The DOI matches its Crossref record; 307 of the 307 references it cites were found in a registry or an index.
What Macromolecular Crowding Can Do to a Protein
Open accessAbstract
The intracellular environment represents an extremely crowded milieu, with a limited amount of free water and an almost complete lack of unoccupied space. Obviously, slightly salted aqueous solutions containing low concentrations of a biomolecule of interest are too simplistic to mimic the “real life” situation, where the biomolecule of interest scrambles and wades through the tightly packed crowd. In laboratory practice, such macromolecular crowding is typically mimicked by concentrated solutions of various polymers that serve as model “crowding agents”. Studies under these conditions revealed that macromolecular crowding might affect protein structure, folding, shape, conformational stability, binding of small molecules, enzymatic activity, protein-protein interactions, protein-nucleic acid interactions, and pathological aggregation. The goal of this review is to systematically analyze currently available experimental data on the variety of effects of macromolecular crowding on a protein molecule. The review covers more than 320 papers and therefore represents one of the most comprehensive compendia of the current knowledge in this exciting area.
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Cites
Principles of polymer chemistry
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Protein Misfolding, Functional Amyloid, and Human Disease
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Intrinsically unstructured proteins and their functions
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Germline P Granules Are Liquid Droplets That Localize by Controlled Dissolution/Condensation
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Intrinsically disordered protein
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Cited by
Uversky, V. N. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.10.015 · Cited by 707
Self-citationSerum albumin in health and disease: esterase, antioxidant, transporting and signaling properties
Belinskaia, D. A., Voronina, P. A., Shmurak, V. I., Jenkins, R. O., & Goncharov, N. V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910318 · Cited by 416
Liquid–Liquid Phase Separation in Crowded Environments
André, A. A. M., & Spruijt, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165908 · Cited by 334
Tardy, B. L., Mattos, B. D., Otoni, C. G., Beaumont, M., Majoinen, J., Kämäräinen, T., & Rojas, O. J. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01333 · Cited by 267
Tau liquid–liquid phase separation: At the crossroads of tau physiology and tauopathy
Islam, M., Shen, F., Regmi, D., Petersen, K., Karim, M. R. U., & Du, D. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.30853 · Cited by 28
Metadata
- Authors
- Kuznetsova, I., Turoverov, K., & Uversky, V.
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2014-12-12
- Volume
- 15
- Issue
- 12
- Pages
- 23090-23140
- ISSN
- 1422-0067 (ISSN-L)
- OpenAlex
- W2012500478
- Cited by
- 564
- References
- 307
- FWCI
- 11.44
- Type
- journal article
- Language
- en
- Open access
- gold
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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).
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