The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Conformation of the Backbone in Unfolded Proteins
Abstract
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“The polyproline II and extended β-basins of the Ramachandran plot are distinguished almost entirely by their φ backbone dihedral angles, with ranges of −75 ± 15° and −120 ± 30°, respectively (26, 27).”
From Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain (2008) · cites this paper as [27]
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Citations
Cites
Intrinsic Disorder in Cell-signaling and Cancer-associated Proteins
Iakoucheva, L. M., Brown, C. J., Lawson, J. D., Obradović, Z., & Dunker, A. K. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00969-5 · Cited by 1,214
Research works printed but not linked: 1
- 10.1021/cr040433a · DOI · Paper page
Cited by
Newberry, R. W., & Raines, R. T. (2017) · Accounts of Chemical Research · doi:10.1021/acs.accounts.7b00121 · Cited by 494
Are Current Molecular Dynamics Force Fields too Helical?
Best, R. B., Buchete, N.-V., & Hummer, G. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.132696 · Cited by 454
Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain
Wells, M., Tidow, H., Rutherford, T. J., Markwick, P., Jensen, M. R., Mylonas, E., Svergun, D. I., Blackledge, M., & Fersht, A. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801353105 · Cited by 434
Small-Angle X-Ray Scattering from RNA, Proteins, and Protein Complexes
Lipfert, J., & Doniach, S. (2007) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.36.040306.132655 · Cited by 300
Metadata
- Authors
- Shi, Z., Chen, K., Liu, Z., & Kallenbach, N. R.
- Venue
- ChemInform
- Publisher
- Wiley
- Published
- 2006-07-11
- Volume
- 37
- Issue
- 31
- ISSN
- 0931-7597
- 1522-2667
- Cited by
- 0
- References
- 1
- Language
- en
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- Shi, Z., Chen, K., Liu, Z., & Kallenbach, N. R. (2006). Conformation of the Backbone in Unfolded Proteins. ChemInform. https://doi.org/10.1002/chin.200631296
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.