Erik Lindahl
Molecular Biology · 2000–2020
A researcher in the Science corpus: 16 papers; trusts 37 researchers and is trusted by 22 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 109 citations into it; #4,518 of 17,773 by trust here, #1,070 by citations
- Materials Chemistry — 60 citations into it; #3,357 of 11,513 by trust here, #1,912 by citations
- Structural Biology — 46 citations into it; #134 of 224 by trust here, #90 by citations
- Surfaces, Coatings and Films — 31 citations into it
- Computational Biology & Bioinformatics — 28 citations into it
- Atomic and Molecular Physics, and Optics — 25 citations into it; #1,484 of 7,135 by trust here, #904 by citations
- Spectroscopy — 12 citations into it; #230 of 1,674 by trust here, #67 by citations
- Condensed Matter Physics — 9 citations into it
Whom Erik Lindahl trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
- Björn Wallner
- John Moult
- Arne Elofsson
- Sjors H. W. Scheres
- Andriy Kryshtafovych
- Krzysztof Fidelis
- David C. Jones
- Marc Delarue
- Ivet Bahar
- R. Lehoucq
Who trusts Erik Lindahl overall
- Bernard O. Offmann
- Eric J. Sorin
- C. Hetényi
- Riviera Maya
- Dariya S. Glazer
- Justin A. Lemkul
- Björn Wallner
- D. van der Spoel
- I. Tsimpanogiannis
- Greg L. Hura
Papers from Erik Lindahl's perspective
Ordered by how strongly the researchers Erik Lindahl trusts endorse each paper. Same corpus, a different order for every researcher.
- Processing and analysis of CASP3 protein structure predictions
- Can correct protein models be identified?
- Basic local alignment search tool.
- Errors in protein structures
- Gapped BLAST and PSI-BLAST: a new generation of protein database search programs.
- SCOP: a structural classification of proteins database for the investigation of sequences and structures.
- MODBASE: a database of annotated comparative protein structure models and associated resources
- Comparative protein modelling by satisfaction of spatial restraints.
- Protein secondary structure prediction based on position-specific scoring matrices.
- MaxSub: an automated measure for the assessment of protein structure prediction quality
Their papers
- Using multiple templates to improve quality of homology models in automated homology modeling (2008) — 159 citations
- GROMACS: Fast, flexible, and free (2005) — 17,374 citations
- GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation. (2008) — 15,253 citations
- GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers (2015) — 23,273 citations
- Prediction of membrane-protein topology from first principles (2008) — 318 citations
- Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2 (2016) — 972 citations
- Characterisation of molecular motions in cryo-EM single-particle data by multi-body refinement in RELION (2018) — 424 citations
- GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit (2013) — 7,077 citations
- Implementation of the CHARMM Force Field in GROMACS: Analysis of Protein Stability Effects from Correction Maps, Virtual Interaction Sites, and Water Models. (2010) — 1,166 citations
- NOMAD-Ref: visualization, deformation and refinement of macromolecular structures based on all-atom normal mode analysis (2006) — 319 citations
- Spatial and energetic-entropic decomposition of surface tension in lipid bilayers from molecular dynamics simulations (2000) — 227 citations
- New tools for automated high-resolution cryo-EM structure determination in RELION-3 (2018) — 4,245 citations
- Heterogeneous Parallelization and Acceleration of Molecular Dynamics Simulations in GROMACS (2020) — 790 citations
- Tackling Exascale Software Challenges in Molecular Dynamics Simulations with GROMACS (2015) — 921 citations
- Improved model quality assessment using ProQ2 (2012) — 193 citations
- GROMACS 3.0: a package for molecular simulation and trajectory analysis (2001) — 6,280 citations