The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Reversible peptide folding in solution by molecular dynamics simulation 1 1Edited by R. Huber
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Citations
Cites
Dominant forces in protein folding
Dill, K. A. (1990) · Biochemistry · doi:10.1021/bi00483a001 · Cited by 3,800
From Levinthal to pathways to funnels
Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293
Creighton, T. E. (1992) · Cited by 1,583
Seebach, D., Overhand, M., Kühnle, F. N. M., Martinoni, B., Oberer, L., Hommel, U., & Widmer, H. (1996) · Helvetica Chimica Acta · doi:10.1002/hlca.19960790402 · Cited by 734
Self-citationβ-Peptide Foldamers: Robust Helix Formation in a New Family of β-Amino Acid Oligomers
Appella, D. H., Christianson, L. A., Karle, I. L., Powell, D. R., & Gellman, S. H. (1996) · Journal of the American Chemical Society · doi:10.1021/ja963290l · Cited by 705
Residue-based control of helix shape in β-peptide oligomers
Appella, D. H., Christianson, L. A., Klein, D. A., Powell, D. R., Huang, X., Barchi, J. J., & Gellman, S. H. (1997) · Nature · doi:10.1038/387381a0 · Cited by 626
Fast Events in Protein Folding: Helix Melting and Formation in a Small Peptide
Williams, S., Causgrove, T. P., Gilmanshin, R., Fang, K. S., Callender, R. H., Woodruff, W. H., & Dyer, R. B. (1996) · Biochemistry · doi:10.1021/bi952217p · Cited by 555
NMR Determination of Residual Structure in a Urea-Denatured Protein, the 434-Repressor
Neri, D., Billeter, M., Wider, G., & Wüthrich, K. (1992) · Science · doi:10.1126/science.1523410 · Cited by 448
Statistical Potentials Extracted From Protein Structures: How Accurate Are They?
Thomas, P. D., & Dill, K. A. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0175 · Cited by 422
The concept of a random coil: Residual structure in peptides and denatured proteins
Smith, L. J., Fiebig, K. M., Schwalbe, H., & Dobson, C. M. (1996) · Folding and Design · doi:10.1016/s1359-0278(96)00046-6 · Cited by 350
Cited by
Biomolecular Modeling: Goals, Problems, Perspectives
van Gunsteren, W. F., Bakowies, D., Baron, R., Chandrasekhar, I., Christen, M., Daura, X., Gee, P., Geerke, D. P., Glättli, A., Hünenberger, P. H., et al. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200502655 · Cited by 561
Self-citationShea, J.-E., & Brooks III, C. L. (2001) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.52.1.499 · Cited by 481
Understanding folding and design: Replica-exchange simulations of ``Trp-cage'' miniproteins
Pitera, J. W., & Swope, W. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1330954100 · Cited by 344
Vasudev, P. G., Chatterjee, S., Shamala, N., & Balaram, P. (2011) · Chemical Reviews · doi:10.1021/cr100100x · Cited by 329
Basic conformers in ?-peptides
(1999) · doi:10.1002/(sici)1097-0282(199908)50:2<167::aid-bip6>3.0.co;2-m
Metadata
- Authors
- Daura, X., Jaun, B., Seebach, D., van Gunsteren, W. F., & Mark, A. E.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1998-07
- Volume
- 280
- Issue
- 5
- Pages
- 925-932
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2113301225
- Cited by
- 373
- References
- 32
- Type
- book review
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Reversible peptide folding in solution by molecular dynamics simulation 1 1Edited by R. Huber. https://app.cochat.ai/papers/10.1006/jmbi.1998.1885
- The paper
- Daura, X., Jaun, B., Seebach, D., van Gunsteren, W. F., & Mark, A. E. (1998). Reversible peptide folding in solution by molecular dynamics simulation 1 1Edited by R. Huber. Journal of Molecular Biology. https://doi.org/10.1006/jmbi.1998.1885
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.
