• Promoting transparency and reproducibility in enhanced molecular simulations (2019) — 1,046 citations
• Structure of the Bacterial Cytoskeleton Protein Bactofilin by NMR Chemical Shifts and Sequence Variation. (2016) — 17 citations
• Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations. (2005) — 692 citations