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

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书目名称Dislocation and Degradation of Proteins from the Endoplasmic Reticulum
编辑Emmanuel Wiertz,Marjolein Kikkert
视频video
概述Includes supplementary material:
丛书名称Current Topics in Microbiology and Immunology
图书封面Titlebook: Dislocation and Degradation of Proteins from the Endoplasmic Reticulum;  Emmanuel Wiertz,Marjolein Kikkert Book 2005 The Editor(s) (if appl
描述The present volume of Current Topics in Microbiology and Immunology c- tains seven chapters that illuminate various aspects of a protein’s genesis and 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 products]. Similarly, the clever strategies used by bacteria or viruses to gain a foothold in the host and ensure their continued survival have uncovered altogether new cell biological principles. It is therefore ?tting that a special volume be devoted to the interplay between pathways of protein degradation in the ER and a wide variety of pathogens. The concept of quality control emerged with the appreciation that, in the case of multimeric glycoproteins, any unpaired glycoprotein subunit had great dif?culties leaving its site of synthesis—the ER—and was destroyed instead. Free immunoglobulin heavy chains were probably the earliest documented example of this kind, and were long known to cause pathology when their accumulation went unchecked. In
出版日期Book 2005
关键词Endoplasmatisches Reticulum; Viruses; bacteria; cell; cell biology; diseases; embryology; immunology; membra
版次1
doihttps://doi.org/10.1007/3-540-28007-3
isbn_softcover978-3-642-42177-8
isbn_ebook978-3-540-28007-1Series ISSN 0070-217X Series E-ISSN 2196-9965
issn_series 0070-217X
copyrightThe Editor(s) (if applicable) and The Author(s), under exclusive license to Springer-Verlag GmbH, DE
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The Role of p97/Cdc48p in Endoplasmic Reticulum-Associated Degradation: From the Immune System to Y substrates. Although p97/Cdc48p is not dedicated exclusively to ERAD, its ability to physically associate with ERAD substrates, with VIMP and with the E3 gp78 suggest that the p97/Cdc48. complex acts as a coordinator that maintains coupling between the different steps in ERAD.
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Dislocation and Degradation of Proteins from the Endoplasmic Reticulum
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0070-217X destroyed instead. Free immunoglobulin heavy chains were probably the earliest documented example of this kind, and were long known to cause pathology when their accumulation went unchecked. In978-3-642-42177-8978-3-540-28007-1Series ISSN 0070-217X Series E-ISSN 2196-9965
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978-3-642-42177-8The Editor(s) (if applicable) and The Author(s), under exclusive license to Springer-Verlag GmbH, DE
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Dislocation and Degradation of Proteins from the Endoplasmic Reticulum978-3-540-28007-1Series ISSN 0070-217X Series E-ISSN 2196-9965
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