The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
The role of structural disorder in the function of RNA and protein chaperones
Abstract
Chaperones are highly sophisticated protein machines that assist the folding of RNA molecules or other proteins. Their function is generally thought to require a fine‐tuned and highly conserved structure: despite the recent recognition of the widespread occurrence of structural disorder in the proteome, this structural trait has never been generally considered in molecular chaperones. In this review we give evidence for the prevalence of functional regions without a well‐defined 3‐D structure in RNA and protein chaperones. By considering a variety of individual examples, we suggest that the structurally disordered chaperone regions either function as molecular recognition elements that act as solubilizers or locally loosen the structure of the kinetically trapped folding intermediate via transient binding to facilitate its conformational search. The importance of structural disorder is underlined by a predictor of natural disordered regions, which shows an extremely high proportion of such regions, unparalleled in any other protein class, within RNA chaperones: 54.2% of their residues fall into disordered regions and 40% fall within disordered regions longer than 30 consecutive residues. Structural disorder also prevails in protein chaperones, for which frequency values are 36.7% and 15%, respectively. In keeping with these and other details, a novel “entropy transfer” model is presented to account for the mechanistic role of structural disorder in chaperone function.—Tompa, P., Csermely, P. The role of structural disorder in the function of RNA and protein chaperones. FASEB J . 18, 1169–1175 (2004)
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Gilbert, W. (1986) · Nature · doi:10.1038/319618a0 · Cited by 2,721
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
Poole, A. M., Jeffares, D. C., & Penny, D. (1998) · Journal of Molecular Evolution · doi:10.1007/pl00006275 · Cited by 274
Pontius, B. W. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90111-y · Cited by 183
Weikl, T., Abelmann, K., & Buchner, J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3172 · Cited by 97 · cited 2×
“Removal of the disordered segment by limited proteolysis often abolishes or markedly reduces chaperone activity in other instances, such as for p23 co-chaperone (18), -crystallin (38), and Hsp25 (19).”
Background
Cited by
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
Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins
Castello, A., Fischer, B., Eichelbaum, K., Horos, R., Beckmann, B. M., Strein, C., Davey, N. E., Humphreys, D. T., Preiss, T., Steinmetz, L. M., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.031 · Cited by 2,132
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
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
Csermely, P., Palotai, R., & Nussinov, R. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.009 · Cited by 821
Self-citationThe 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
Self-citationYB ‐1 protein: functions and regulation
Lyabin, D. N., Eliseeva, I. A., & Ovchinnikov, L. P. (2014) · WIREs RNA · doi:10.1002/wrna.1200 · Cited by 381
Hong, W., Jiao, W., Hu, J., Zhang, J., Liu, C., Fu, X., Shen, D., Xia, B., & Chang, Z. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503934200 · Cited by 132
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
Koduri, V., & Blacklow, S. C. (2007) · Biochemistry · doi:10.1021/bi700049g · Cited by 25
Murvai, N., Kalmar, L., Szalaine Agoston, B., Szabo, B., Tantos, A., Csikos, G., Micsonai, A., Kardos, J., Vertommen, D., Nguyen, P. N., et al. (2020) · Cells · doi:10.3390/cells9081856 · Cited by 13
Self-citation
Metadata
- Authors
- Tompa, P., & Csermely, P.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2004-08
- Volume
- 18
- Issue
- 11
- Pages
- 1169-1175
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W2113039254
- Cited by
- 553
- References
- 5
- FWCI
- 7.00
- Type
- journal article
- Language
- en
- Open access
- closed
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
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.
