The DOI matches its Crossref record; 70 of the 70 references it cites were found in a registry or an index.
Protein aggregation in crowded environments
Abstract
The generic tendency of proteins to aggregate into non-functional, and sometimes cytotoxic, structures poses a universal problem for all types of cell. This tendency is greatly exacerbated by the high total concentration of macromolecules found within most intracellular compartments, a phenomenon referred to as macromolecular crowding. This review discusses the quantitative effects of crowding on protein aggregation and the role of molecular chaperones in combating this problem.
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
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
Hartl, F. U., & Hayer-Hartl, M. (2002) · Science · doi:10.1126/science.1068408 · Cited by 3,347
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
Self-citationMacromolecular Crowding: Biochemical, Biophysical, and Physiological Consequences
Zimmerman, S. B., & Minton, A. P. (1993) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.bb.22.060193.000331 · Cited by 1,513
Self-citationCrick, F. (1958) · PubMed · Cited by 1,487
Minton, A. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100005200 · Cited by 1,474 · cited 3×
“…limited by decay of the transition state to product: g g1 i-1ok sk (5)i i gts and gtsok ;k , (6)-i i gi where kio and k-io denote the forward and backward rate constants in the absence of background molecules, and gts denotes the activity coefficient of the transition-state complex (Minton, 2001b).”
BackgroundSelf-citationZimmerman, S. B., & Trach, S. O. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90499-v · Cited by 1,337
The spaces in a uniform random suspension of fibres
Ogston, A. G. (1958) · Transactions of the Faraday Society · doi:10.1039/tf9585401754 · Cited by 1,058
The structural basis of protein folding and its links with human disease
Dobson, C. M. (2001) · Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences · doi:10.1098/rstb.2000.0758 · Cited by 932
Cited by
Molecular chaperones in protein folding and proteostasis
Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,381
In vivo aspects of protein folding and quality control
Balchin, D., Hayer-Hartl, M., & Hartl, F. U. (2016) · Science · doi:10.1126/science.aac4354 · Cited by 1,439
Csermely, P., Palotai, R., & Nussinov, R. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.009 · Cited by 821
Proteostasis impairment in protein-misfolding and -aggregation diseases
Hipp, M. S., Park, S.-H., & Hartl, F. U. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.05.003 · Cited by 663
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
Metadata
- Authors
- Ellis, R. J., & Minton, A. P.
- Venue
- Biological Chemistry
- Publisher
- Walter de Gruyter GmbH
- Published
- 2006-01-01
- Volume
- 387
- Issue
- 5
- Pages
- 485-97
- ISSN
- 1431-6730 (ISSN-L)
- 1437-4315
- OpenAlex
- W2053202443
- Cited by
- 421
- References
- 70
- FWCI
- 7.49
- 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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Protein aggregation in crowded environments. https://app.cochat.ai/papers/10.1515/bc.2006.064
- The paper
- Ellis, R. J., & Minton, A. P. (2006). Protein aggregation in crowded environments. Biological Chemistry. https://doi.org/10.1515/bc.2006.064
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.
