The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
A toolkit and benchmark study for FRET-restrained high-precision structural modeling
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Principles of Fluorescence Spectroscopy
Lakowicz, J. R. (1999) · Springer eBooks · doi:10.1007/978-1-4757-3061-6 · Cited by 26,947
Principles of Fluorescence Spectroscopy
(2006) · Springer eBooks · doi:10.1007/978-0-387-46312-4 · Cited by 19,339
The Amber biomolecular simulation programs
Case, D. A., Cheatham, T. E., Darden, T., Gohlke, H., Luo, R., Merz, K. M., Onufriev, A., Simmerling, C., Wang, B., & Woods, R. J. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20290 · Cited by 9,535
Self-citationConstant pressure molecular dynamics algorithms
Martyna, G. J., Tobias, D. J., & Klein, M. L. (1994) · The Journal of Chemical Physics · doi:10.1063/1.467468 · Cited by 5,804
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
Brünger, A. T. (1992) · Nature · doi:10.1038/355472a0 · Cited by 3,873
Dynamic personalities of proteins
Henzler-Wildman, K., & Kern, D. (2007) · Nature · doi:10.1038/nature06522 · Cited by 2,545
Fluorescence Energy Transfer as a Spectroscopic Ruler
Stryer, L. (1978) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.47.070178.004131 · Cited by 2,406
Huang, H., Chopra, R., Verdine, G. L., & Harrison, S. C. (1998) · Science · doi:10.1126/science.282.5394.1669 · Cited by 1,420
Ha, T., Enderle, T., Ogletree, D. F., Chemla, D. S., Selvin, P. R., & Weiss, S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.13.6264 · Cited by 1,242
Protein Dynamism and Evolvability
Tokuriki, N., & Tawfik, D. S. (2009) · Science · doi:10.1126/science.1169375 · Cited by 940
Dale, R. E., Eisinger, J., & Blumberg, W. E. (1979) · Biophysical Journal · doi:10.1016/s0006-3495(79)85243-1 · Cited by 755
Resonance Energy Transfer: Theory and Data
van der Meer, B. W., Coker, E. G., & Chen, S.-Y. S. (1994) · Cited by 679
The RosettaDock server for local protein-protein docking
Lyskov, S., & Gray, J. J. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn216 · Cited by 592
Merchant, K. A., Best, R. B., Louis, J. M., Gopich, I. V., & Eaton, W. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607097104 · Cited by 350
Shot-Noise Limited Single-Molecule FRET Histograms: Comparison between Theory and Experiments
Nir, E., Michalet, X., Hamadani, K. M., Laurence, T. A., Neuhauser, D., Kovchegov, Y., & Weiss, S. (2006) · The Journal of Physical Chemistry B · doi:10.1021/jp063483n · Cited by 314
Mekler, V., Kortkhonjia, E., Mukhopadhyay, J., Knight, J., Revyakin, A., Kapanidis, A. N., Niu, W., Ebright, Y. W., Levy, R., & Ebright, R. H. (2002) · Cell · doi:10.1016/s0092-8674(02)00667-0 · Cited by 302
Margittai, M., Widengren, J., Schweinberger, E., Schröder, G. F., Felekyan, S., Haustein, E., König, M., Fasshauer, D., Grubmüller, H., Jahn, R., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2331232100 · Cited by 290
Self-citationAccurate Single-Molecule FRET Studies Using Multiparameter Fluorescence Detection
Sisamakis, E., Valeri, A., Kalinin, S., Rothwell, P. J., & Seidel, C. A. M. (2010) · Methods in Enzymology · doi:10.1016/s0076-6879(10)75018-7 · Cited by 268
Self-citationSindbert, S., Kalinin, S., Nguyen, H., Kienzler, A., Clima, L., Bannwarth, W., Appel, B., Müller, S., & Seidel, C. A. M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja105725e · Cited by 268
Self-citationEggeling, C., Berger, S., Brand, L., Fries, J. R., Schaffer, J., Volkmer, A., & Seidel, C. A. M. (2001) · Journal of Biotechnology · doi:10.1016/s0168-1656(00)00412-0 · Cited by 268
Self-citationRothwell, P. J., Berger, S., Kensch, O., Felekyan, S., Antonik, M., Wöhrl, B. M., Restle, T., Goody, R. S., & Seidel, C. A. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0434003100 · Cited by 225
Self-citationAntonik, M., Felekyan, S., Gaiduk, A., & Seidel, C. A. M. (2006) · The Journal of Physical Chemistry B · doi:10.1021/jp057257+ · Cited by 210
Self-citationEffect of flexibility and cis residues in single-molecule FRET studies of polyproline
Best, R. B., Merchant, K. A., Gopich, I. V., Schuler, B., Bax, A., & Eaton, W. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709567104 · Cited by 209
Single-molecule FRET measures bends and kinks in DNA
Woźniak, A. K., Schröder, G. F., Grubmüller, H., Seidel, C. A. M., & Oesterhelt, F. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800977105 · Cited by 199
Self-citationSingle-molecule FRET–derived model of the synaptotagmin 1–SNARE fusion complex
Choi, U. B., Strop, P., Vrljic, M., Chu, S., Brunger, A. T., & Weninger, K. R. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1763 · Cited by 197
A nano-positioning system for macromolecular structural analysis
Muschielok, A., Andrecka, J., Jawhari, A., Brückner, F., Cramer, P., & Michaelis, J. (2008) · Nature Methods · doi:10.1038/nmeth.1259 · Cited by 193
Detecting the conformation of individual proteins in live cells
Sakon, J. J., & Weninger, K. R. (2010) · Nature Methods · doi:10.1038/nmeth.1421 · Cited by 166
Patel, P. H., Jacobo-Molina, A., Ding, J., Tantillo, C., Clark, A. D., Raag, R., Nanni, R. G., Hughes, S. H., & Arnold, E. (1995) · Biochemistry · doi:10.1021/bi00016a006 · Cited by 164
Hoefling, M., Lima, N., Haenni, D., Seidel, C. A. M., Schuler, B., & Grubmüller, H. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019791 · Cited by 118
Self-citationBouřa, E., Różycki, B., Herrick, D. Z., Chung, H. S., Večeř, J., Eaton, W. A., Cafiso, D. S., Hummer, G., & Hurley, J. H. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1101763108 · Cited by 116
Fretting about FRET: Correlation between κ and R
VanBeek, D. B., Zwier, M. C., Shorb, J. M., & Krueger, B. P. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.092650 · Cited by 112
Single-molecule tracking of mRNA exiting from RNA polymerase II
Andrecka, J., Lewis, R., Brückner, F., Lehmann, E., Cramer, P., & Michaelis, J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703815105 · Cited by 108
Felekyan, S., Kalinin, S., Sanabria, H., Valeri, A., & Seidel, C. A. M. (2012) · ChemPhysChem · doi:10.1002/cphc.201100897 · Cited by 107
Self-citationThree-dimensional molecular modeling with single molecule FRET
Brünger, A. T., Strop, P., Vrljic, M., Chu, S., & Weninger, K. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.09.004 · Cited by 103
Single-Macromolecule Fluorescence Resonance Energy Transfer and Free-Energy Profiles
Gopich, I. V., & Szabó, A. (2003) · The Journal of Physical Chemistry B · doi:10.1021/jp027481o · Cited by 99
Characterizing Single‐Molecule FRET Dynamics with Probability Distribution Analysis
Santoso, Y., Torella, J. P., & Kapanidis, A. N. (2010) · ChemPhysChem · doi:10.1002/cphc.201000129 · Cited by 92
Kalinin, S., Felekyan, S., Valeri, A., & Seidel, C. A. M. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp711942q · Cited by 76
Self-citationPushing the limits of what is achievable in protein–DNA docking: benchmarking HADDOCK’s performance
van Dijk, M., & Bonvin, A. M. J. J. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq222 · Cited by 62
Muschielok, A., & Michaelis, J. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp2060377 · Cited by 53
Domain Orientation in the N-Terminal PDZ Tandem from PSD-95 Is Maintained in the Full-Length Protein
McCann, J. J., Zheng, L., Chiantia, S., & Bowen, M. E. (2011) · Structure · doi:10.1016/j.str.2011.02.017 · Cited by 43
Knight, J. L., Mekler, V. M., Mukhopadhyay, J., Ebright, R. H., & Levy, R. M. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.050187 · Cited by 42
Global Structure of Forked DNA in Solution Revealed by High-Resolution Single-Molecule FRET
Sabir, T., Schroeder, G. F., Toulmin, A., McGlynn, P., & Magennis, S. W. (2010) · Journal of the American Chemical Society · doi:10.1021/ja108626w · Cited by 38
Reverse transcriptase in motion: Conformational dynamics of enzyme–substrate interactions
Götte, M., Rausch, J. W., Marchand, B., Sarafianos, S. G., & Grice, S. F. J. L. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.07.020 · Cited by 38
Peletskaya, E. N., Kogon, A. A., Tuske, S. J., Arnold, E., & Hughes, S. H. (2004) · Journal of Virology · doi:10.1128/jvi.78.7.3387-3397.2004 · Cited by 37
Discussion: Jackknife, Bootstrap and Other Resampling Methods in Regression Analysis
Efron, B. (1986) · The Annals of Statistics · doi:10.1214/aos/1176350145 · Cited by 29
Balci, H., Arslan, S., Myong, S., Lohman, T. M., & Ha, T. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.07.010 · Cited by 14
Upadhyay, A. K., Talele, T. T., & Pandey, V. N. (2009) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-009-0316-x · Cited by 6
Cited by
Precision and accuracy of single-molecule FRET measurements—a multi-laboratory benchmark study
Hellenkamp, B., Schmid, S., Doroshenko, O., Opanasyuk, O., Kühnemuth, R., Rezaei Adariani, S., Ambrose, B., Aznauryan, M., Barth, A., Birkedal, V., et al. (2018) · Nature Methods · doi:10.1038/s41592-018-0085-0 · Cited by 519
Self-citationPrinciples for Integrative Structural Biology Studies
Rout, M. P., & Sali, A. (2019) · Cell · doi:10.1016/j.cell.2019.05.016 · Cited by 258
Multidomain structure and correlated dynamics determined by self-consistent FRET networks
Hellenkamp, B., Wortmann, P., Kandzia, F., Zacharias, M., & Hugel, T. (2017) · Nature Methods · doi:10.1038/nmeth.4081 · Cited by 137
Complex RNA Folding Kinetics Revealed by Single-Molecule FRET and Hidden Markov Models
Keller, B. G., Kobitski, A., Jäschke, A., Nienhaus, G. U., & Noé, F. (2014) · Journal of the American Chemical Society · doi:10.1021/ja4098719 · Cited by 84
Biased cytochrome P450-mediated metabolism via small-molecule ligands binding P450 oxidoreductase
Jensen, S. B., Thodberg, S., Parween, S., Moses, M. E., Hansen, C. C., Thomsen, J., Sletfjerding, M. B., Knudsen, C., Del Giudice, R., Lund, P. M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22562-w · Cited by 64
Metadata
- Authors
- Kalinin, S., Peulen, T., Sindbert, S., Rothwell, P. J., Berger, S., Restle, T., Goody, R. S., Gohlke, H., & Seidel, C. A. M.
- Venue
- Nature Methods
- Published
- 2012-11-11
- Volume
- 9
- Issue
- 12
- Pages
- 1218-1225
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- OpenAlex
- W1973699439
- Cited by
- 434
- References
- 47
- FWCI
- 8.02
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.