A toolkit and benchmark study for FRET-restrained high-precision structural modeling
By S. Kalinin, Thomas O. Peulen, S. Sindbert, P. Rothwell, S. Berger, T. Restle, R. Goody, Holger Gohlke, C. Seidel. Nature Methods, 2012
437 citations recorded by the source corpus.
Subfields: Materials Chemistry, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/17d1dd7138bb923aed129d55ff83012835969347
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Materials Chemistry
- Torsten Schwede
- Andriy Kryshtafovych
- Yang Zhang
- Lorenza Bordoli
- Andrej Sali
- Ben M. Webb
- Krzysztof Fidelis
- John Moult
In Molecular Biology
- Torsten Schwede
- Andriy Kryshtafovych
- Yang Zhang
- Lorenza Bordoli
- Andrej Sali
- Ben M. Webb
- Björn Wallner
- Liam J. McGuffin
Citations in the corpus
- Protein Modelling: What Happened to the “Protein Structure Gap”? (2013, positive): “Recent advances in the measurement and interpretation of single molecule Forster fluorescence resonance energy transfer (FRET) experiments allow the generation of highly accurate distance constraints as input for restrained modeling of biomolecules and complexes (Kalinin et al., 2012).”
- Outcome of the First wwPDB Hybrid/Integrative Methods Task Force Workshop (2015, neutral): “Claus Seidel outlined state-of-the-art single-molecule and ensemble Förster resonance energy transfer (FRET) spectroscopy (Kalinin et al., 2012) and live cell imaging, as well as related label-based spectroscopic methods for measuring select interatomic distances in macromolecular systems.”