• Publications
  • Influence
Macromolecular crowding: obvious but underappreciated.
  • R. Ellis
  • Biology, Medicine
  • Trends in biochemical sciences
  • 1 October 2001
Biological macromolecules evolve and function within intracellular environments that are crowded with other macromolecules. Crowding results in surprisingly large quantitative effects on both theExpand
Homologous plant and bacterial proteins chaperone oligomeric protein assembly
An abundant chloroplast protein is implicated in the assembly of the oligomeric enzyme ribulose bisphosphate carboxylase-oxygenase, which catalyses photosynthetic CO2-fixation in higher plants. TheExpand
The most abundant protein in the world
Abstract The most abundant protein in nature is probably the chloroplast enzyme ribulose bisphosphate carboxylase/oxygenase (Fraction I protein). It is arguably the most important enzyme because itExpand
Macromolecular crowding: an important but neglected aspect of the intracellular environment.
  • R. Ellis
  • Mathematics, Medicine
  • Current opinion in structural biology
  • 2001
Biological macromolecules have evolved over billions of years to function inside cells, so it is not surprising that researchers studying the properties of such molecules, either in extracts or inExpand
Molecular Chaperones
Protein synthesis in chloroplasts. IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts.
Isolated pea (Pisum sativum) chloroplasts incorporate [35S]methionine into the large subunit of the chloroplast enzyme ribulose bisphosphate carboxylase. When chloroplasts are incubated in a mediumExpand
Cell biology: Join the crowd
Cells are packed with large molecules. The ramifications of this 'crowding' for a wide range of intracellular processes are only now becoming more generally understood.
Effects of macromolecular crowding on protein folding and aggregation
We have studied the effects of polysaccharide and protein crowding agents on the refolding of oxidized and reduced hen lysozyme in order to test the prediction that association constants ofExpand
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 exacerbatedExpand
Principles of protein folding in the cellular environment.
  • R. Ellis, F. Hartl
  • Biology, Medicine
  • Current opinion in structural biology
  • 1 February 1999
The ability of newly synthesised protein chains to fold into their functional conformations has evolved within the complex intracellular environment. Until recently, however, this ability has beenExpand
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