The environmentally responsive molecular chaperone Hsp90 assists the maturation of many
key regulatory proteins. An unexpected consequence of this essential biochemical function …

Our work suggests that the forces that govern protein folding exert a profound effect on how
genotypes are translated into phenotypes and that this in turn has strong effects on …

Canalization, or phenotypic robustness in the face of environmental and genetic
perturbation, is an emergent property of living systems. Although this phenomenon has long …

Protein chaperones direct the folding of polypeptides into functional proteins, facilitate
developmental signalling and, as heat-shock proteins (HSPs), can be indispensable for …

The protein-folding chaperone Hsp90 has been proposed to buffer the phenotypic effects of
mutations. The potential for Hsp90 and other putative buffers to increase robustness to …

HSP90 is a protein chaperone particularly important in the maturation of a diverse set of
proteins that regulate key steps in a multitude of biological processes. Alterations in HSP90 …

Modulation of the activity of the molecular chaperone HSP90 has been extensively
discussed as a means to alter phenotype in many traits and organisms. Such changes can …

Interactions among mutations within a protein have the potential to make molecular
evolution contingent and irreversible, but the extent to which epistasis actually shaped …

Genetic capacitors moderate expression of heritable variation and provide a novel
mechanism for rapid evolution. The prototypic genetic capacitor, Hsp90, interfaces stress …

How can species remain unaltered for long periods yet also undergo rapid diversification?
By linking genetic variation to phenotypic variation via environmental stress, the Hsp90 …