Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway
Published 2016 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway
Authors
Keywords
-
Journal
Scientific Reports
Volume 6, Issue 1, Pages -
Publisher
Springer Nature
Online
2016-02-09
DOI
10.1038/srep20261
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- The ER-Associated Degradation Adaptor Protein Sel1L Regulates LPL Secretion and Lipid Metabolism
- (2014) Haibo Sha et al. Cell Metabolism
- Sel1L is indispensable for mammalian endoplasmic reticulum-associated degradation, endoplasmic reticulum homeostasis, and survival
- (2014) Shengyi Sun et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Crystallization and preliminary X-ray diffraction analysis of the Sel1-like repeats of SEL1L
- (2014) Hanbin Jeong et al. Acta Crystallographica Section F-Structural Biology Communications
- Role of HERP and a HERP-related Protein in HRD1-dependent Protein Degradation at the Endoplasmic Reticulum
- (2013) Chih-Hsiang Huang et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- The Four Canonical TPR Subunits of Human APC/C Form Related Homo-Dimeric Structures and Stack in Parallel to Form a TPR Suprahelix
- (2013) Ziguo Zhang et al. JOURNAL OF MOLECULAR BIOLOGY
- Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane
- (2013) Martin Mehnert et al. NATURE CELL BIOLOGY
- Cleaning Up: ER-Associated Degradation to the Rescue
- (2012) Jeffrey L. Brodsky CELL
- Structural and Biochemical Basis of Yos9 Protein Dimerization and Possible Contribution to Self-association of 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase Degradation Ubiquitin-Ligase Complex
- (2012) Jennifer Hanna et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- 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
- Defining human ERAD networks through an integrative mapping strategy
- (2011) John C. Christianson et al. NATURE CELL BIOLOGY
- Road to Ruin: Targeting Proteins for Degradation in the Endoplasmic Reticulum
- (2011) M. H. Smith et al. SCIENCE
- Features and development ofCoot
- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- PHENIX: a comprehensive Python-based system for macromolecular structure solution
- (2010) Paul D. Adams et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Retrotranslocation of a Misfolded Luminal ER Protein by the Ubiquitin-Ligase Hrd1p
- (2010) Pedro Carvalho et al. CELL
- Herp Regulates Hrd1-mediated Ubiquitylation in a Ubiquitin-like Domain-dependent Manner
- (2010) Melanie Kny et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LSsubstrates
- (2010) Riccardo Bernasconi et al. JOURNAL OF CELL BIOLOGY
- Design, function and structure of a monomeric ClC transporter
- (2010) Janice L. Robertson et al. NATURE
- The E3 Ubiquitin Ligases Hrd1 and gp78 Bind to and Promote Cholera Toxin Retro-Translocation
- (2009) Kaleena M. Bernardi et al. MOLECULAR BIOLOGY OF THE CELL
- Usa1 Functions as a Scaffold of the HRD-Ubiquitin Ligase
- (2009) Sabine C. Horn et al. MOLECULAR CELL
- The ubiquitylation machinery of the endoplasmic reticulum
- (2009) Christian Hirsch et al. NATURE
- 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
Create your own webinar
Interested in hosting your own webinar? Check the schedule and propose your idea to the Peeref Content Team.
Create NowAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started