The DOI matches its Crossref record; 175 of the 175 references it cites were found in a registry or an index.
Intrinsically Disordered Proteins and Their Environment: Effects of Strong Denaturants, Temperature, pH, Counter Ions, Membranes, Binding Partners, Osmolytes, and Macromolecular Crowding
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Citations
Cites
p53 Mutations in Human Cancers
Hollstein, M., Sidransky, D., Vogelstein, B., & Harris, C. C. (1991) · Science · doi:10.1126/science.1905840 · Cited by 8,018
Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871
Living with Water Stress: Evolution of Osmolyte Systems
Yancey, P. H., Clark, M. E., Hand, S. C., Bowlus, R. D., & Somero, G. N. (1982) · Science · doi:10.1126/science.7112124 · Cited by 3,740
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
Macromolecular crowding: obvious but underappreciated
Ellis, R. J. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01938-7 · Cited by 2,309
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
[14]Determination and analysis of urea and guanidine hydrochloride denaturation curves
Pace, C. N. (1986) · Methods in Enzymology · doi:10.1016/0076-6879(86)31045-0 · Cited by 2,258
Stability of Proteins Small Globular Proteins
Privalov, P. L. (1979) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60460-x · Cited by 2,159
Tanford, C. (1968) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60401-5 · Cited by 2,130
Why are ?natively unfolded? proteins unstructured under physiologic conditions?
Uversky, V. N., Gillespie, J. R., & Fink, A. L. (2000) · Proteins: Structure, Function, and Genetics · doi:10.1002/1097-0134(20001115)41:3<415::aid-prot130>3.0.co;2-7 · Cited by 2,078
Self-citation
Cited by
Neuroinflammation as a common feature of neurodegenerative disorders
Guzman-Martinez, L., Maccioni, R. B., Andrade, V., Navarrete, L. P., Pastor, M. G., & Ramos-Escobar, N. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01008 · Cited by 702
Effects of Molecular Crowding on the Structures, Interactions, and Functions of Nucleic Acids
Nakano, S.-I., Miyoshi, D., & Sugimoto, N. (2014) · Chemical Reviews · doi:10.1021/cr400113m · Cited by 567
Unusual biophysics of intrinsically disordered proteins
Uversky, V. N. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.12.008 · Cited by 566
Self-citationIntrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics
Uversky, V. N. (2019) · Frontiers in Physics · doi:10.3389/fphy.2019.00010 · Cited by 532
Self-citationRandom coil chemical shift for intrinsically disordered proteins: effects of temperature and pH
Kjaergaard, M., Brander, S., & Poulsen, F. M. (2011) · Journal of Biomolecular NMR · doi:10.1007/s10858-011-9472-x · Cited by 313
Metadata
- Authors
- Uversky, V. N.
- Venue
- The Protein Journal
- Published
- 2009-09-19
- Volume
- 28
- Issue
- 7-8
- Pages
- 305-325
- ISSN
- 1572-3887 (ISSN-L)
- 1875-8355
- OpenAlex
- W2019511236
- Cited by
- 360
- References
- 175
- FWCI
- 8.28
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Intrinsically Disordered Proteins and Their Environment: Effects of Strong Denaturants, Temperature, pH, Counter Ions, Membranes, Binding Partners, Osmolytes, and Macromolecular Crowding. https://app.cochat.ai/papers/10.1007/s10930-009-9201-4
- The paper
- Uversky, V. N. (2009). Intrinsically Disordered Proteins and Their Environment: Effects of Strong Denaturants, Temperature, pH, Counter Ions, Membranes, Binding Partners, Osmolytes, and Macromolecular Crowding. The Protein Journal. https://doi.org/10.1007/s10930-009-9201-4
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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.
