The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Residue – Residue Potentials with a Favorable Contact Pair Term and an Unfavorable High Packing Density Term, for Simulation and Threading
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Citations
Cites
Needleman, S. B., & Wunsch, C. D. (1970) · Journal of Molecular Biology · doi:10.1016/0022-2836(70)90057-4 · Cited by 11,288
Funnels, pathways, and the energy landscape of protein folding: A synthesis
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648 · cited 7×
“assumption is also equivalent to the assumption that the distribution of the numbers of contacts in protein structures is a ‘‘self-averaging property’’ in the terms of Bryngelson et al. (1995), which means it is, in the present case, the property of heteropolymers rather than of the detailed amino acid order of protei…”
BackgroundInfluentialA new approach to protein fold recognition
Jones, D. T., Taylort, W. R., & Thornton, J. M. (1992) · Nature · doi:10.1038/358086a0 · Cited by 1,221
Cited by
THEORY OF PROTEIN FOLDING: The Energy Landscape Perspective
Onuchic, J. N., Luthey-Schulten, Z., & Wolynes, P. G. (1997) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.48.1.545 · Cited by 2,210
The Rosetta All-Atom Energy Function for Macromolecular Modeling and Design
Alford, R. F., Leaver-Fay, A., Jeliazkov, J. R., O’Meara, M. J., DiMaio, F. P., Park, H., Shapovalov, M. V., Renfrew, P. D., Mulligan, V. K., Kappel, K., et al. (2017) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.7b00125 · Cited by 1,532
PIPER: An FFT‐based protein docking program with pairwise potentials
Kozakov, D., Brenke, R., Comeau, S. R., & Vajda, S. (2006) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.21117 · Cited by 865
Keskin, O., Ma, B., & Nussinov, R. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.077 · Cited by 519
Finding low-energy conformations of lattice protein models by quantum annealing
Perdomo-Ortiz, A., Dickson, N., Drew-Brook, M., Rose, G., & Aspuru-Guzik, A. (2012) · Scientific Reports · doi:10.1038/srep00571 · Cited by 366
Metadata
- Authors
- Miyazawa, S., & Jernigan, R. L.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1996-03
- Volume
- 256
- Issue
- 3
- Pages
- 623-644
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2171546617
- Cited by
- 1,230
- References
- 3
- FWCI
- 12.74
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
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- CoChat. (2026). Citation check: Residue – Residue Potentials with a Favorable Contact Pair Term and an Unfavorable High Packing Density Term, for Simulation and Threading. https://app.cochat.ai/papers/10.1006/jmbi.1996.0114
- The paper
- Miyazawa, S., & Jernigan, R. L. (1996). Residue – Residue Potentials with a Favorable Contact Pair Term and an Unfavorable High Packing Density Term, for Simulation and Threading. Journal of Molecular Biology. https://doi.org/10.1006/jmbi.1996.0114
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.
