Research Topics
| R John EllisSummaryAffiliation: University of Warwick Country: UK Publications
| Collaborators |
Detail Information
Publications
Molecular chaperones: assisting assembly in addition to foldingR John Ellis
Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK
Trends Biochem Sci 31:395-401. 2006....
Protein aggregation in crowded environmentsR John Ellis
Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK
Biol Chem 387:485-97. 2006..This review discusses the quantitative effects of crowding on protein aggregation and the role of molecular chaperones in combating this problem...
Protein misassembly: macromolecular crowding and molecular chaperonesR John Ellis
Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK
Adv Exp Med Biol 594:1-13. 2007..This review discusses some of the basic evidence and key concepts relating to this conclusion...
Macromolecular crowding: an important but neglected aspect of the intracellular environmentR J Ellis
Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK
Curr Opin Struct Biol 11:114-9. 2001..It is proposed that the addition of crowding agents should become as routine as controlling pH and ionic strength if we are to meet the objective of studying biological molecules under more physiologically relevant conditions...
Macromolecular crowding: obvious but underappreciatedR J Ellis
Dept of Biological Sciences, University of Warwick, Coventry, CV4 7AL, UK
Trends Biochem Sci 26:597-604. 2001..Positive results of crowding include enhancing the collapse of polypeptide chains into functional proteins, the assembly of oligomeric structures and the efficiency of action of some molecular chaperones and metabolic pathways...
Molecular chaperones: inside and outside the Anfinsen cageR J Ellis
Department of Biological Sciences, University of Warwick, CV4 7AL, Coventry, UK
Curr Biol 11:R1038-40. 2001..Refolding aconitase is too large to enter the cage but reversible binding to GroEL reduces its aggregration. Unexpectedly, confinement in the cage increases the rate of refolding of rubisco, but not rhodanese...
Protein folding: importance of the Anfinsen cageR John Ellis
Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK
Curr Biol 13:R881-3. 2003
Chaperomics: in vivo GroEL function definedR John Ellis
Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK
Curr Biol 15:R661-3. 2005..These proteins are enriched in alpha/beta domains and 13 are essential for growth...
Protein folding: inside the cageR John Ellis
Nature 442:360-2. 2006
The attention of researchers on the biological process of protein folding has turned to the formation and properties of aggregatesR John Ellis
Semin Cell Dev Biol 15:1-2. 2004
Cell biology: join the crowdR John Ellis
Nature 425:27-8. 2003
Medicine: danger--misfolding proteinsR John Ellis
Nature 416:483-4. 2002
The chaperone function: meanings and mythsPeter A Lund
School of Biological Sciences, University of Birmingham, Birmingham B15 2TT, UK
Novartis Found Symp 291:23-36; discussion 36-44, 137-40. 2008..The aim of this article is to provide a brief summary of the origin and concepts used in the intracellular chaperone field, to provide a backdrop for discussion of their possible roles outside the cell...
