The glycan-dependent ERAD machinery degrades topologically diverse misfolded proteins-Reference-Cited by-同舟云学术

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The glycan-dependent ERAD machinery degrades topologically diverse misfolded proteins

Published:2018-03-14 Issue:2 Volume:94 Page:246-259
ISSN:0960-7412
Container-title:The Plant Journal
language:en
Short-container-title:Plant J

Author:

Shin Yun-Ji¹,Vavra Ulrike¹,Veit Christiane¹,Strasser Richard¹^ORCID

Affiliation:

1. Department of Applied Genetics and Cell Biology; University of Natural Resources and Life Sciences; Muthgasse 18 Vienna A-1190 Austria

Funder

Austrian Science Fund

Publisher

Wiley

Subject

Cell Biology,Plant Science,Genetics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/tpj.13851/fullpdf

Reference64 articles.

1. Secretory pathway quality control operating in Golgi, plasmalemmal, and endosomal systems;Arvan;Traffic,2002

2. In vivo aspects of protein folding and quality control;Balchin;Science,2016

3. Autoubiquitination of the Hrd1 ligase triggers protein retrotranslocation in ERAD;Baldridge;Cell,2016

4. Delivery of a secreted soluble protein to the vacuole via a membrane anchor;Barrieu;Plant Physiol.,1999

5. Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates;Bernasconi;J. Cell Biol.,2010

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2. Hexosamine biosynthesis and related pathways, protein N-glycosylation and O-GlcNAcylation: their interconnection and role in plants;Frontiers in Plant Science;2024-03-06

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