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The amyloid hypothesis of Alzheimer's disease at 25 years
Despite continuing debate about the amyloid β‐protein (or Aβ hypothesis, new lines of
evidence from laboratories and clinics worldwide support the concept that an imbalance …
evidence from laboratories and clinics worldwide support the concept that an imbalance …
Molecular dynamics simulations and novel drug discovery
X Liu, D Shi, S Zhou, H Liu, H Liu… - Expert opinion on drug …, 2018 - Taylor & Francis
Introduction: Molecular dynamics (MD) simulations can provide not only plentiful dynamical
structural information on biomacromolecules but also a wealth of energetic information …
structural information on biomacromolecules but also a wealth of energetic information …
Cu and Zn coordination to amyloid peptides: From fascinating chemistry to debated pathological relevance
E Atrián-Blasco, P Gonzalez, A Santoro, B Alies… - Coordination chemistry …, 2018 - Elsevier
Several diseases share misfolding of different peptides and proteins as a key feature for
their development. This is the case of important neurodegenerative diseases such as …
their development. This is the case of important neurodegenerative diseases such as …
Alzheimer's disease: How metal ions define β-amyloid function
KP Kepp - Coordination Chemistry Reviews, 2017 - Elsevier
Alzheimer's disease is increasingly recognized to be linked to the function and status of
metal ions, and recently, the amyloid hypothesis has been strongly intertwined with the …
metal ions, and recently, the amyloid hypothesis has been strongly intertwined with the …
Pathways of amyloid-β aggregation depend on oligomer shape
One of the main research topics related to Alzheimer's disease is the aggregation of the
amyloid-β peptide, which was shown to follow different pathways for the two major alloforms …
amyloid-β peptide, which was shown to follow different pathways for the two major alloforms …
Spontaneous formation of β-sheet nano-barrels during the early aggregation of Alzheimer's amyloid beta
Soluble low-molecular-weight oligomers formed during the early aggregation of amyloid
peptides have been hypothesized as a major toxic species of amyloidogenesis. Herein, we …
peptides have been hypothesized as a major toxic species of amyloidogenesis. Herein, we …
Tetrameric Aβ40 and Aβ42 β-barrel structures by extensive atomistic simulations. II. In aqueous solution
PH Nguyen, JM Campanera, ST Ngo… - The Journal of …, 2019 - ACS Publications
Alzheimer's disease (AD) is characterized by the accumulation of extracellular Aβ42 and
Aβ40 oligomers and plaques. In a recent computational study, we found that the presence of …
Aβ40 oligomers and plaques. In a recent computational study, we found that the presence of …
Aβ propagation and strains: Implications for the phenotypic diversity in Alzheimer's disease
C Condello, J Stöehr - Neurobiology of disease, 2018 - Elsevier
The progressive nature of Alzheimer's disease (AD) is thought to occur, at least in part, by
the self-replication and spreading of Aβ and Tau aggregates through a prion mechanism …
the self-replication and spreading of Aβ and Tau aggregates through a prion mechanism …
Using mass spectrometry‐based methods to understand amyloid formation and inhibition of alpha‐synuclein and amyloid beta
WJ Wagner, ML Gross - Mass spectrometry reviews, 2024 - Wiley Online Library
Amyloid fibrils, insoluble β‐sheets structures that arise from protein misfolding, are
associated with several neurodegenerative disorders. Many small molecules have been …
associated with several neurodegenerative disorders. Many small molecules have been …
Molecular dynamics simulations reveal the mechanism of graphene oxide nanosheet inhibition of Aβ 1–42 peptide aggregation
The aggregation of the amyloid-beta (Aβ) peptides into toxic β-sheet-rich oligomers,
protofibrils and mature fibrils is the major pathological hallmark of Alzheimer's disease (AD) …
protofibrils and mature fibrils is the major pathological hallmark of Alzheimer's disease (AD) …