A glycine zipper motif mediates the formation of toxic β-amyloid oligomers in vitro and in vivo

Aberrant Amyloid Precursor Protein (APP) Processing in Hereditary Forms of Alzheimer Disease Caused by APP Familial Alzheimer Disease Mutations Can Be Rescued by Mutations in the APP GxxxG Motif

(2010) Lisa-Marie Munter et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Alzheimer's Disease-Associated Amyloid β-Protein Is an Antimicrobial Peptide

(2010) Stephanie J. Soscia et al.   PLoS One

Role of Amyloid-  Glycine 33 in Oligomerization, Toxicity, and Neuronal Plasticity

(2009) A. Harmeier et al.   JOURNAL OF NEUROSCIENCE

The structure of a cytolytic α-helical toxin pore reveals its assembly mechanism

(2009) Marcus Mueller et al.   NATURE

A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides

(2009) A. Abedini et al.   PROTEIN ENGINEERING DESIGN & SELECTION

Destabilizing Protein Polymorphisms in the Genetic Background Direct Phenotypic Expression of Mutant SOD1 Toxicity

(2009) Tali Gidalevitz et al.   PLoS Genetics

Computationally Designed Peptide Inhibitors of Protein−Protein Interactions in Membranes†

(2008) Gregory A. Caputo et al.   BIOCHEMISTRY

Amyloid-  Peptide (A ) Neurotoxicity Is Modulated by the Rate of Peptide Aggregation: A  Dimers and Trimers Correlate with Neurotoxicity

(2008) L. W. Hung et al.   JOURNAL OF NEUROSCIENCE

The β amyloid peptide can act as a modular aggregation domain

(2008) Christopher D. Link et al.   NEUROBIOLOGY OF DISEASE

Structures of the glycine-rich diastereomeric peptides bombinin H2 and H4

(2008) Klaus Zangger et al.   TOXICON

Alzheimer's disease-type neuronal tau hyperphosphorylation induced by Aβ oligomers

(2007) Fernanda G. De Felice et al.   NEUROBIOLOGY OF AGING