The DOI matches its Crossref record; 96 of the 96 references it cites were found in a registry or an index.
Energetics of Protein Folding
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Citations
Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
The interpretation of protein structures: Estimation of static accessibility
Lee, B., & Richards, F. M. (1971) · Journal of Molecular Biology · doi:10.1016/0022-2836(71)90324-x · Cited by 5,850
Nicholls, A., Sharp, K. A., & Honig, B. (1991) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,240
Some Factors in the Interpretation of Protein Denaturation
Kauzmann, W. (1959) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60608-7 · Cited by 4,870
Dominant forces in protein folding
Dill, K. A. (1990) · Biochemistry · doi:10.1021/bi00483a001 · Cited by 3,800
Interfaces and the driving force of hydrophobic assembly
Chandler, D. (2005) · Nature · doi:10.1038/nature04162 · Cited by 3,591
AREAS, VOLUMES, PACKING, AND PROTEIN STRUCTURE
Richards, F. M. (1977) · Annual Review of Biophysics and Bioengineering · doi:10.1146/annurev.bb.06.060177.001055 · Cited by 2,661
Structure of the cross-β spine of amyloid-like fibrils
Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. Ø., Riekel, C., Grothe, R., & Eisenberg, D. (2005) · Nature · doi:10.1038/nature03680 · Cited by 2,202
Stability of Proteins Small Globular Proteins
Privalov, P. L. (1979) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60460-x · Cited by 2,159
Accurate Calculation of Hydration Free Energies Using Macroscopic Solvent Models
Sitkoff, D., Sharp, K. A., & Honig, B. (1994) · The Journal of Physical Chemistry · doi:10.1021/j100058a043 · Cited by 2,131
Cited by
Macromolecular Modeling with Rosetta
Das, R., & Baker, D. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.062906.171838 · Cited by 989
Ab Initio Folding of Proteins with All-Atom Discrete Molecular Dynamics
Ding, F., Tsao, D., Nie, H., & Dokholyan, N. V. (2008) · Structure · doi:10.1016/j.str.2008.03.013 · Cited by 326
The Hydrophobic Temperature Dependence of Amino Acids Directly Calculated from Protein Structures
van Dijk, E., Hoogeveen, A., & Abeln, S. (2015) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1004277 · Cited by 162
“It is thought that this hydrophobic force gives the single largest contribution to the stability of most protein folds [1].”
BackgroundFrancis, B. R. (2013) · Journal of Molecular Evolution · doi:10.1007/s00239-013-9567-y · Cited by 34
Metadata
- Authors
- Baldwin, R. L.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2007-08
- Volume
- 371
- Issue
- 2
- Pages
- 283-301
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2156408001
- Cited by
- 305
- References
- 96
- FWCI
- 8.62
- 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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- The paper
- Baldwin, R. L. (2007). Energetics of Protein Folding. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2007.05.078
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.