Molecular chaperones and substrate ubiquitination control the efficiency of endoplasmic reticulum-associated degradation.
Goeckeler
J L
JL
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA.
Brodsky
J L
JL
D000818:Animals; D004721:Endoplasmic Reticulum / Q000502:physiology*; D015966:Gene Expression Regulation, Fungal / Q000502:physiology; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology; D006801:Humans; D008954:Models, Biological; D018832:Molecular Chaperones / Q000096:biosynthesis / Q000235:genetics / Q000502:physiology*; D017510:Protein Folding; D012441:Saccharomyces cerevisiae / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D054875:Ubiquitination / Q000502:physiology*
D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins