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Protein misfolding, functional amyloid, and human disease
Peptides or proteins convert under some conditions from their soluble forms into highly
ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging …
ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging …
Spherulites
Spherulites | Chemical Reviews Recently Viewedclose modal ACS ACS Publications C&EN CAS
Find my institution Log In ACS Publications. Most Trusted. Most Cited. Most Read Chemical …
Find my institution Log In ACS Publications. Most Trusted. Most Cited. Most Read Chemical …
Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status
M Groenning - Journal of chemical biology, 2010 - Springer
Because understanding amyloid fibrillation in molecular detail is essential for development
of strategies to control amyloid formation and overcome neurodegenerative disorders …
of strategies to control amyloid formation and overcome neurodegenerative disorders …
The binding of thioflavin-T to amyloid fibrils: localisation and implications
MRH Krebs, EHC Bromley, AM Donald - Journal of structural biology, 2005 - Elsevier
Amyloid fibrils are a polymeric form of protein, involving a continuous β-sheet with the
strands perpendicular to the long axis of the fibril. Although typically implicated in diseases …
strands perpendicular to the long axis of the fibril. Although typically implicated in diseases …
Characterization of the nanoscale properties of individual amyloid fibrils
We report the detailed mechanical characterization of individual amyloid fibrils by atomic
force microscopy and spectroscopy. These self-assembling materials, formed here from the …
force microscopy and spectroscopy. These self-assembling materials, formed here from the …
Protein aggregation and neurodegenerative diseases: From theory to therapy
The study of protein misfolding and aggregation saw resurgence in the last decade.
Aggregation is the main cause of several human neurodegenerative diseases which makes …
Aggregation is the main cause of several human neurodegenerative diseases which makes …
Aβ (1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils
J Meinhardt, C Sachse, P Hortschansky… - Journal of molecular …, 2009 - Elsevier
Amyloid fibrils characterize a diverse group of human diseases that includes Alzheimer's
disease, Creutzfeldt-Jakob and type II diabetes. Alzheimer's amyloid fibrils consist of …
disease, Creutzfeldt-Jakob and type II diabetes. Alzheimer's amyloid fibrils consist of …
Structural polymorphism of Alzheimer Aβ and other amyloid fibrils
M Fändrich, J Meinhardt, N Grigorieff - Prion, 2009 - Taylor & Francis
Deposits of amyloid fibrils characterize a diverse group of human diseases that includes
Alzheimer's disease, Creutzfeldt-Jakob disease and type II diabetes. Amyloid fibrils formed …
Alzheimer's disease, Creutzfeldt-Jakob disease and type II diabetes. Amyloid fibrils formed …
Polyferrocenylsilane block copolymer spherulites in dilute solution
Self-assembly of block copolymers (BCP) into uniform 3D structures in solution is an
extremely rare phenomenon. Furthermore, the investigation of general prerequisites for …
extremely rare phenomenon. Furthermore, the investigation of general prerequisites for …
Nanomaterials: amyloids reflect their brighter side
Amyloid fibrils belong to the group of ordered nanostructures that are self-assembled from a
wide range of polypeptides/proteins. Amyloids are highly rigid structures possessing a high …
wide range of polypeptides/proteins. Amyloids are highly rigid structures possessing a high …