The DOI matches its Crossref record; 15 of the 16 references it cites were found in a registry or an index.
The protein trinity—linking function and disorder
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In the citing paper
“Many IDPs/IDRs are capable of at least partial ordering upon interaction with specific partners [7–18].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [8]
Citations
Cites
Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196
Lethality and centrality in protein networks
Jeong, H., Mason, S., Barabási, A., & Oltvai, Z. (2001) · Nature · doi:10.1038/35075138 · Cited by 5,327
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
Wright, P. E., & Dyson, H. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3110 · Cited by 2,968
Intrinsically disordered protein
Dunker, A. K., Lawson, J. D., Brown, C. J., Williams, R. M., Romero, P., Oh, J. S., Oldfield, C. J., Campen, A. M., Ratliff, C. M., Hipps, K. W., et al. (2001) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(00)00138-8 · Cited by 2,272
Self-citationEinfluss der Configuration auf die Wirkung der Enzyme
Fischer, E. (1894) · Berichte der deutschen chemischen Gesellschaft · doi:10.1002/cber.18940270364 · Cited by 1,841
Target Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide Complex
Meador, W. E., Means, A. R., & Quiocho, F. A. (1992) · Science · doi:10.1126/science.1519061 · Cited by 1,032
Crystal structures of human calcineurin and the human FKBP12–FK506–calcineurin complex
Kissinger, C. R., Parge, H. E., Knighton, D. R., Lewis, C. T., Pelletier, L. A., Tempczyk, A., Kalish, V. J., Tucker, K. D., Showalter, R. E., Moomaw, E. W., et al. (1995) · Nature · doi:10.1038/378641a0 · Cited by 768
Kriwacki, R. W., Hengst, L., Tennant, L. L., Reed, S. I., & Wright, P. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11504 · Cited by 576
IEEE International Conference on Neural Networks
(1993) · doi:10.1109/icnn.1993 · Cited by 550
On the Structure of Native, Denatured, and Coagulated Proteins
Mirsky, A. E., & Pauling, L. C. (1936) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.22.7.439 · Cited by 523
Research works printed but not linked: 4
- Wu, H. Chinese J. Physiol. 1, 219–234 (1931).
- Dunker, A.K., Obradovic, Z., Romero, P., Garner, E.C. & Brown, C.J. Genome Informat. 11, 161–171 (2000).
- Schulz, G.E. In Molecular mechanism of biological recognition. (ed. Balaban, M.) 79–94 (Elsevier/North-Holland Biomedical Press, New York, NY; 1979).
- Reeves, R. Genes, in press (2001).
Cited by
Sorted by citations
The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
Arnold, K., Bordoli, L., Kopp, J., & Schwede, T. F. (2005) · Bioinformatics · doi:10.1093/bioinformatics/bti770 · Cited by 7,031
Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life
Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F., & Jones, D. T. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.002 · Cited by 2,010
Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 Concept
Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125924 · Cited by 1,447
Self-citationCoupling of folding and binding for unstructured proteins
Dyson, H. J., & Wright, P. E. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00289-0 · Cited by 1,327
PONDR-FIT: A meta-predictor of intrinsically disordered amino acids
Xue, B., Dunbrack, R. L., Williams, R. W., Dunker, A. K., & Uversky, V. N. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.01.011 · Cited by 1,239
Self-citation
Metadata
- Authors
- Dunker, A. K., & Obradovic, Z.
- Affiliations
- Washington State University (US)
- ORCID
- Dunker, A. Keith
- Venue
- Nature Biotechnology
- Published
- 2001-09
- Volume
- 19
- Issue
- 9
- Pages
- 805-806
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- OpenAlex
- W121768123
- Cited by
- 581
- References
- 16
- Citations by year
- 2026: 7 · 2025: 11 · 2024: 16 · 2023: 16 · 2022: 18 · 2021: 18 · 2020: 25 · 2019: 22 · 2018: 17 · 2017: 17 · 2016: 23 · 2015: 26 · 2014: 27 · 2013: 33 · 2012: 37
- FWCI
- 6.59
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Biotechnology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Keywords
- intrinsically disordered proteins, protein function, protein disorder, signal transduction, taurine, casein, protein conformation, structure-function relationship, enzyme binding
- MeSH terms
- Algorithms, Biotechnology, Models, Biological, Protein Conformation, Proteins, Structure-Activity Relationship, Transcription Factors
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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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