Macromolecular crowding: an important but neglected aspect of the intracellular environment.
By R. Ellis. Current Opinion in Structural Biology, 2001
1,053 citations recorded by the source corpus.
Subfields: Molecular Biology, Spectroscopy
View Paper: https://www.semanticscholar.org/paper/b42682e3de4d60d5af8f64d257530a92771b55b0
How researchers see this paper
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In Molecular Biology
- S. Alberti
- D. Dormann
- Ralf Metzler
- Jesse D. Bloom
- P. Muchowski
- Matthew J. Glassman
- Jennifer L. Wacker
- Jae-Hyung Jeon
In Spectroscopy
- M. Grimaldo
- F. Roosen‐Runge
- Christopher M. Dobson
- S. Alberti
- Maura Coughlin
- J. Paul Taylor
- A. Kanagaraj
- Hong Joo Kim
Citations in the corpus
- Biological Physics of the Developing Embryo (2005, neutral): “It is not surprising, therefore, that simple diffusion is increasingly seen to be not an entirely adequate mechanism for extended intracellular transport (Ellis, 2001; Hall and Minton, 2003; Medalia et al., 2002); at best it can act on a submicrometer scale (Goulian and Simon, 2000; Shav-Tal et al.”
- Liquid-Liquid Phase Separation in Disease. (2019, background): “For proteins, this fraction amounts to more than 30%, translating to an overall concentration of 150 mg/ml in eukaryotic cells (47).”
- Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization (2015, positive): “Whereas LLPS by hnRNPA1 occurs spontaneously in a temperature- and protein-concentration-dependent manner in the absence of a crowding agent (Figure S4A), we mapped the phase diagram in the presence of Ficoll, a typical crowding agent, to mimic the crowded cellular environment, which is thought to c”
- Inferring Stabilizing Mutations from Protein Phylogenies: Application to Influenza Hemagglutinin (2009, background): “However, many proteins do not fold reversibly [45,54,116], and even for those that do, the measured stabilities can be sensitive to the solvent conditions [89,117,118], which are usually quite different from the in vivo cellular milieu [119].”
- Dynamics of proteins in solution (2019, background): “…also the protein internal dynamics, and thus potentially protein function including reaction equilibria, is expected and indeed found to be affected by macromolecular crowding, i.e. by the high concentrations found in physiological environments (see e.g. (Ellis, 2001; Grimaldo et al., 2014)).”
- Protein Crowding in Lipid Bilayers Gives Rise to Non-Gaussian Anomalous Lateral Diffusion of Phospholipids and Proteins (2016, background): “biological cells [11], membranes are crowded with proteins”
- Protein folding and misfolding (2003, background): “But because incompletely folded proteins must inevitably expose to the solvent at least some regions of structure that are buried in the native state, they are prone to inappropriate interaction with other molecules within the crowded environment of a cel”
- Modulation of neurodegeneration by molecular chaperones (2005, background): “As a consequence, protein folding in vivo is typically not spontaneou”
- Fundamental Limits to Cellular Sensing (2015, background): “They also take up valuable space: both the membrane and the cytoplasm are highly crowded, with proteins occupying 25–75 % of the membrane area [50] and 20–30 % of the cytoplasmic volume [29].”