標(biāo)題: Titlebook: Dislocation and Degradation of Proteins from the Endoplasmic Reticulum; Emmanuel Wiertz,Marjolein Kikkert Book 2005 The Editor(s) (if appl [打印本頁] 作者: Iodine 時間: 2025-3-21 19:07
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書目名稱Dislocation and Degradation of Proteins from the Endoplasmic Reticulum影響因子(影響力)學(xué)科排名
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書目名稱Dislocation and Degradation of Proteins from the Endoplasmic Reticulum讀者反饋
書目名稱Dislocation and Degradation of Proteins from the Endoplasmic Reticulum讀者反饋學(xué)科排名
作者: 畏縮 時間: 2025-3-21 21:11
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.作者: 分發(fā) 時間: 2025-3-22 00:42
Dislocation and Degradation of Proteins from the Endoplasmic Reticulum作者: Offstage 時間: 2025-3-22 08:38 作者: 債務(wù) 時間: 2025-3-22 09:50
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 作者: 結(jié)果 時間: 2025-3-22 15:55 作者: 結(jié)果 時間: 2025-3-22 18:45 作者: hysterectomy 時間: 2025-3-22 22:47 作者: 無可爭辯 時間: 2025-3-23 01:37
978-3-642-42177-8The Editor(s) (if applicable) and The Author(s), under exclusive license to Springer-Verlag GmbH, DE作者: Systemic 時間: 2025-3-23 07:39
Dislocation and Degradation of Proteins from the Endoplasmic Reticulum978-3-540-28007-1Series ISSN 0070-217X Series E-ISSN 2196-9965 作者: Lyme-disease 時間: 2025-3-23 12:53 作者: Enliven 時間: 2025-3-23 14:29
https://doi.org/10.1007/978-3-662-24970-3isfolding in the secretory pathway. Molecular chaperones and ER lumenal lectins are essential components of this process because they maintain the solubility of unfolded proteins and can target ERAD substrates to the cytoplasmic proteasome. Other factors are likely required to aid in the selection o作者: 拖網(wǎng) 時間: 2025-3-23 20:33 作者: Morsel 時間: 2025-3-24 01:45
https://doi.org/10.1007/978-3-662-24970-3own at present. This review provides an overview of ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s) with a role in the degradation of ER proteins. Their structure and functions are described, as well as their mutual interactions. Substrate specificity and functional redundancy of E3 作者: lesion 時間: 2025-3-24 02:24 作者: bromide 時間: 2025-3-24 06:51
https://doi.org/10.1007/978-3-662-24970-3mical processes involving biosynthesis, degradation, translocation, intracellular transport, diffusion, and many more. Critical intermediates and end products of this cascade of events are peptides. The peptides are generated by the proteasome, degraded by peptidases unless transported into the ER w作者: 不可救藥 時間: 2025-3-24 14:24 作者: 聚集 時間: 2025-3-24 17:42 作者: 制定 時間: 2025-3-24 22:40 作者: Occupation 時間: 2025-3-25 00:18
The Role of the Ubiquitination Machinery in Dislocation and Degradation of Endoplasmic Reticulum PrER proteins. Their structure and functions are described, as well as their mutual interactions. Substrate specificity and functional redundancy of E3 ligases are discussed, and other components of the ER degradation machinery that may associate with the ubiquitination system are reviewed.作者: 使人煩燥 時間: 2025-3-25 06:17
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.作者: SEEK 時間: 2025-3-25 09:40
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作者: flavonoids 時間: 2025-3-25 15:13
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.作者: Malcontent 時間: 2025-3-25 16:48
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.作者: GULLY 時間: 2025-3-25 20:20
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).作者: 鍵琴 時間: 2025-3-26 00:13
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.作者: Circumscribe 時間: 2025-3-26 05:22
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.作者: amygdala 時間: 2025-3-26 11:55
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).作者: Mettle 時間: 2025-3-26 12:48 作者: 輪流 時間: 2025-3-26 17:25
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.作者: 全部 時間: 2025-3-27 01:01 作者: 出處 時間: 2025-3-27 01:41 作者: N防腐劑 時間: 2025-3-27 08:37 作者: Congruous 時間: 2025-3-27 09:47
CPY* and the Power of Yeast Genetics in the Elucidation of Quality Control and Associated Protein Ds the vacuole, the destination of its wild type counterpart. Its creation, through mutation, had a major impact on the elucidation of the mechanisms of quality control and associated protein degradation of the endoplasmic reticulum, the eukaryotic organelle, where secretory proteins start the passag作者: LANCE 時間: 2025-3-27 16:47
The Role of the Ubiquitination Machinery in Dislocation and Degradation of Endoplasmic Reticulum Prown at present. This review provides an overview of ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s) with a role in the degradation of ER proteins. Their structure and functions are described, as well as their mutual interactions. Substrate specificity and functional redundancy of E3 作者: 無關(guān)緊要 時間: 2025-3-27 19:47 作者: 項目 時間: 2025-3-28 00:25
The Ins and Outs of Intracellular Peptides and Antigen Presentation by MHC Class I Molecules,mical processes involving biosynthesis, degradation, translocation, intracellular transport, diffusion, and many more. Critical intermediates and end products of this cascade of events are peptides. The peptides are generated by the proteasome, degraded by peptidases unless transported into the ER w作者: exophthalmos 時間: 2025-3-28 02:48 作者: 暴行 時間: 2025-3-28 08:33
10樓作者: 同來核對 時間: 2025-3-28 12:06
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