The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Natively unfolded proteins
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Proteasomal degradation of tau protein
David, D. C., Layfield, R., Serpell, L., Narain, Y., Goedert, M., & Spillantini, M. G. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01137.x · Cited by 327
Love, J. J., Li, X., Chung, J., Dyson, H. J., & Wright, P. E. (2004) · Biochemistry · doi:10.1021/bi049591m · Cited by 66
Cited by
Flexible nets: The roles of intrinsic disorder in protein interaction networks
Dunker, A. K., Cortese, M. S., Romero, P., Iakoucheva, L. M., & Uversky, V. N. (2005) · The FEBS Journal · doi:10.1111/j.1742-4658.2005.04948.x · Cited by 1,122
Structure and mechanism of the Hsp90 molecular chaperone machinery
Pearl, L. H., & Prodromou, C. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142738 · Cited by 1,103
LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana
Hundertmark, M., & Hincha, D. K. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-118 · Cited by 1,044
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2005) · Journal of Molecular Recognition · doi:10.1002/jmr.747 · Cited by 847
Intrinsic Disorder in Transcription Factors
Liu, J., Perumal, N. B., Oldfield, C. J., Su, E. W., Uversky, V. N., & Dunker, A. K. (2006) · Biochemistry · doi:10.1021/bi0602718 · Cited by 792
The interplay between structure and function in intrinsically unstructured proteins
Tompa, P. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.072 · Cited by 717
Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
Hilser, V. J., & Thompson, E. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700329104 · Cited by 406
DISC1: Structure, Function, and Therapeutic Potential for Major Mental Illness
Soares, D. C., Carlyle, B. C., Bradshaw, N. J., & Porteous, D. J. (2011) · ACS Chemical Neuroscience · doi:10.1021/cn200062k · Cited by 129
Sequence‐similar, structure‐dissimilar protein pairs in the PDB
Kosloff, M., & Kolodny, R. (2008) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.21770 · Cited by 124
Does Intrinsic Disorder in Proteins Favor Their Interaction with Lipids?
Deryusheva, E., Nemashkalova, E., Galloux, M., Richard, C., Eléouët, J., Kovacs, D., Van Belle, K., Tompa, P., Uversky, V., & Permyakov, S. (2019) · PROTEOMICS · doi:10.1002/pmic.201800098 · Cited by 34
Deletion of drosophila nopp140 induces subcellular ribosomopathies
He, F., James, A., Raje, H., Ghaffari, H., & DiMario, P. (2015) · Chromosoma · doi:10.1007/s00412-014-0490-9 · Cited by 27
AlphaFold2 modeling and molecular dynamics simulations of an intrinsically disordered protein
Guo, H.-B., Huntington, B., Perminov, A., Smith, K., Hastings, N., Dennis, P., Kelley-Loughnane, N., & Berry, R. (2024) · PLOS ONE · doi:10.1371/journal.pone.0301866 · Cited by 13
Metadata
- Authors
- Fink, A. L.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2005-02
- Volume
- 15
- Issue
- 1
- Pages
- 35-41
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2092153867
- Cited by
- 698
- References
- 2
- FWCI
- 23.16
- 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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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.
