Only amyloidogenic intermediates of transthyretin induce apoptosis (Q40727157)

23 September 2017

title

Only amyloidogenic intermediates of transthyretin induce apoptosis (English)

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23 September 2017

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Karin Andersson

1

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23 September 2017

Anders Olofsson

2

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23 September 2017

Ellen Holm Nielsen

3

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23 September 2017

Sven-Erik Svehag

4

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23 September 2017

Erik Lundgren

5

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23 September 2017

publication date

1 June 2002

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Biochemical and Biophysical Research Communications

23 September 2017

published in

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23 September 2017

volume

294

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23 September 2017

issue

2

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23 September 2017

page(s)

309-314

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Familial amyloidotic polyneuropathy

23 September 2017

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Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins

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

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Characterization of two highly amyloidogenic mutants of transthyretin

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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Vectors for selective expression of cloned DNAs by T7 RNA polymerase

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Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro

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The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid

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Examination of the Structure of the Transthyretin Amyloid Fibril by Image Reconstruction from Electron Micrographs

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Amyloid beta peptide induces necrosis rather than apoptosis

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The Aβ Peptide of Alzheimer's Disease Directly Produces Hydrogen Peroxide through Metal Ion Reduction†

7 January 2021

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Cu(II) potentiation of alzheimer abeta neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction.

7 January 2021

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7 January 2021

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Interaction of the receptor for advanced glycation end products (RAGE) with transthyretin triggers nuclear transcription factor kB (NF-kB) activation

7 January 2021

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7 January 2021

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inferred from DOI database lookup

7 January 2021

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Identifiers

DOI

10.1016/S0006-291X(02)00465-5

1 reference

23 September 2017

1 reference