Publications related to Neurodegenerative disease

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

Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of alpha-synuclein and beta-amyloid and protect against amyloid-induced toxicity

Hilal Lashuel, Pierre-Alain Carrupt, Magdalena Zweckstetter, Saviana Di Giovanni, Simona Eleuteri

Parkinson disease (PD) is the second most common neurodegenerative disorder after Alzheimer disease (AD). There is considerable consensus that the increased production and/or aggregation of alpha-synuclein (alpha-syn) plays a central role in the pathogenes ...

American Society for Biochemistry and Molecular Biology2010

Beta amyloid and hyperphosphorylated tau deposits in the pancreas in type 2 diabetes

László Forró, Aleksandra Radenovic, Andras Kis

Strong epidemiologic evidence suggests an association between Alzheimer disease (AD) and type 2 diabetes. To determine if amyloid beta (A

\beta

) and hyperphosphorylated tau occurs in type 2 diabetes, pancreas tissues from 21 autopsy cases (10 type 2 diabe ...

Elsevier2010

Fibrillar vs Crystalline Full-Length beta-2-Microglobulin Studied by High-Resolution Solid-State NMR Spectroscopy

David Lyndon Emsley

Elucidating the fine structure of amyloid fibrils as well as understanding their processes of nucleation and growth remains a difficult yet essential challenge, directly linked to our current poor insight into protein misfolding and aggregation diseases. H ...

AMER CHEMICAL SOC2010

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

Phosphorylation of synucleins by members of the Polo-like kinase family

Hilal Lashuel, Harald Hirling, Magdalena Zweckstetter, Abid Oueslati, Martial Mbefo Kamdem

Phosphorylation of alpha-synuclein (alpha-syn) at Ser-129 is a hallmark of Parkinson disease and related synucleinopathies. However, the identity of the natural kinases and phosphatases responsible for regulating alpha-syn phosphorylation remain unknown. H ...

American Society for Biochemistry and Molecular Biology2010

Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson's disease pathogenesis and therapies

Hilal Lashuel, Abid Oueslati

A better understanding of the molecular and cellular determinants that influence the pathology of Parkinson's disease (PD) is essential for developing effective diagnostic, preventative and therapeutic strategies to treat this devastating disease. A number ...

Elsevier2010

Amyloidogenic protein-membrane interactions: mechanistic insight from model systems

Hilal Lashuel

The toxicity of amyloid-forming proteins is correlated with their interactions with cell membranes. Binding events between amyloidogenic proteins and membranes result in mutually disruptive structural perturbations, which are associated with toxicity. Memb ...

2010

Novel gamma-secretase inhibitors uncover a common nucleotide-binding site in JAK3, SIRT2, and PS1

Patrick Fraering, Nikita Rudinskiy, Claude André Schweizer

Gamma-secretase is an intramembrane-cleaving protease responsible for the final proteolytic event in the production of the amyloid-beta peptides (Abeta) implicated in Alzheimer's disease (AD). Inhibition of gamma-secretase activity is thus an attractive th ...

2010

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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

Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of alpha-synuclein and beta-amyloid and protect against amyloid-induced toxicity

Beta amyloid and hyperphosphorylated tau deposits in the pancreas in type 2 diabetes

Fibrillar vs Crystalline Full-Length beta-2-Microglobulin Studied by High-Resolution Solid-State NMR Spectroscopy

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

Phosphorylation of synucleins by members of the Polo-like kinase family

Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson's disease pathogenesis and therapies

Amyloidogenic protein-membrane interactions: mechanistic insight from model systems

Novel gamma-secretase inhibitors uncover a common nucleotide-binding site in JAK3, SIRT2, and PS1

Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of alpha-synuclein and beta-amyloid and protect against amyloid-induced toxicity

Beta amyloid and hyperphosphorylated tau deposits in the pancreas in type 2 diabetes

Understanding amyloid aggregation by statistical analysis of atomic force microscopy images

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

Fibrillar vs Crystalline Full-Length beta-2-Microglobulin Studied by High-Resolution Solid-State NMR Spectroscopy

Novel gamma-secretase inhibitors uncover a common nucleotide-binding site in JAK3, SIRT2, and PS1

Amyloidogenic protein-membrane interactions: mechanistic insight from model systems

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

Phosphorylation of synucleins by members of the Polo-like kinase family

Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson's disease pathogenesis and therapies