In vivo regulation of the A disintegrin and metalloproteinase 10 (ADAM10) by the tetraspanin 15-Reference-Cited by-同舟云学术

In vivo regulation of the A disintegrin and metalloproteinase 10 (ADAM10) by the tetraspanin 15

Published:2018-03-08 Issue:17 Volume:75 Page:3251-3267
ISSN:1420-682X
Container-title:Cellular and Molecular Life Sciences
language:en
Short-container-title:Cell. Mol. Life Sci.

Author:

Seipold Lisa,Altmeppen Hermann,Koudelka Tomas,Tholey Andreas,Kasparek Petr,Sedlacek Radislav,Schweizer Michaela,Bär Julia,Mikhaylova Marina,Glatzel Markus,Saftig Paul

Funder

Deutsche Forschungsgemeinschaft

Ministry of Education, Youth and Sports

Academy of Sciences of the Czech Republic

Deutsche Forschungsgemeinschaft Emmy-Noether-Programm

Creutzfeldt-Jakob Disease Foundation, Inc.

Werner-Otto-Stiftung

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Cellular and Molecular Neuroscience,Pharmacology,Molecular Biology,Molecular Medicine

Link

http://link.springer.com/article/10.1007/s00018-018-2791-2/fulltext.html

Reference50 articles.

1. Saftig P, Lichtenthaler SF (2015) The alpha secretase ADAM10: a metalloprotease with multiple functions in the brain. Prog Neurobiol 135:1–20

2. Howard L, Lu X, Mitchell S, Griffiths S, Glynn P (1996) Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types. Biochem J 317(Pt 1):45–50

3. Karkkainen I, Rybnikova E, Pelto-Huikko M, Huovila AP (2000) Metalloprotease-disintegrin (ADAM) genes are widely and differentially expressed in the adult CNS. Mol Cell Neurosci 15:547–560

4. Marcinkiewicz M, Seidah NG (2000) Coordinated expression of beta-amyloid precursor protein and the putative beta-secretase BACE and alpha-secretase ADAM10 in mouse and human brain. J Neurochem 75:2133–2143

5. Anders A, Gilbert S, Garten W, Postina R, Fahrenholz F (2001) Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases. FASEB J 15:1837–1839

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