Figures
Amyloid growth in yeast.
Recent discoveries show that prion phenomena in both humans and yeast are determined by amyloid-like conformations of misfolded proteins, and similar conformations are associated with noninfectious diseases such as Alzheimer's. Shown are AFM images of new amyloid growth from the ends of epitope-labeled seeds encapsulated in diagrams of yeast cells. (See Collins, et al.)
Image Credit: Image by Angela DePace
Citation: (2004) PLoS Biology Issue Image | Vol. 2(10) October 2004. PLoS Biol 2(10): ev02.i10. https://doi.org/10.1371/image.pbio.v02.i10
Published: October 26, 2004
Copyright: © 2004 Angela DePace. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Recent discoveries show that prion phenomena in both humans and yeast are determined by amyloid-like conformations of misfolded proteins, and similar conformations are associated with noninfectious diseases such as Alzheimer's. Shown are AFM images of new amyloid growth from the ends of epitope-labeled seeds encapsulated in diagrams of yeast cells. (See Collins, et al.)
Image Credit: Image by Angela DePace