Amyloid structure--one but not the same: the many levels of fibrillar polymorphism.
about
Mapping out the multistage fibrillation of glucagonUnlocked concanavalin A forms amyloid-like fibrils from coagulation of long-lived "crinkled" intermediates.Structural analysis of peptide-analogues of human Zona Pellucida ZP1 protein with amyloidogenic properties: insights into mammalian Zona Pellucida formationA monomer-trimer model supports intermittent glucagon fibril growth.Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue levelInfrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation.Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif.The emergence of superstructural order in insulin amyloid fibrils upon multiple rounds of self-seedingAFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species.Natural and amyloid self-assembly of S100 proteins: structural basis of functional diversity.The nature of amyloid-like glucagon fibrilsThe effect of osmolytes on protein fibrillationPeptide and protein-based nanotubes for nanobiotechnology.Molecular understanding of a potential functional link between antimicrobial and amyloid peptides.Application and use of differential scanning calorimetry in studies of thermal fluctuation associated with amyloid fibril formation.An amyloidogenic determinant in N-terminal pro-brain natriuretic peptide (NT-proBNP): Implications for cardiac amyloidoses.High resolution spectroscopy reveals fibrillation inhibition pathways of insulin.Small heat shock protein AgsA forms dynamic fibrils.Factors affecting the physical stability (aggregation) of peptide therapeutics.Response surface methodology for optimizing the bovine serum albumin fibrillation.Influence of the β-sheet content on the mechanical properties of aggregates during amyloid fibrillization.Insights into Insulin Fibril Assembly at Physiological and Acidic pH and Related Amyloid Intrinsic Fluorescence.Directing peptide crystallization through curvature control of nanotubesHelD, an RNA Polymerase Interacting Helicase, Forms Amyloid-Like FibrilsDifferent morphology of amyloid fibrils originating from agitated and non-agitated conditions
P2860
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P2860
Amyloid structure--one but not the same: the many levels of fibrillar polymorphism.
description
2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年學術文章
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2010年學術文章
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2010年學術文章
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name
Amyloid structure--one but not the same: the many levels of fibrillar polymorphism.
@en
Amyloid structure--one but not the same: the many levels of fibrillar polymorphism.
@nl
type
label
Amyloid structure--one but not the same: the many levels of fibrillar polymorphism.
@en
Amyloid structure--one but not the same: the many levels of fibrillar polymorphism.
@nl
prefLabel
Amyloid structure--one but not the same: the many levels of fibrillar polymorphism.
@en
Amyloid structure--one but not the same: the many levels of fibrillar polymorphism.
@nl
P2860
P1433
P1476
Amyloid structure--one but not the same: the many levels of fibrillar polymorphism.
@en
P2093
Christian B Andersen
P2860
P304
P356
10.1111/J.1742-4658.2010.07888.X
P407
P577
2010-11-01T00:00:00Z