The Hsp110 Molecular Chaperone Stabilizes Apolipoprotein B from Endoplasmic Reticulum-associated Degradation (ERAD)

Eitemau Tebyg

• Chaperoning Endoplasmic Reticulum–Associated Degradation (ERAD) and Protein Conformational Diseases
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  Cyhoeddwyd: (2019)
• Molecular chaperones and substrate ubiquitination control the efficiency of endoplasmic reticulum-associated degradation
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  Cyhoeddwyd: (2010)
• The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulum-associated degradation)
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  Cyhoeddwyd: (2007)
• Protein disulfide isomerases contribute differentially to the endoplasmic reticulum–associated degradation of apolipoprotein B and other substrates
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  Cyhoeddwyd: (2012)
• Hsp70 Molecular Chaperone Facilitates Endoplasmic Reticulum-associated Protein Degradation of Cystic Fibrosis Transmembrane Conductance Regulator in Yeast
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  Cyhoeddwyd: (2001)