Liisa Lutter
YOU?
Author Swipe
View article: Structural reconstruction of individual filaments in Aβ42 fibril populations assembled in vitro reveal rare species that resemble ex vivo amyloid polymorphs from human brains
Structural reconstruction of individual filaments in Aβ42 fibril populations assembled in vitro reveal rare species that resemble ex vivo amyloid polymorphs from human brains Open
View article: How short peptides disassemble tau fibrils in Alzheimer’s disease
How short peptides disassemble tau fibrils in Alzheimer’s disease Open
View article: Three-dimensional single-particle reconstruction by atomic force microscopy allows rapid structural-based validation of recombinant SARS-CoV-2 Spike protein from a single topology image
Three-dimensional single-particle reconstruction by atomic force microscopy allows rapid structural-based validation of recombinant SARS-CoV-2 Spike protein from a single topology image Open
Atomic force microscopy (AFM) is a versatile multi-modal imaging method frequently used for structural characterisation of biological surfaces at the nanoscale. However, AFM-based three-dimensional single-particle reconstruction has hither…
View article: The architecture of amyloid fibrils formed by a human tau-derived hexapeptide VQIVYK
The architecture of amyloid fibrils formed by a human tau-derived hexapeptide VQIVYK Open
The sequence VQIVYK is an aggregation prone region of the tau protein implicated in driving assembly of tau into paired helical filaments. These filaments accumulate as intraneuronal neurofibrillary tangles in Alzheimers disease and a rang…
View article: How short peptides can disassemble ultra‐stable tau fibrils extracted from Alzheimer’s disease brain by a strain‐relief mechanism
How short peptides can disassemble ultra‐stable tau fibrils extracted from Alzheimer’s disease brain by a strain‐relief mechanism Open
Background Reducing fibrous aggregates of protein tau is a possible strategy for halting progression of Alzheimer’s disease (AD). Previously we found that in vitro the D‐peptide D‐TLKIVWC fragments tau fibrils from AD brains (AD‐tau) into …
View article: How short peptides can disassemble ultra-stable tau fibrils extracted from Alzheimer’s disease brain by a strain-relief mechanism
How short peptides can disassemble ultra-stable tau fibrils extracted from Alzheimer’s disease brain by a strain-relief mechanism Open
View article: How short peptides can disassemble ultra-stable tau fibrils extracted from Alzheimer’s disease brain by a strain-relief mechanism
How short peptides can disassemble ultra-stable tau fibrils extracted from Alzheimer’s disease brain by a strain-relief mechanism Open
Reducing fibrous aggregates of protein tau is a possible strategy for halting progression of Alzheimer’s disease (AD). Previously we found that in vitro the D-peptide D-TLKIVWC disassembles tau fibrils from AD brains (AD-tau) into benign s…
View article: Structural reconstruction of individual filaments in Aβ42 fibril populations assembled<i>in vitro</i>reveal rare species that resemble<i>ex vivo</i>amyloid polymorphs from human brains
Structural reconstruction of individual filaments in Aβ42 fibril populations assembled<i>in vitro</i>reveal rare species that resemble<i>ex vivo</i>amyloid polymorphs from human brains Open
Structural polymorphism has been demonstrated for both in vitro and ex vivo amyloid fibrils associated with disease. The manner in which different filament structures are assembled from common building blocks remains unclear but the assemb…
View article: Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils
Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils Open
The self-assembly of the Nucleocapsid protein (NCAP) of SARS-CoV-2 is crucial for its function. Computational analysis of the amino acid sequence of NCAP reveals low-complexity domains (LCDs) akin to LCDs in other proteins known to self-as…
View article: Structural Identification of Individual Helical Amyloid Filaments by Integration of Cryo-Electron Microscopy-Derived Maps in Comparative Morphometric Atomic Force Microscopy Image Analysis
Structural Identification of Individual Helical Amyloid Filaments by Integration of Cryo-Electron Microscopy-Derived Maps in Comparative Morphometric Atomic Force Microscopy Image Analysis Open
View article: Structural identification of individual helical amyloid filaments by integration of cryo-electron microscopy-derived maps in comparative morphometric atomic force microscopy image analysis
Structural identification of individual helical amyloid filaments by integration of cryo-electron microscopy-derived maps in comparative morphometric atomic force microscopy image analysis Open
The presence of amyloid fibrils is a hallmark of more than 50 human disorders, including neurodegenerative diseases and systemic amyloidoses. A key unresolved challenge in understanding the involvement of amyloid in disease is to explain t…
View article: Quantification of amyloid fibril polymorphism by nano-morphometry reveals the individuality of filament assembly
Quantification of amyloid fibril polymorphism by nano-morphometry reveals the individuality of filament assembly Open
View article: Three-dimensional reconstruction of individual helical nano-filament structures from atomic force microscopy topographs
Three-dimensional reconstruction of individual helical nano-filament structures from atomic force microscopy topographs Open
Atomic force microscopy, AFM, is a powerful tool that can produce detailed topographical images of individual nano-structures with a high signal-to-noise ratio without the need for ensemble averaging. However, the application of AFM in str…
View article: Quantification of amyloid fibril polymorphism by nano-morphometry reveals the individuality of filament assembly
Quantification of amyloid fibril polymorphism by nano-morphometry reveals the individuality of filament assembly Open
Amyloid fibrils are highly polymorphic structures formed by many different proteins. They provide biological function but also abnormally accumulate in numerous human diseases. The physicochemical principles of amyloid polymorphism are not…
View article: Three-dimensional reconstruction of individual helical nano-filament structures from atomic force microscopy topographs
Three-dimensional reconstruction of individual helical nano-filament structures from atomic force microscopy topographs Open
Atomic force microscopy, AFM, is a powerful tool that can produce detailed topographical images of individual nano-structures with a high signal-to-noise ratio without the need for ensemble averaging. However, the application of AFM in str…
View article: Tau (297‐391) forms filaments that structurally mimic the core of paired helical filaments in Alzheimer’s disease brain
Tau (297‐391) forms filaments that structurally mimic the core of paired helical filaments in Alzheimer’s disease brain Open
The constituent paired helical filaments (PHFs) in neurofibrillary tangles are insoluble intracellular deposits central to the development of Alzheimer’s disease (AD) and other tauopathies. Full‐length tau requires the addition of anionic …