[1] |
FAGONE P, JACKOWSKI S. Membrane phospholipid synthesis and endoplasmic reticulum function. Journal of Lipid Research, 2009, 50 Suppl(50 Suppl):S311. DOI: 10.1194/jlr.R800049-JLR200.
doi: 10.1194/jlr.R800049-JLR200
|
[2] |
BRAAKMAN I, HEBERT D N. Protein folding in the endoplasmic reticulum. Cold Spring Harbor Perspectives in Biology, 2013,5(5):a013201-a013201. DOI: 10.1101/cshperspect.a013201.
pmid: 23637286
|
[3] |
WANG M, KAUFMAN R J. Protein misfolding in the endoplasmic reticulum as a conduit to human disease. Nature, 2016,529(7586):326-335. DOI: 10.1038/nature17041.
doi: 10.1038/nature17041
pmid: 26791723
|
[4] |
BOHNERT K R, MCMILLAN J D, KUMAR A. Emerging roles of ER stress and unfolded protein response pathways in skeletal muscle health and disease. Journal of Cellular Physiology, 2017. DOI: 10.1002/jcp.25852.
pmid: 32725819
|
[5] |
HETZ C. The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nature Reviews Molecular Cell Biology, 2012,13:H2410-H2418. DOI: 10.1038/nrm3270.
|
[6] |
WALTER P, RON D. The unfolded protein response: From stress pathway to homeostatic regulation. Science, 2011,334(6059):1081-1086. DOI: 10.1126/science.1209038.
doi: 10.1126/science.1209038
pmid: 22116877
|
[7] |
BERTOLOTTI A, ZHANG Y H, HENDERSHOT L M, HARDING H P, RON D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein respons. Nature Cell Biology, 2000,2(6):326-332. DOI: 10.1038/35014014.
pmid: 10854322
|
[8] |
HETZ C, PAPA F R. The unfolded protein response and cell fate control. Molecular Cell, 2017,69(2). DOI: 10.1016/j.molcel.2017.06.017.
doi: 10.1016/j.molcel.2017.06.017
pmid: 29107536
|
[9] |
LEE A H, IWAKOSHI N N, GLIMCHER L H. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Molecular and Cellular Biology, 2003,23(21):7448-7459. DOI: 10.1128/MCB.23.21.7448-7459.2003.
doi: 10.1128/mcb.23.21.7448-7459.2003
pmid: 14559994
|
[10] |
王镜淇, 龚国清. 内质网应激与炎症反应的研究进展. 药学研究, 2017,36(5):279-282. DOI: 10.13506/j.cnki.jpr.2017.05.009.
|
|
WANG J Q, GONG G Q. Research progress on endoplasmic reticulum stress and inflammatory response. Journal of Pharmaceutical Research, 2017,36(5):279-282. DOI: 10.13506/j.cnki.jpr.2017.05.009. (in Chinese)
|
[11] |
DING W X, NI H M, GAO W T, HOU Y F, MELAN M A, CHEN X划 Y, STOLZ D B, SHAO Z M, YIN X M. Differential effects of endoplasmic reticulum stress-induced autophagy on cell survival. Journal of Biological Chemistry, 2007,282(7):4702-4710. DOI: 10.1074/jbc.m609267200.
pmid: 17135238
|
[12] |
HERBERT T P, LAYBUTT D R. A reevaluation of the role of the unfolded protein response in islet dysfunction: maladaptation or a failure to Adapt? Diabetes, 2016,65(6):1472-1480. DOI: 10.2337/db15-1633.
pmid: 27222391
|
[13] |
徐静尊, 鲁敏. 内质网应激与自噬及其交互作用影响内皮细胞凋亡. 中国生物化学与分子生物学报, 2019,35(3). DOI: 10.13865/j.cnki.cjbmb.2019.03.02.
|
|
XU J Z, LU M. Effects of endoplasmic reticulum stress and autophagy on endothelial cell apoptosis. Chinese Journal of Biochemistry and Molecular Biology, 2019,35(3). DOI: 10.13865/j.cnki.cjbmb.2019.03.02.(in Chinese)
|
[14] |
ZHOU Y S, GU Y X, QI B Z, ZHANG Y K, LI X L, FANG W H. Porcine circovirus type 2 capsid protein induces unfolded protein response with subsequent activation of apoptosis. Journal of Zhejiang University-SCIENCE B, 2017,18(4):316-323. DOI: 10.1631/jzus.B1600208.
doi: 10.1631/jzus.B1600208
pmid: 28378569
|
[15] |
HE W C, XU H L, GOU H C, YUAN J, LIAO J D, CHEN Y M, FAN S Q, XIE B M, DENG S F, ZHANG Y Y, CHEN J D, ZHAO M Q. CSFV Infection up-regulates the unfolded protein response to promote its replication. Frontiers in Microbiology, 2017,8:2129. DOI: 10.3389/fmicb.2017.02129.
doi: 10.3389/fmicb.2017.02129
pmid: 29163417
|
[16] |
YANG S B, PEI Y, ZHAO A Y. iTRAQ-based proteomic analysis of porcine kidney Epithelial PK15 cells infected with Pseudorabies virus. Scientific Reports, 2017,7:45922. DOI: 10.1038/srep45922.
doi: 10.1038/srep45922
pmid: 28374783
|
[17] |
YANG S B, ZHU J J, ZHOU X L, WANG H, LI X C, ZHAO A Y. Induction of the unfolded protein response (UPR) during pseudorabies virus infection. Veterinary Microbiology, 2019,239. DOI: 10.1016/j.vetmic.2019.108485.
pmid: 31767081
|
[18] |
SU S F, CHANG Y W, ANDREU-VIEYRA C, FANG J Y, YANG Z, HAN B, LEE A S, LIANG G. miR-30d, miR-181a and miR-199a-5p cooperatively suppress the endoplasmic reticulum chaperone and signaling regulator GRP78 in cancer. Oncogene, 2013,32(39):4694-4701. DOI: 10.1038/onc.2012.483.
pmid: 23085757
|
[19] |
OGLESBY I K, AGRAWAL R, MALL M A, MCELVANEY N G, GREENE C M. miRNA-221 is elevated in cystic fibrosis airway epithelial cells and regulates expression of ATF6. Molecular and Cellular Pediatrics, 2015,2(1):1. DOI: 10.1186/s40348-014-0012-0.
pmid: 26542291
|
[20] |
ZHANG W G, CHEN L, DONG Q, HE J, ZHAO H D, LI F L, LI H. Mmu-miR-702 functions as an anti-apoptotic mirtron by mediating ATF6 inhibition in mice. Gene, 2013,531(2):235-242. DOI: 10.1016/j.gene.2013.09.005.
doi: 10.1016/j.gene.2013.09.005
pmid: 24035931
|
[21] |
YANG F, ZHANG L, WANG F, WANG Y, HUO X S, YIN Y X, WANG Y Q, ZHANG L, SUN S H. Modulation of the unfolded protein response is the core of microrna-122-involved sensitivity to chemotherapy in hepatocellular carcinoma. Neoplasia, 2011,13(7):590. DOI: 10.1593/neo.11422.
pmid: 21750653
|
[22] |
BYRD A E, ARAGON I V, BREWER J W. MicroRNA-30c-2* limits expression of proadaptive factor XBP1 in the unfolded protein response. Journal of Cell Biology, 2012,196(6):689-698. DOI: 10.1083/jcb.201201077.
pmid: 22431749
|
[23] |
LIU F, ZHENG H, TONG W, LI G X, TIAN Q, LIANG C, LI L W, ZHENG X C, TONG G Z. Identification and analysis of novel viral and host dysregulated micrornas in variant pseudorabies virus-infected PK15 cells. PLoS ONE, 2016,11(3):e0151546. DOI: 10.1371/journal. pone.0151546.
pmid: 26998839
|
[24] |
邓少锋, 叶佐东, 范双旗, 陈金顶, 张静远, 朱梦娇, 赵明秋. PK-15细胞中与CSFV感染相关的microRNAs筛选及miR-214的功能研究. 中国农业科学, 2018,51(21):156-167. DOI: 10.3864/j.issn.0578-1752.2018.21.014.
|
|
DENG S F, YE Z D, FAN S Q, CHEN J D, ZHANG J Y, ZHU M J, ZHAO M Q. Screen of micrornas in classical swine fever virus-infected pk-15 cells and the regulation of virus replication by miR-214. Scientia Agricultura Sinica, 2018,51(21):156-167. DOI: 10.3864/j.issn.0578-1752.2018.21.014.(in Chinese)
|
[25] |
HEINDRYCKX F, BINET F, PONTICOS M, ROMBOUTS K, LAU J, KREUGER J, GERWINS P. Endoplasmic reticulum stress enhances fibrosis through IRE1α-mediated degradation of miR-150 and XBP-1 splicing. EMBO Molecular Medicine, 2016,8. DOI: 10.15252/emmm.201505925.
pmid: 27621275
|
[26] |
YU J, LIU F H, YIN P, ZHU X Y, CHENG G L, WANG N, LU A, LUAN W L, ZHANG N W, LI J F, GUO K J, YIN Y L, WANG H C, XU J Q. Integrating miRNA and mRNA expression profiles in response to heat stress-induced injury in rat small intestine. Functional & Integrative Genomics, 2011,11(2):203-213. DOI: 10.1007/s10142-010-0198-8.
pmid: 21057845
|
[27] |
LIU X Y, ZHANG Y, WANG S, LIU G Y, RUAN L M. Loss of miR-143 and miR-145 in condyloma acuminatum promotes cellular proliferation and inhibits apoptosis by targeting NRAS. Royal Society Open Science, 2018. DOI: 10.1098/rsos.172376.
pmid: 32742688
|
[28] |
AHMADI A, KHANSARINEJAD B, HOSSEINKHANI S, GHANEI M, MOWLA S J. miR-199a-5p and miR-495 target GRP78 within UPR pathway of lung cancer. Gene, 2017,620:15-22. DOI: 10.1016/j.gene.2017.03.032.
pmid: 28363780
|
[29] |
GUPTA A, HOSSAIN M M, READ D E, HETZ C, SAMALI A, GUPTA S. PERK regulated miR-424(322)-503 cluster fine-tunes activation of IRE1 and ATF6 during Unfolded Protein Response. Scientific Reports, 2016,5(1):18304. DOI: 10.1038/srep18304.
doi: 10.1038/srep18304
|
[30] |
ADACHI Y, YAMAMOTO K, OKADA T, YOSHIDA H, HARADA A, MORI K. ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum. Cell Structure and Function, 2008,33(1):75-89. DOI: 10.1247/csf.07044.
doi: 10.1247/csf.07044
pmid: 18360008
|