Holger Gohlke
Molecular Biology · 2000–2012
A researcher in the Science corpus: 10 papers; trusts 12 researchers and is trusted by 43 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 62 citations into it; #936 of 17,773 by trust here, #1,334 by citations
- Materials Chemistry — 25 citations into it; #940 of 11,513 by trust here, #3,270 by citations
- Computational Chemistry & Drug Discovery — 24 citations into it; #139 of 425 by trust here, #148 by citations
- Computational Biology & Bioinformatics — 11 citations into it
- Evaluation & Benchmarks — 8 citations into it
- Organic Chemistry — 8 citations into it
Whom Holger Gohlke trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
- Hans-Joachim Böhm
- Matthias Rarey
- Peter A. Kollman
- S. W. Lockless
- Christopher W. Murray
- Bernd Kramer
- Eugene I. Shakhnovich
- Michael Levitt
- Thomas Lengauer
- Sarah A. Teichmann
Who trusts Holger Gohlke overall
- Samuel Genheden
- Zhong-Ru Xie
- Ulf Ryde
- Sérgio Filipe Sousa
- Marcel L. Verdonk
- Wijnand T. M. Mooij
- Gerhard Klebe
- Pedro J. Ballester
- Tatu Pantsar
- Jinn-Moon Yang
Papers from Holger Gohlke's perspective
Ordered by how strongly the researchers Holger Gohlke trusts endorse each paper. Same corpus, a different order for every researcher.
- A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic Molecules J. Am. Chem. Soc. 1995, 117, 5179−5197
- A general and fast scoring function for protein-ligand interactions: a simplified potential approach.
- \the Protein Data Bank: a Computer-based Archival Le for Macromolecular Structures,"
- A new approach to protein fold recognition
- A method to identify protein sequences that fold into a known three-dimensional structure.
- Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading.
- Evolutionarily conserved pathways of energetic connectivity in protein families.
- Energy functions that discriminate X-ray and near native folds from well-constructed decoys.
- Comparison of simple potential functions for simulating liquid water
- SMoG: de Novo Design Method Based on Simple, Fast, and Accurate Free Energy Estimates. 1. Methodology and Supporting Evidence
Their papers
- The Amber biomolecular simulation programs (2005) — 8,841 citations
- Knowledge-based scoring function to predict protein-ligand interactions. (2000) — 1,037 citations
- A toolkit and benchmark study for FRET-restrained high-precision structural modeling (2012) — 437 citations
- Assessing scoring functions for protein-ligand interactions. (2004) — 440 citations
- Approaches to the description and prediction of the binding affinity of small-molecule ligands to macromolecular receptors. (2002) — 687 citations
- DrugScore(CSD)-knowledge-based scoring function derived from small molecule crystal data with superior recognition rate of near-native ligand poses and better affinity prediction. (2005) — 333 citations
- Converging free energy estimates: MM‐PB(GB)SA studies on the protein–protein complex Ras–Raf (2004) — 828 citations
- Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes. (2003) — 1,073 citations
- MMPBSA.py: An Efficient Program for End-State Free Energy Calculations. (2012) — 4,086 citations
- Free Energy Calculations by the Molecular Mechanics Poisson−Boltzmann Surface Area Method (2012) — 1,060 citations