Association of the SEL1L protein transmembrane domain with HRD1 ubiquitin ligase regulates ERAD-L
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Title
Association of the SEL1L protein transmembrane domain with HRD1 ubiquitin ligase regulates ERAD-L
Authors
Keywords
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Journal
FEBS Journal
Volume 283, Issue 1, Pages 157-172
Publisher
Wiley
Online
2015-10-16
DOI
10.1111/febs.13564
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- (2012) Randolph Y Hampton et al. CURRENT OPINION IN CELL BIOLOGY
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- (2012) Daniel N. Hebert et al. TRENDS IN BIOCHEMICAL SCIENCES
- The Cdc48 machine in endoplasmic reticulum associated protein degradation
- (2011) Dieter H. Wolf et al. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
- Recognition of an ERAD-L substrate analyzed by site-specific in vivo photocrosslinking
- (2011) Ann Marie Stanley et al. FEBS LETTERS
- SEL1L Protein Critically Determines the Stability of the HRD1-SEL1L Endoplasmic Reticulum-associated Degradation (ERAD) Complex to Optimize the Degradation Kinetics of ERAD Substrates
- (2011) Yasutaka Iida et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Molecular chaperones in protein folding and proteostasis
- (2011) F. Ulrich Hartl et al. NATURE
- Road to Ruin: Targeting Proteins for Degradation in the Endoplasmic Reticulum
- (2011) M. H. Smith et al. SCIENCE
- Protein quality control in the ER: balancing the ubiquitin checkbook
- (2011) Jasper H.L. Claessen et al. TRENDS IN CELL BIOLOGY
- A Comprehensive Comparison of Transmembrane Domains Reveals Organelle-Specific Properties
- (2010) Hayley J. Sharpe et al. CELL
- Retrotranslocation of a Misfolded Luminal ER Protein by the Ubiquitin-Ligase Hrd1p
- (2010) Pedro Carvalho et al. CELL
- Quality and quantity control at the endoplasmic reticulum
- (2010) Ramanujan S Hegde et al. CURRENT OPINION IN CELL BIOLOGY
- Protein Quality Control in the Cytosol and the Endoplasmic Reticulum: Brothers in Arms
- (2010) Alexander Buchberger et al. MOLECULAR CELL
- ERAD substrate recognition in budding yeast
- (2010) Wei Xie et al. SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
- Sec61p is part of the endoplasmic reticulum-associated degradation machinery
- (2009) Antje Schäfer et al. EMBO JOURNAL
- N-glycan structures: recognition and processing in the ER
- (2009) Markus Aebi et al. TRENDS IN BIOCHEMICAL SCIENCES
- Human XTP3-B Forms an Endoplasmic Reticulum Quality Control Scaffold with the HRD1-SEL1L Ubiquitin Ligase Complex and BiP
- (2008) Nobuko Hosokawa et al. JOURNAL OF BIOLOGICAL CHEMISTRY
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- (2008) Monica Cattaneo et al. JOURNAL OF CELLULAR PHYSIOLOGY
- Gp78 Cooperates with RMA1 in Endoplasmic Reticulum-associated Degradation of CFTRΔF508
- (2008) Daisuke Morito et al. MOLECULAR BIOLOGY OF THE CELL
- OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1–SEL1L ubiquitin ligase complex for ERAD
- (2008) John C. Christianson et al. NATURE CELL BIOLOGY
- SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins
- (2008) B. Mueller et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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