Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site-Reference-Cited by-同舟云学术

Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site

Published:2016-02-19 Issue:1 Volume:11 Page:
ISSN:1750-1326
Container-title:Molecular Neurodegeneration
language:en
Short-container-title:Mol Neurodegeneration

Author:

Schönherr Caroline,Bien Jessica,Isbert Simone,Wichert Rielana,Prox Johannes,Altmeppen Hermann,Kumar Sathish,Walter Jochen,Lichtenthaler Stefan F.,Weggen Sascha,Glatzel Markus,Becker-Pauly Christoph,Pietrzik Claus U.

Funder

Deutsche Forschungsgemeinschaft (DE)

Sonderforschungsbereich

Bundesministerium für Bildung und Forschung (DE)

Publisher

Springer Science and Business Media LLC

Subject

Cellular and Molecular Neuroscience,Clinical Neurology,Molecular Biology

Link

http://link.springer.com/content/pdf/10.1186/s13024-016-0084-5

Reference73 articles.

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2. Koo EH, Squazzo SL. Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J Biol Chem. 1994;269(26):17386–9.

3. Vassar R, Bennett BD, Babu-Khan S, Kahn S, Mendiaz EA, Denis P, et al. Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science. 1999;286(5440):735–41.

4. Golde TE, Estus S, Younkin LH, Selkoe DJ, Younkin SG. Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science. 1992;255(5045):728–30.

5. Haass C, Schlossmacher MG, Hung AY, Vigo-Pelfrey C, Mellon A, Ostaszewski BL, et al. Amyloid beta-peptide is produced by cultured cells during normal metabolism. Nature. 1992;359(6393):322–5. doi: 10.1038/359322a0 .

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