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For: Molinari M. ER-phagy responses in yeast, plants, and mammalian cells and their crosstalk with UPR and ERAD. Dev Cell 2021;56:949-66. [PMID: 33765438 DOI: 10.1016/j.devcel.2021.03.005] [Cited by in Crossref: 4] [Cited by in F6Publishing: 5] [Article Influence: 4.0] [Reference Citation Analysis]
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7 Christianson JC, Carvalho P. Order through destruction: how ER-associated protein degradation contributes to organelle homeostasis. EMBO J 2022;:e109845. [PMID: 35170763 DOI: 10.15252/embj.2021109845] [Reference Citation Analysis]
8 Kang C, Avery L. The FMRFamide Neuropeptide FLP-20 Acts as a Systemic Signal for Starvation Responses in Caenorhabditis elegans. Mol Cells 2021;44:529-37. [PMID: 34140426 DOI: 10.14348/molcells.2021.0051] [Reference Citation Analysis]
9 Navarro-Betancourt JR, Papillon J, Guillemette J, Chung CF, Iwawaki T, Cybulsky AV. The unfolded protein response transducer IRE1α promotes reticulophagy in podocytes. Biochim Biophys Acta Mol Basis Dis 2022;1868:166391. [PMID: 35304860 DOI: 10.1016/j.bbadis.2022.166391] [Reference Citation Analysis]
10 Pinto C, Ninfole E, Benedetti A, Marzioni M, Maroni L. Involvement of Autophagy in Ageing and Chronic Cholestatic Diseases. Cells 2021;10:2772. [PMID: 34685751 DOI: 10.3390/cells10102772] [Reference Citation Analysis]
11 Li H, Sun S. Protein Aggregation in the ER: Calm behind the Storm. Cells 2021;10:3337. [PMID: 34943844 DOI: 10.3390/cells10123337] [Reference Citation Analysis]
12 Harada Y, Ohkawa Y, Maeda K, Taniguchi N. Glycan quality control in and out of the endoplasmic reticulum of mammalian cells. FEBS J 2021. [PMID: 34492158 DOI: 10.1111/febs.16185] [Reference Citation Analysis]
13 Yu H, Kamber RA, Denic V. The peroxisomal exportomer directly inhibits phosphoactivation of the pexophagy receptor Atg36 to suppress pexophagy in yeast. Elife 2022;11:e74531. [PMID: 35404228 DOI: 10.7554/eLife.74531] [Reference Citation Analysis]
14 Henne WM. Organelle homeostasis principles: How organelle quality control and inter-organelle crosstalk promote cell survival. Dev Cell 2021;56:878-80. [PMID: 33823134 DOI: 10.1016/j.devcel.2021.03.012] [Reference Citation Analysis]
15 Gubas A, Dikic I. ER remodeling via ER-phagy. Mol Cell 2022;82:1492-500. [PMID: 35452617 DOI: 10.1016/j.molcel.2022.02.018] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
16 Sun J, Wang W, Zheng H. ROOT HAIR DEFECTIVE3 Is a Receptor for Selective Autophagy of the Endoplasmic Reticulum in Arabidopsis. Front Plant Sci 2022;13:817251. [PMID: 35283874 DOI: 10.3389/fpls.2022.817251] [Reference Citation Analysis]
17 Fregno I, Fasana E, Soldà T, Galli C, Molinari M. N-glycan processing selects ERAD-resistant misfolded proteins for ER-to-lysosome-associated degradation. EMBO J 2021;40:e107240. [PMID: 34152647 DOI: 10.15252/embj.2020107240] [Cited by in Crossref: 1] [Cited by in F6Publishing: 3] [Article Influence: 1.0] [Reference Citation Analysis]
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19 Wang B, Zhang J, Liu X, Chai Q, Lu X, Yao X, Yang Z, Sun L, Johnson SF, Schwartz RC, Zheng YH. Protein disulfide isomerases (PDIs) negatively regulate ebolavirus structural glycoprotein expression in the endoplasmic reticulum (ER) via the autophagy-lysosomal pathway. Autophagy 2022;:1-18. [PMID: 35130104 DOI: 10.1080/15548627.2022.2031381] [Reference Citation Analysis]
20 Wiseman RL, Mesgarzadeh JS, Hendershot LM. Reshaping endoplasmic reticulum quality control through the unfolded protein response. Mol Cell 2022;82:1477-91. [PMID: 35452616 DOI: 10.1016/j.molcel.2022.03.025] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
21 Reggiori F, Molinari M. ER-phagy: mechanisms, regulation and diseases connected to the lysosomal clearance of the endoplasmic reticulum. Physiol Rev 2022. [PMID: 35188422 DOI: 10.1152/physrev.00038.2021] [Reference Citation Analysis]