The DOI matches its Crossref record; 79 of the 79 references it cites were found in a registry or an index.
Models of macromolecular crowding effects and the need for quantitative comparisons with experiment
Open accessAbstract
Summary In recent years significant effort has been devoted to exploring the potential effects of macromolecular crowding on protein folding and association phenomena. Theoretical calculations and molecular simulations have, in particular, been exploited to describe aspects of protein behavior in crowded and confined conditions and many aspects of the simulated behavior have reflected, at least at a qualitative level, the behavior observed in experiments. One major and immediate challenge for the theorists is to now produce models capable of making quantitatively accurate predictions of in vitro behavior. A second challenge is to derive models that explain results obtained from experiments performed in vivo, the results of which appear to call into question the assumed dominance of excluded volume effects in vivo.
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
VMD: visual molecular dynamics
Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952
Some Topics in the Theory of Fluids
Widom, B. (1963) · The Journal of Chemical Physics · doi:10.1063/1.1734110 · Cited by 3,035
Zhou, H.-X., Rivas, G., & Minton, A. P. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125817 · Cited by 2,149
Macromolecular 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
Statistical Mechanics of Rigid Spheres
Reiss, H., Frisch, H. L., & Lebowitz, J. L. (1959) · The Journal of Chemical Physics · doi:10.1063/1.1730361 · Cited by 1,433
Converging concepts of protein folding in vitro and in vivo
Hartl, F. U., & Hayer-Hartl, M. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1591 · Cited by 1,185
Rapid, electrostatically assisted association of proteins
Schreiber, G., & Fersht, A. R. (1996) · Nature Structural Biology · doi:10.1038/nsb0596-427 · Cited by 559
Molecular crowding enhances native state stability and refolding rates of globular proteins
Cheung, M. S., Klimov, D., & Thirumalai, D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409630102 · Cited by 558
Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges
Hall, D., & Minton, A. P. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/s1570-9639(03)00167-5 · Cited by 488
Lee, H., Venable, R. M., MacKerell, A. D., & Pastor, R. W. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.133025 · Cited by 472
Cited by
Anomalous transport in the crowded world of biological cells
Höfling, F., & Franosch, T. (2013) · Reports on Progress in Physics · doi:10.1088/0034-4885/76/4/046602 · Cited by 1,247
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
Macromolecular Crowding and Protein Stability
Wang, Y., Sarkar, M., Smith, A. E., Krois, A. S., & Pielak, G. J. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305300m · Cited by 346
A quantitative measure for protein conformational heterogeneity
Lyle, N., Das, R. K., & Pappu, R. V. (2013) · The Journal of Chemical Physics · doi:10.1063/1.4812791 · Cited by 85
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
Metadata
- Authors
- Elcock, A. H.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2010-04
- Volume
- 20
- Issue
- 2
- Pages
- 196-206
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2096759266
- Cited by
- 286
- References
- 79
- FWCI
- 10.99
- Type
- journal article
- Language
- en
- Open access
- green
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: Models of macromolecular crowding effects and the need for quantitative comparisons with experiment. https://app.cochat.ai/papers/10.1016/j.sbi.2010.01.008
- The paper
- Elcock, A. H. (2010). Models of macromolecular crowding effects and the need for quantitative comparisons with experiment. Current Opinion in Structural Biology. https://doi.org/10.1016/j.sbi.2010.01.008
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.
