Display Settings:

Items per page
We are sorry, but NCBI web applications do not support your browser and may not function properly. More information

Results: 8

1.
Figure 6

Figure 6. Staggered and fixed structures of amyloid polymers.. From: The Effects of Amino Acid Composition of Glutamine-Rich Domains on Amyloid Formation and Fragmentation.

Schematic representation of amyloid polymers with a fixed fold, as proposed for yeast prion polymers, and a staggered fold, as proposed for polyQX amyloids.

Alexander I. Alexandrov, et al. PLoS One. 2012;7(10):e46458.
2.
Figure 2

Figure 2. Polymerization of polyQX proteins in the absence of [PIN+].. From: The Effects of Amino Acid Composition of Glutamine-Rich Domains on Amyloid Formation and Fragmentation.

Lysates of 74-D694/ΔS35 ΔRNQ1 cells producing QX proteins of different length were analyzed by SDD-AGE. Cells were grown for 20 generations after obtaining transformants. Staining with anti-S35NM antibodies.

Alexander I. Alexandrov, et al. PLoS One. 2012;7(10):e46458.
3.
Figure 7

Figure 7. Schematic model of the structure of the Sup35 prion domain.. From: The Effects of Amino Acid Composition of Glutamine-Rich Domains on Amyloid Formation and Fragmentation.

Fragmentation-promoting residues (blue rectangles), such as tyrosine, are hidden inside the amyloid core structure and cannot act as recognition signals for chaperones. Residues in the exposed area (yellow triangles) are available and can thus facilitate fragmentation.

Alexander I. Alexandrov, et al. PLoS One. 2012;7(10):e46458.
4.
Figure 4

Figure 4. Small SDS-insoluble polymers of QX proteins.. From: The Effects of Amino Acid Composition of Glutamine-Rich Domains on Amyloid Formation and Fragmentation.

(A) Lysates of 74-D694/ΔS35 [PIN+] Δprb1 cells producing 76QY, 96QW and 81QF were analyzed by SDS-PAGE without boiling the samples using large pore 5% gel. (B) 74-D694/ΔS35 [PIN+] Δprb1 cells producing 76QY were grown for different periods of time in the presence of GuHCl (3 mM), and then their lysates were analyzed by SDD-AGE (left panel) and SDS-PAGE without boiling the samples (large pore 5% gel) (right panel).

Alexander I. Alexandrov, et al. PLoS One. 2012;7(10):e46458.
5.
Figure 1

Figure 1. Polymerization of polyQX proteins in the presence of [PIN+].. From: The Effects of Amino Acid Composition of Glutamine-Rich Domains on Amyloid Formation and Fragmentation.

Lysates of 74-D694/ΔS35 [PIN+] cells producing indicated QX proteins were analyzed by SDD-AGE. (A) Most QX proteins readily form SDS-insoluble polymers of varying size. Staining with anti-S35NM antibodies. (B) Polymerization of QX proteins, which did not polymerize in a [PIN+] background on their own, in the presence of 85Q-GFP polymers and after loss of the plasmid encoding 85Q-GFP. Staining with anti-Sup35C.

Alexander I. Alexandrov, et al. PLoS One. 2012;7(10):e46458.
6.
Figure 8

Figure 8. Amino acid content of yeast prion domains.. From: The Effects of Amino Acid Composition of Glutamine-Rich Domains on Amyloid Formation and Fragmentation.

Percentages represent the proportion of the appropriate amino acids in yeast prion domains. The extent of the prion domains were taken from [32]. Fragmentation-promoting amino acids which are abundant in certain prion domains are marked in bold. Numbers on the left represent the group number we assigned to certain residues according to their effect on amyloid formation and fragmentation.

Alexander I. Alexandrov, et al. PLoS One. 2012;7(10):e46458.
7.
Figure 5

Figure 5. Thermal stability of prion polymers of full-size and truncated Sup35.. From: The Effects of Amino Acid Composition of Glutamine-Rich Domains on Amyloid Formation and Fragmentation.

(A) The lysates of [PSI+] yeast cells producing full-sized or truncated Sup35 were analyzed by SDD-AGE. (B, C) Lysates were heated in the presence of sample buffer containing 2% SDS at different temperatures and analyzed by SDD-AGE. The thermal denaturation curves were derived from densitometric analysis of the stained blot images.

Alexander I. Alexandrov, et al. PLoS One. 2012;7(10):e46458.
8.
Figure 3

Figure 3. Polyglutamine domain length influences polymer size and not polymer stability.. From: The Effects of Amino Acid Composition of Glutamine-Rich Domains on Amyloid Formation and Fragmentation.

(A) Lysates of 74-D694/ΔS35 [PIN+] cells producing QX proteins of different length were analyzed by SDD-AGE. Staining with anti-S35NM antibodies. (B) The lysates of 74-D694/ΔS35 [PIN+] cells producing QA71 and QA110 proteins were incubated at different temperatures in the presence of sample buffer containing 2% SDS and analyzed by SDD-AGE. The thermal denaturation curves were obtained by densitometric analysis of the stained blot images.

Alexander I. Alexandrov, et al. PLoS One. 2012;7(10):e46458.

Display Settings:

Items per page

Supplemental Content

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Write to the Help Desk