Putative aggregation initiation sites in prion protein.

Putative aggregation initiation sites in prion protein.

Item
http://www.wikidata.org/entity/Q47844161
Prion protein self-peptides modulate prion interactions and conversion.Structural and dynamic properties of the human prion protein.Prion protein misfolding.Copper alters aggregation behavior of prion protein and induces novel interactions between its N- and C-terminal regions.Computer simulation study of amyloid fibril formation by palindromic sequences in prion peptidesEnergy landscape of the prion protein helix 1 probed by metadynamics and NMR.The protonation state of histidine 111 regulates the aggregation of the evolutionary most conserved region of the human prion protein.Determination of amyloid core structure using chemical shifts.Structural and hydration properties of the partially unfolded states of the prion protein.Structural, thermodynamical, and dynamical properties of oligomers formed by the amyloid NNQQ peptide: Insights from coarse-grained simulationsProduction of Whey Protein-Based Aggregates Under Ohmic Heating
P2860

Putative aggregation initiation sites in prion protein.

Item
http://www.wikidata.org/entity/Q47844161
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh
2006年學術文章
@zh-hant
name
Putative aggregation initiation sites in prion protein.
@en
Putative aggregation initiation sites in prion protein.
@nl
type
label
Putative aggregation initiation sites in prion protein.
@en
Putative aggregation initiation sites in prion protein.
@nl
prefLabel
Putative aggregation initiation sites in prion protein.
@en
Putative aggregation initiation sites in prion protein.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P921
P356
P1433
P1476
Putative aggregation initiation sites in prion protein.
@en
P2093
P2860
P304
P31
P356
10.1016/J.FEBSLET.2006.03.002
P407
P433
P478
P577
P5875
P698
P921