SFTPCmutations cause SP-C degradation and aggregate formation without increasing ER stress-Reference-Cited by-同舟云学术

SFTPCmutations cause SP-C degradation and aggregate formation without increasing ER stress

Published:2013-05-24 Issue:8 Volume:43 Page:791-800
ISSN:0014-2972
Container-title:European Journal of Clinical Investigation
language:en
Short-container-title:Eur J Clin Invest

Author:

Thurm Tobias¹,Kaltenborn Eva¹,Kern Sunčana¹,Griese Matthias¹,Zarbock Ralf¹

Affiliation:

1. Dr. von Hauner Children's Hospital; Ludwig-Maximilians-University; Munich; Germany

Publisher

Wiley

Subject

Clinical Biochemistry,Biochemistry,General Medicine

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/eci.12107/fullpdf

Reference40 articles.

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3. Pulmonary type II cell lamellar body ultrastructure preserved by rapid freezing and freeze drying;McAteer;Anat Rec,1984

4. Localization, synthesis, and processing of surfactant protein SP-C in rat lung analyzed by epitope-specific antipeptide antibodies;Beers;J Biol Chem,1994

5. Proteomic analysis of lamellar bodies isolated from rat lungs;Wang;BMC Cell Biol,2008

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