Publications related to Synthesis, structure, and activity of diclofenac analogues as transthyretin amyloid fibril formation inhibitors

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

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

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

Switch-peptides: design and characterization of controllable super-amyloid-forming host-guest peptides as tools for identifying anti-amyloid agents

Hilal Lashuel, Adrian Schmid, Sonia Dos Santos, Marie-Stéphanie Camus

Several amyloid-forming proteins are characterized by the presence of hydrophobic and highly amyloidogenic core sequences that play critical roles in the initiation and progression of amyloid fibril formation. Therefore targeting these sequences represents ...

Wiley-Blackwell2008

Disruption of amyloid-derived peptide assemblies through the controlled induction of a beta-sheet to alpha-helix transformation: application of the switch concept

Hilal Lashuel, Adrian Schmid, Richard Alan Mimna, Marie-Stéphanie Camus

Reversal of amyloid formation through a controlled induced transformation from beta-sheet to sol. alpha-helix structures through the use of a switch element S could have an important consequences understanding the mechanisms of amyloid formation and cleara ...

2007

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Synthesis, structure, and activity of diclofenac analogues as transthyretin amyloid fibril formation inhibitors

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

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

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

Understanding amyloid aggregation by statistical analysis of atomic force microscopy images

Nucleation Dependent Polymerization of Amyloid-ß (Aß) as an Important Determinant of Aß Amyloid Formation and Neurotoxicity

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

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

Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Abeta fibrils and protofibrils

Switch-peptides: design and characterization of controllable super-amyloid-forming host-guest peptides as tools for identifying anti-amyloid agents

Disruption of amyloid-derived peptide assemblies through the controlled induction of a beta-sheet to alpha-helix transformation: application of the switch concept

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Chat with Graph Search

Nucleation Dependent Polymerization of Amyloid-ß (Aß) as an Important Determinant of Aß Amyloid Formation and Neurotoxicity

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

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

Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Abeta fibrils and protofibrils

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

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

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

Switch-peptides: design and characterization of controllable super-amyloid-forming host-guest peptides as tools for identifying anti-amyloid agents

Disruption of amyloid-derived peptide assemblies through the controlled induction of a beta-sheet to alpha-helix transformation: application of the switch concept