Abstract
Amyloid fibrils share a structural motif consisting of highly ordered β-sheets aligned perpendicular to the fibril axis. 1,2 At each fibril end, β-sheets provide a template for recruiting and converting monomers. 3 Different amyloid fibrils often co-occur in the same individual, yet whether a protein aggregate aids or inhibits the assembly of a heterologous protein is unclear. In prion disease, diverse prion aggregate structures, known as strains, are thought to be the basis of disparate disease phenotypes in the same species expressing identical prion protein sequences. 4-7 Here we explore the interactions reported to occur when two distinct prion strains occur together in the central nervous system.
| Original language | English |
|---|---|
| Pages (from-to) | 52-55 |
| Number of pages | 4 |
| Journal | Prion |
| Volume | 5 |
| Issue number | 2 |
| DOIs |
|
| State | Published - Apr 2011 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Biochemistry
- Cell Biology
- Infectious Diseases
- Cellular and Molecular Neuroscience
Cite this
Tracking protein aggregate interactions. / Sigurdson, Christina J.; Bartz, Jason C.; Nilsson, K. Peter R.
In: Prion, Vol. 5, No. 2, 04.2011, p. 52-55.Research output: Contribution to journal › Comment/debate
}
TY - JOUR
T1 - Tracking protein aggregate interactions
AU - Sigurdson, Christina J.
AU - Bartz, Jason C.
AU - Nilsson, K. Peter R
PY - 2011/4
Y1 - 2011/4
N2 - Amyloid fibrils share a structural motif consisting of highly ordered β-sheets aligned perpendicular to the fibril axis. 1,2 At each fibril end, β-sheets provide a template for recruiting and converting monomers. 3 Different amyloid fibrils often co-occur in the same individual, yet whether a protein aggregate aids or inhibits the assembly of a heterologous protein is unclear. In prion disease, diverse prion aggregate structures, known as strains, are thought to be the basis of disparate disease phenotypes in the same species expressing identical prion protein sequences. 4-7 Here we explore the interactions reported to occur when two distinct prion strains occur together in the central nervous system.
AB - Amyloid fibrils share a structural motif consisting of highly ordered β-sheets aligned perpendicular to the fibril axis. 1,2 At each fibril end, β-sheets provide a template for recruiting and converting monomers. 3 Different amyloid fibrils often co-occur in the same individual, yet whether a protein aggregate aids or inhibits the assembly of a heterologous protein is unclear. In prion disease, diverse prion aggregate structures, known as strains, are thought to be the basis of disparate disease phenotypes in the same species expressing identical prion protein sequences. 4-7 Here we explore the interactions reported to occur when two distinct prion strains occur together in the central nervous system.
UR - http://www.scopus.com/inward/record.url?scp=79959436260&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79959436260&partnerID=8YFLogxK
U2 - 10.4161/pri.5.2.16173
DO - 10.4161/pri.5.2.16173
M3 - Comment/debate
C2 - 21597336
AN - SCOPUS:79959436260
VL - 5
SP - 52
EP - 55
JO - Prion
JF - Prion
SN - 1933-6896
IS - 2
ER -