The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Thermodynamic β -sheet propensities measured using a zinc-finger host peptide
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Citations
Cites
Garnier, J., Osguthorpe, D. J., & Robson, B. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90297-8 · Cited by 4,523
Chou, P. Y., & Fasman, G. D. (1974) · Biochemistry · doi:10.1021/bi00699a001 · Cited by 2,172
Zinc Finger-DNA Recognition: Crystal Structure of a Zif268-DNA Complex at 2.1 Å
Pavletich, N. P., & Pabo, C. O. (1991) · Science · doi:10.1126/science.2028256 · Cited by 2,061
A Thermodynamic Scale for the Helix-Forming Tendencies of the Commonly Occurring Amino Acids
O'Neil, K. T., & DeGrado, W. F. (1990) · Science · doi:10.1126/science.2237415 · Cited by 1,188
Prediction of Protein Structure and the Principles of Protein Conformation
(1989) · Springer eBooks · doi:10.1007/978-1-4613-1571-1 · Cited by 816
Conformational preferences of amino acids in globular proteins
Levitt, M. (1978) · Biochemistry · doi:10.1021/bi00613a026 · Cited by 653
β-Sheet topology and the relatedness of proteins
Richardson, J. S. (1977) · Nature · doi:10.1038/268495a0 · Cited by 552
Side Chain Contributions to the Stability of Alpha-Helical Structure in Peptides
Lyu, P. C., Liff, M. I., Marky, L. A., & Kallenbach, N. R. (1990) · Science · doi:10.1126/science.2237416 · Cited by 463
Relative helix-forming tendencies of nonpolar amino acids
Padmanabhan, S., Marqusee, S., Ridgeway, T., Laue, T. M., & Baldwin, R. L. (1990) · Nature · doi:10.1038/344268a0 · Cited by 462
McGregor, M. J., Islam, S. A., & Sternberg, M. J. E. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90314-7 · Cited by 420
Cited by
Collagen Structure and Stability
Shoulders, M. D., & Raines, R. T. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.032207.120833 · Cited by 3,923
Measurement of the β-sheet-forming propensities of amino acids
Minor, D. L., & Kim, P. S. (1994) · Nature · doi:10.1038/367660a0 · Cited by 593
De Novo Design and Structural Characterization of Proteins and Metalloproteins
DeGrado, W. F., Summa, C. M., Pavone, V., Nastri, F., & Lombardi, A. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.779 · Cited by 572
Probability‐based protein secondary structure identification using combined NMR chemical‐shift data
Wang, Y., & Jardetzky, O. (2002) · Protein Science · doi:10.1110/ps.3180102 · Cited by 445
A Thermodynamic Scale for the .beta.-Sheet Forming Tendencies of the Amino Acids
Smith, C. K., Withka, J. M., & Regan, L. (1994) · Biochemistry · doi:10.1021/bi00184a020 · Cited by 395
Metadata
- Authors
- Kim, C. A., & Berg, J. M.
- Venue
- Nature
- Published
- 1993-03
- Volume
- 362
- Issue
- 6417
- Pages
- 267-270
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1991653374
- Cited by
- 347
- References
- 17
- FWCI
- 6.37
- 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: Thermodynamic β -sheet propensities measured using a zinc-finger host peptide. https://app.cochat.ai/papers/10.1038/362267a0
- The paper
- Kim, C. A., & Berg, J. M. (1993). Thermodynamic β -sheet propensities measured using a zinc-finger host peptide. Nature. https://doi.org/10.1038/362267a0
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.
