(Q24307407)

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alphaB-crystallin competes with Alzheimer's disease beta-amyloid peptide for peptide-peptide interactions and induces oxidation of Abeta-Met35

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alphaB-crystallin competes with Alzheimer's disease beta-amyloid peptide for peptide-peptide interactions and induces oxidation of Abeta-Met35 (English)

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Alzheimer's disease

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object named as

Bernd Reif

4

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author name string

Saravanakumar Narayanan

1

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Bram Kamps

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Wilbert C Boelens

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language of work or name

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publication date

30 October 2006

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580

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25

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5941-6

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The molecular chaperone alphaB-crystallin enhances amyloid beta neurotoxicity

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Folding proteins in fatal ways

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Neurodegenerative disease: amyloid pores from pathogenic mutations.

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Amyloid beta-peptide-associated free radical oxidative stress, neurotoxicity, and Alzheimer's disease

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Beta-amyloid peptides induce mitochondrial dysfunction and oxidative stress in astrocytes and death of neurons through activation of NADPH oxidase.

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Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta

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Interaction of intracellular beta amyloid peptide with chaperone proteins

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Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease

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Alpha B crystallin and HSP28 are enhanced in the cerebral cortex of patients with Alzheimer's disease.

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Cytosolic beta-amyloid deposition and supranuclear cataracts in lenses from people with Alzheimer's disease

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Alpha-B-crystallin in neuropathology

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Dementia with beta-amyloid deposition: involvement of alpha B-crystallin supports two main diseases.

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A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy

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Myofibrillar myopathy caused by novel dominant negative alpha B-crystallin mutations.

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Interaction between beta-amyloid and lens alphaB-crystallin.

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Importance of low-oligomeric-weight species for prion propagation in the yeast prion system Sup35/Hsp104.

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Characterization of chemical exchange between soluble and aggregated states of beta-amyloid by solution-state NMR upon variation of salt conditions.

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Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set

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Yeast prion-protein, sup35, fibril formation proceeds by addition and substraction of oligomers.

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Solution NMR studies of the A beta(1-40) and A beta(1-42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation

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1H NMR of A beta amyloid peptide congeners in water solution. Conformational changes correlate with plaque competence

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A molecular switch in amyloid assembly: Met35 and amyloid beta-protein oligomerization

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Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy

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Expression and aggregation of recombinant alpha A-crystallin and its two domains

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Small heat shock proteins inhibit in vitro A beta(1-42) amyloidogenesis

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Role of glycine-33 and methionine-35 in Alzheimer's amyloid beta-peptide 1-42-associated oxidative stress and neurotoxicity

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A novel NMR method for determining the interfaces of large protein-protein complexes

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Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons.

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inferred from DOI database lookup

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10.1016/J.FEBSLET.2006.09.063

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