A multi-pathway perspective on protein aggregation: implications for control of the rate and extent of amyloid formation.
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Measurement of amyloid formation by turbidity assay-seeing through the cloudComparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formationBiophysical chemistry of the ageing eye lens.Supersaturation-limited and Unlimited Phase Transitions Compete to Produce the Pathway Complexity in Amyloid Fibrillation.What Can the Kinetics of Amyloid Fibril Formation Tell about Off-pathway Aggregation?Factors affecting the physical stability (aggregation) of peptide therapeutics.Biophysical studies of protein solubility and amorphous aggregation by systematic mutational analysis and a helical polymerization model.Heparin-dependent aggregation of hen egg white lysozyme reveals two distinct mechanisms of amyloid fibrillation.
P2860
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P2860
A multi-pathway perspective on protein aggregation: implications for control of the rate and extent of amyloid formation.
description
2015 nî lūn-bûn
@nan
2015 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
A multi-pathway perspective on ...... d extent of amyloid formation.
@ast
A multi-pathway perspective on ...... d extent of amyloid formation.
@en
type
label
A multi-pathway perspective on ...... d extent of amyloid formation.
@ast
A multi-pathway perspective on ...... d extent of amyloid formation.
@en
prefLabel
A multi-pathway perspective on ...... d extent of amyloid formation.
@ast
A multi-pathway perspective on ...... d extent of amyloid formation.
@en
P2860
P50
P1433
P1476
A multi-pathway perspective on ...... d extent of amyloid formation.
@en
P2093
Herman Edskes
P2860
P304
P356
10.1016/J.FEBSLET.2015.01.032
P407
P577
2015-01-31T00:00:00Z