Publications related to Transthyretin

Novel Mechanistic Insight into the Molecular Basis of Amyloid Polymorphism and Secondary Nucleation during Amyloid Formation

Giovanni Dietler, Hilal Lashuel, Annalisa Ansaloni, Jae Sun Jeong, Raffaele Mezzenga

The formation of amyloid β (Aβ) fibrils is crucial in initiating the cascade of pathological events that culminates in Alzheimer's disease. In this study, we investigated the mechanism of Aβ fibril formation from hydrodynamically well defined species under ...

Academic Press Ltd- Elsevier Science Ltd2013

The Role of γ-Secretase Activating Protein (GSAP) and Imatinib in the Regulation of γ-Secretase Activity and Amyloid-β Generation

Valérie Eligert, Patrick Fraering, Mitko Dimitrov

gamma-Secretase is a large enzyme complex comprising presenilin, nicastrin, presenilin enhancer 2, and anterior pharynx-defective 1 that mediates the intramembrane proteolysis of a large number of proteins including amyloid precursor protein and Notch. Rec ...

2013

Chemical strategies for controlling protein folding and elucidating the molecular mechanisms of amyloid formation and toxicity

Hilal Lashuel, Bruno Claude Daniel Fauvet, Loay Awad, Mirva Hejjaoui

It has been more than a century since the first evidence linking the process of amyloid formation to the pathogenesis of Alzheimer's disease. During the last three decades in particular, increasing evidence from various sources (pathology, genetics, cell c ...

Elsevier2012

Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species

Hilal Lashuel, Igor Allaman, Mohammad Asad Jan Qureshi

The identification of toxic Aβ species and/or the process of their formation is crucial for understanding the mechanism(s) of Aβ neurotoxicity in Alzheimer disease and also for the development of effective diagnostic and therapeutic interventions. To eluci ...

2011

Understanding amyloid aggregation by statistical analysis of atomic force microscopy images

Giovanni Dietler, Paolo De Los Rios, Jérôme Flakowski, Raffaele Mezzenga

The aggregation of proteins is central to many aspects of daily life, including food processing, blood coagulation, eye cataract formation disease and prion-related neurodegenerative infections[1–5]. However, the physical mechanisms responsible for amyloid ...

Nature Publishing Group2010

1) Trace copper(II) or zinc(II) ions drastically modify the aggregation behaviour of Aβ1–42: an AFM study

Angela Casini, Andrea Innocenti Malini

Formation of amyloid-beta (A beta)(1-42) amyloid fibrils, a characteristic feature of Alzheimer's disease (AD), was monitored in situ through atomic force microscopy (AFM). Well-structured amyloid fibrils slowly formed in solution within 24 hours for which ...

2010

The anti-Parkinsonian drug selegiline delays the nucleation phase of α-synuclein aggregation leading to the formation of nontoxic species

Hilal Lashuel, Saviana Di Giovanni

Parkinson's disease (PD) is a movement disorder characterized by the loss of dopaminergic neurons in the substantia nigra and the formation of intraneuronal inclusions called Lewy bodies, which are composed mainly of α-synuclein (α-syn). Selegiline (Sel) i ...

2010

Formation and maintenance of Alzheimer's disease beta-amyloid plaques in the absence of microglia

Tristan Bolmont

In Alzheimer's disease, microglia cluster around beta-amyloid deposits, suggesting that these cells are important for amyloid plaque formation, maintenance and/or clearance. We crossed two distinct APP transgenic mouse strains with CD11b-HSVTK mice, in whi ...

Nature Publishing Group2009

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Transthyretin

Novel Mechanistic Insight into the Molecular Basis of Amyloid Polymorphism and Secondary Nucleation during Amyloid Formation

The Role of γ-Secretase Activating Protein (GSAP) and Imatinib in the Regulation of γ-Secretase Activity and Amyloid-β Generation

Chemical strategies for controlling protein folding and elucidating the molecular mechanisms of amyloid formation and toxicity

Investigation of Biophysical Properties of Biomolecules by Means of Atomic Force Microscopy

Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species

The Gamma-Secretase-Mediated Proteolytic Processing of APP C-Terminal Fragments as a Therapeutic Target for Alzheimer's Disease

Understanding amyloid aggregation by statistical analysis of atomic force microscopy images

1) Trace copper(II) or zinc(II) ions drastically modify the aggregation behaviour of Aβ1–42: an AFM study

The anti-Parkinsonian drug selegiline delays the nucleation phase of α-synuclein aggregation leading to the formation of nontoxic species

Formation and maintenance of Alzheimer's disease beta-amyloid plaques in the absence of microglia

Graph Chatbot

Chat with Graph Search

Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species

Formation and maintenance of Alzheimer's disease beta-amyloid plaques in the absence of microglia

Chemical strategies for controlling protein folding and elucidating the molecular mechanisms of amyloid formation and toxicity

The Role of γ-Secretase Activating Protein (GSAP) and Imatinib in the Regulation of γ-Secretase Activity and Amyloid-β Generation

Investigation of Biophysical Properties of Biomolecules by Means of Atomic Force Microscopy

Understanding amyloid aggregation by statistical analysis of atomic force microscopy images

The Gamma-Secretase-Mediated Proteolytic Processing of APP C-Terminal Fragments as a Therapeutic Target for Alzheimer's Disease

The anti-Parkinsonian drug selegiline delays the nucleation phase of α-synuclein aggregation leading to the formation of nontoxic species

1) Trace copper(II) or zinc(II) ions drastically modify the aggregation behaviour of Aβ1–42: an AFM study

Novel Mechanistic Insight into the Molecular Basis of Amyloid Polymorphism and Secondary Nucleation during Amyloid Formation