Amyloid-a state in many guises: survival of the fittest fibril fold.
about
Prions, protein homeostasis, and phenotypic diversityTransient dynamics of Aβ contribute to toxicity in Alzheimer's diseaseEnvironmental conditions affect the kinetics of nucleation of amyloid fibrils and determine their morphology.Protective role of human insulin against the cytotoxicity associated with human mutant S20G islet amyloid polypeptide.Aggregation of a multidomain protein: a coagulation mechanism governs aggregation of a model IgG1 antibody under weak thermal stressEndoplasmic reticulum export, subcellular distribution, and fibril formation by Pmel17 require an intact N-terminal domain junction.An analytical solution to the kinetics of breakable filament assembly.Biochemical stabilization of glucagon at alkaline pH.In vitro and in vivo evaluation of native glucagon and glucagon analog (MAR-D28) during aging: lack of cytotoxicity and preservation of hyperglycemic effectBranching in amyloid fibril growth.Toxic oligomers and islet beta cell death: guilty by association or convicted by circumstantial evidence?Amyloid structure--one but not the same: the many levels of fibrillar polymorphism.The nature of amyloid-like glucagon fibrilsProtein fibrillation and nanoparticle interactions: opportunities and challenges.Formation of multimeric antibodies for self-delivery of active monomers.Stability and cytotoxicity of crystallin amyloid nanofibrils.Force Sensitivity in Saccharomyces cerevisiae Flocculins.Thermodynamic description of polymorphism in Q- and N-rich peptide aggregates revealed by atomistic simulation.Fibrillation of the major curli subunit CsgA under a wide range of conditions implies a robust design of aggregation.Amyloid fibrils containing fragmented ATTR may be the standard fibril composition in ATTR amyloidosis.Spectroscopic evidence for the existence of an obligate pre-fibrillar oligomer during glucagon fibrillation.Self-assembly of short peptides composed of only aliphatic amino acids and a combination of aromatic and aliphatic amino acids.An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils.Stop-and-go kinetics in amyloid fibrillationFunctional Amyloids in Bacteria
P2860
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P2860
Amyloid-a state in many guises: survival of the fittest fibril fold.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
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2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
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2007年學術文章
@zh-hant
name
Amyloid-a state in many guises: survival of the fittest fibril fold.
@en
Amyloid-a state in many guises: survival of the fittest fibril fold.
@nl
type
label
Amyloid-a state in many guises: survival of the fittest fibril fold.
@en
Amyloid-a state in many guises: survival of the fittest fibril fold.
@nl
prefLabel
Amyloid-a state in many guises: survival of the fittest fibril fold.
@en
Amyloid-a state in many guises: survival of the fittest fibril fold.
@nl
P2860
P356
P1433
P1476
Amyloid-a state in many guises: survival of the fittest fibril fold.
@en
P2860
P356
10.1110/PS.073127808
P577
2007-11-27T00:00:00Z