Publications related to Switch peptides

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

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

Mohammad Asad Jan Qureshi

Aggregation and fibril formation of amyloid-β (Aβ) peptides play a pivotal role in the pathogenesis of Alzheimer's disease (AD). Aβ peptides, principally comprising of 40 or 42 amino acid residues (Aβ40 and Aβ42), are produced by proteolytic processing of ...

EPFL2010

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

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

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

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

Preparation and characterization of toxic Abeta aggregates for structural and functional studies in Alzheimer's disease research

Hilal Lashuel, Mohammad Asad Jan Qureshi

The amyloid cascade hypothesis, supported by strong evidence from genetics, pathology and studies using animal models, implicates amyloid-beta (Abeta) oligomerization and fibrillogenesis as central causative events in the pathogenesis of Alzheimer's diseas ...

Nature Publishing Group2010

Novel Pentameric Thiophene Derivatives for in Vitro and in Vivo Optical Imaging of a Plethora of Protein Aggregates in Cerebral Amyloidoses

Tristan Bolmont

Molecular probes for selective Identification of protein aggregates are important to advance our understanding of the molecular pathogenesis underlying cerebral amyloidoses. Here we report the chemical design of pentameric thiophene derivatives, denoted lu ...

American Chemical Society2009

Cryoelectron microscopy structure of purified gamma-secretase at 12 A resolution

Lorène Aeschbach, Patrick Fraering, Hua Li

Gamma-secretase, an integral membrane protein complex, catalyzes the intramembrane cleavage of the beta-amyloid precursor protein (APP) during the neuronal production of the amyloid beta-peptide. As such, the protease has emerged as a key target for develo ...

Elsevier2009

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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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

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

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

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

Preparation and characterization of toxic Abeta aggregates for structural and functional studies in Alzheimer's disease research

Novel Pentameric Thiophene Derivatives for in Vitro and in Vivo Optical Imaging of a Plethora of Protein Aggregates in Cerebral Amyloidoses

Cryoelectron microscopy structure of purified gamma-secretase at 12 A resolution

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

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

Novel Pentameric Thiophene Derivatives for in Vitro and in Vivo Optical Imaging of a Plethora of Protein Aggregates in Cerebral Amyloidoses

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

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

Preparation and characterization of toxic Abeta aggregates for structural and functional studies in Alzheimer's disease research

Cryoelectron microscopy structure of purified gamma-secretase at 12 A resolution

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

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