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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Integrity signals
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Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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
Flagged first, then by citations
1 of the 16 references couldn’t be matched to a known paper.
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
Items 101–106 of 106
Cooperative Unfolding of Compact Conformations of the Intrinsically Disordered Protein Osteopontin
Kurzbach, D., Platzer, G., Schwarz, T. C., Henen, M. A., Konrat, R., & Hinderberger, D. (2013) · Biochemistry · doi:10.1021/bi400502c · Cited by 105
Fonin, A. V., Darling, A. L., Kuznetsova, I. M., Turoverov, K. K., & Uversky, V. N. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03276-1 · Cited by 91
AlphaFold and the amyloid landscape
Pinheiro, F., Santos, J., & Ventura, S. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167059 · Cited by 88
Sequence-to-conformation relationships of disordered regions tethered to folded domains of proteins
Mittal, A., Holehouse, A. S., Cohan, M. C., & Pappu, R. V. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.05.012 · Cited by 72
Networks of Networks: An Essay on Multi-Level Biological Organization
Uversky, V. N., & Giuliani, A. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.706260 · Cited by 28
Brown, A. H., Rodger, P. M., Evans, J. S., & Walsh, T. R. (2014) · Biomacromolecules · doi:10.1021/bm501263s · Cited by 28
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
About these checks
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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