Macromolecular crowding: An important but neglected aspect of the intracellular environment

Current Opinion in Structural Biology

Volumn 11, Issue 1, 2001, Pages 114-119

  Ellis, R J ^a  

^a UNIVERSITY OF WARWICK   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN; DEXTRAN 70; FICOLL; GREEN FLUORESCENT PROTEIN; ISOTHIOCYANIC ACID; OVALBUMIN; PROTEIN; RNA; WATER;

ACTIN FILAMENT; CELL COMPOSITION; CELL PH; CYTOPLASM; ESCHERICHIA COLI; EUKARYOTIC CELL; EXTRACT; HEMOGLOBIN DETERMINATION; INTERMEDIATE FILAMENT; INTRACELLULAR FLUID; IONIC STRENGTH; MACROMOLECULE; METABOLIC REGULATION; METABOLITE; MICROTUBULE; MOLECULAR WEIGHT; NONHUMAN; NONLINEAR SYSTEM; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; REVIEW; RIBOSOME; THERMODYNAMICS;

ESCHERICHIA COLI; EUKARYOTA; NEGIBACTERIA;

EID: 0035253217     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(00)00172-X     Document Type: Review

References (30)

1. Effects of crowding in protein solutions
2. Influence of excluded volume upon macromolecular structure and associations in crowded media
3. Macromolecular crowding effects on macromolecular interactions: Some implications for genome structure and function
4. Implications of macromolecular crowding for protein assembly
5. Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli
6. The effect of volume occupancy upon the thermodynamic activity of proteins: Some biochemical consequences
7. Macromolecular crowding: Biochemical, biophysical and physiological consequences
8. Molecular crowding: Analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion
9. Confinement as a determinant of macromolecular structure and reactivity. II. Effects of weakly attractive interactions between confined macrosolutes and confining structures
10. Protein mobility in the cytoplasm of Escherichia coli
11. Direct observation of the self-association of dilute proteins in the presence of inert macromolecules at high concentration via tracer sedimentation equilibrium: Theory, experiment and biological significance
12. Effects of macromolecular crowding on protein folding and aggregation
13. Macromolecular crowding perturbs protein refolding kinetics: Implications for folding inside the cell
14. Avoiding the crowd
15. Principles of protein folding in the cellular environment
16. Protein folding in the cell: Competing models of chaperonin function
17. The effect of macromolecular crowding in chaperonin-mediated protein folding
18. Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein folding
19. In vivo newly translated polypeptides are sequestered in a protected folding environment
20. Molecular chaperones: Pathways and networks
21. Model for the role of macromolecular crowding in regulation of cellular volume
22. Photobleaching recovery and anisotropy decay of green fluorescent protein GFP S65T in solution and cells: Cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion
23. Rapid diffusion of green fluorescent protein in the mitochondrial matrix
24. Tracer diffusion of globular proteins in concentrated protein solutions
25. Determinants of the translational mobility of a small solute in cell cytoplasm
26. Translational diffusion of macromolecule-sized solutes in cytoplasm and nucleus
27. Molecular crowding and viscosity as determinants of translational diffusion of metabolites in subcellular organelles
28. Cytoarchitecture and physical properties of cytoplasm: Volume, viscosity, diffusion, intracellular surface area
29. Direct observation of the enhancement of non-cooperative protein self-assembly by macromolecular crowding