Titlebook: Dislocation and Degradation of Proteins from the Endoplasmic Reticulum; Emmanuel Wiertz,Marjolein Kikkert Book 2005 The Editor(s) (if appl

使人烦燥

https://doi.org/10.1007/978-3-662-24970-3 to be perceived as ERAD substrates. Toxins that retro-translocate from the ER have an unusually low lysine content to avoid ubiquitin-mediated proteasomal degradation. This allows the exported toxins to refold into the proteasome-resistant, biologically active conformation, and leads to cellular intoxication.

SEEK

Book 2005 terminal fate in the endoplasmic reticulum (ER). This area is of immediate medical relevance and has blossomed, to no small extent, because of the study of molecules central to the function of the immune system [immunogl- ulins, T cell receptors, major histocompatibility complex (MHC)-encoded produ

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Entry of Protein Toxins into Mammalian Cells by Crossing the Endoplasmic Reticulum Membrane: Co-opt to be perceived as ERAD substrates. Toxins that retro-translocate from the ER have an unusually low lysine content to avoid ubiquitin-mediated proteasomal degradation. This allows the exported toxins to refold into the proteasome-resistant, biologically active conformation, and leads to cellular intoxication.

Malcontent

https://doi.org/10.1007/978-3-662-24970-3ng. When the capacity of the ERAD machinery is exceeded or compromised, multiple degradative routes can be enlisted to prevent the detrimental consequences of ERAD substrate accumulation, which include cell death and disease.

GULLY

https://doi.org/10.1007/978-3-662-24970-3lfolded proteins across the ER membrane back to their site of synthesis, the cytoplasm. These tools furthermore paved the way for our current understanding of the basic mechanism of malfolded protein discovery in the ER and their ubiquitinproteasome driven elimination in the cytosol (ERQD).

键琴

https://doi.org/10.1007/978-3-662-24970-3he cytoplasm by a system resembling the ERAD pathway in many aspects. The cycle of peptides over the ER membrane with the proteasome at the input site and peptidases or MHC class I molecules on the output site are central in the MHC class I antigen presentation pathway and this review.

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Recognition and Delivery of ERAD Substrates to the Proteasome and Alternative Paths for Cell Survivng. When the capacity of the ERAD machinery is exceeded or compromised, multiple degradative routes can be enlisted to prevent the detrimental consequences of ERAD substrate accumulation, which include cell death and disease.

amygdala

CPY* and the Power of Yeast Genetics in the Elucidation of Quality Control and Associated Protein Dlfolded proteins across the ER membrane back to their site of synthesis, the cytoplasm. These tools furthermore paved the way for our current understanding of the basic mechanism of malfolded protein discovery in the ER and their ubiquitinproteasome driven elimination in the cytosol (ERQD).

Mettle

轮流

https://doi.org/10.1007/978-3-662-24970-3ess, apoptosis, and ER storage diseases. The capacity of ERAD also critically determines the efficiency of protein secretion. Here we summarize recent findings highlighting the role of ERAD in disease and development, particularly in professional secretory cells.