The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
FlgM gains structure in living cells
Open accessAbstract
Intrinsically disordered proteins such as FlgM play important roles in biology, but little is known about their structure in cells. We use NMR to show that FlgM gains structure inside living Escherichia coli cell s and under physiologically relevant conditions in vitro , i.e., in solutions containing high concentrations (≥400 g/liter) of glucose, BSA, or ovalbumin. Structure formation represents solute-induced changes in the equilibrium between the structured and disordered forms of FlgM. The results provide insight into how the environment of intrinsically disordered proteins could dictate their structure and, in turn, emphasize the relevance of studying proteins in living cells and in vitro under physiologically realistic conditions.
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Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
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
Intrinsic Disorder and Protein Function
Dunker, A. K., Brown, C. J., Lawson, J. D., Iakoucheva, L. M., & Obradović, Z. (2002) · Biochemistry · doi:10.1021/bi012159+ · Cited by 1,731
Minton, A. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100005200 · Cited by 1,474
Cited by
Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions
Oldfield, C. J., & Dunker, A. K. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072711-164947 · Cited by 1,057
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
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
From Water and Ions to Crowded Biomacromolecules: In Vivo Structuring of a Prokaryotic Cell
Spitzer, J. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00010-11 · Cited by 77
Rational design of 19F NMR labelling sites to probe protein structure and interactions
Streit, J. O., Chan, S. H. S., Daya, S., & Christodoulou, J. (2025) · Nature Communications · doi:10.1038/s41467-025-59105-6 · Cited by 17
Metadata
- Authors
- Dedmon, M. M., Patel, C. N., Young, G. B., & Pielak, G. J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2002-09-23
- Volume
- 99
- Issue
- 20
- Pages
- 12681-12684
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1995838356
- Cited by
- 317
- References
- 4
- FWCI
- 4.43
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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