Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein.
about
Denatured mammalian protein mixtures exhibit unusually high solubility in nucleic acid-free pure water.Protein folding and aggregation into amyloid: the interference by natural phenolic compoundsAggregation of Full-length Immunoglobulin Light Chains from Systemic Light Chain Amyloidosis (AL) Patients Is Remodeled by Epigallocatechin-3-gallate.Mechanistic investigation of domain specific unfolding of human serum albumin and the effect of sucrose.Sucrose prevents protein fibrillation through compaction of the tertiary structure but hardly affects the secondary structure.Effect of buffer additives on solubilization and refolding of reteplase inclusion bodies
P2860
Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年学术文章
@wuu
2013年学术文章
@zh-cn
2013年学术文章
@zh-hans
2013年学术文章
@zh-my
2013年学术文章
@zh-sg
2013年學術文章
@yue
2013年學術文章
@zh
2013年學術文章
@zh-hant
name
Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein.
@en
Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein.
@nl
type
label
Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein.
@en
Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein.
@nl
prefLabel
Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein.
@en
Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein.
@nl
P2093
P2860
P356
P1433
P1476
Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein.
@en
P2093
Akira Monji
Masahiro Abe
Shigenobu Kanba
Tadashi Ueda
Takatoshi Ohkuri
Tomonori Mishima
P2860
P304
P356
10.1002/PRO.2228
P50
P577
2013-02-21T00:00:00Z