DDIT3 DDIT3の概要

DDIT3

出典: フリー百科事典『ウィキペディア(Wikipedia)』 (2023/10/28 07:03 UTC 版)

DDIT3
識別子
記号DDIT3, CEBPZ, CHOP, CHOP-10, CHOP10, GADD153, DNA damage-inducible transcript 3, DNA damage inducible transcript 3, C/EBPzeta, AltDDIT3
外部IDOMIM: 126337 MGI: 109247 HomoloGene: 3012 GeneCards: DDIT3
遺伝子の位置 (ヒト)
染色体12番染色体 (ヒト)[1]
バンドデータ無し開始点57,516,588 bp[1]
終点57,521,737 bp[1]
遺伝子の位置 (マウス)
染色体10番染色体 (マウス)[2]
バンドデータ無し開始点127,126,643 bp[2]
終点127,132,157 bp[2]
RNA発現パターン
さらなる参照発現データ
遺伝子オントロジー
分子機能 DNA結合
cAMP response element binding protein binding
transcription corepressor activity
DNA-binding transcription factor activity
DNA-binding transcription activator activity, RNA polymerase II-specific
転写因子結合
transcription cis-regulatory region binding
RNA polymerase II cis-regulatory region sequence-specific DNA binding
leucine zipper domain binding
血漿タンパク結合
protein heterodimerization activity
protein homodimerization activity
DNA-binding transcription factor activity, RNA polymerase II-specific
細胞の構成要素 細胞質
細胞質基質
late endosome
CHOP-C/EBP complex
核質
transcription factor AP-1 complex
protein-DNA complex
CHOP-ATF4 complex
CHOP-ATF3 complex
細胞核
生物学的プロセス アポトーシス
release of sequestered calcium ion into cytosol
negative regulation of protein kinase B signaling
negative regulation of fat cell differentiation
negative regulation of myoblast differentiation
regulation of transcription, DNA-templated
positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway
positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress
negative regulation of DNA binding
mRNA transcription by RNA polymerase II
positive regulation of neuron death
negative regulation of transcription by RNA polymerase II
Wntシグナル経路
cell redox homeostasis
response to endoplasmic reticulum stress
PERK-mediated unfolded protein response
ER overload response
cellular response to DNA damage stimulus
transcription, DNA-templated
positive regulation of transcription, DNA-templated
ATF6-mediated unfolded protein response
positive regulation of neuron apoptotic process
response to unfolded protein
intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding
positive regulation of interleukin-8 production
餓死
negative regulation of determination of dorsal identity
細胞周期
regulation of DNA-templated transcription in response to stress
negative regulation of transcription, DNA-templated
negative regulation of canonical Wnt signaling pathway
positive regulation of transcription by RNA polymerase II
proteasome-mediated ubiquitin-dependent protein catabolic process
blood vessel maturation
negative regulation of CREB transcription factor activity
小胞体ストレス
establishment of protein localization to mitochondrion
intrinsic apoptotic signaling pathway in response to nitrosative stress
negative regulation of DNA-binding transcription factor activity
positive regulation of DNA-binding transcription factor activity
protein complex oligomerization
negative regulation of cold-induced thermogenesis
regulation of autophagy
positive regulation of intrinsic apoptotic signaling pathway
出典:Amigo / QuickGO
オルソログ
ヒトマウス
Entrez
Ensembl
UniProt
RefSeq
(mRNA)
NM_001195053
NM_001195054
NM_001195055
NM_001195056
NM_001195057

NM_004083

NM_001290183
NM_007837

RefSeq
(タンパク質)
NP_001181982
NP_001181983
NP_001181984
NP_001181985
NP_001181986

NP_004074

NP_001277112
NP_031863

場所
(UCSC)
Chr 12: 57.52 – 57.52 MbChr 12: 127.13 – 127.13 Mb
PubMed検索[3][4]
ウィキデータ
閲覧/編集 ヒト閲覧/編集 マウス

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000175197 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025408 - Ensembl, May 2017
  3. ^ Human PubMed Reference:
  4. ^ Mouse PubMed Reference:
  5. ^ “Induction by ionizing radiation of the gadd45 gene in cultured human cells: lack of mediation by protein kinase C”. Molecular and Cellular Biology 11 (2): 1009–16. (February 1991). doi:10.1128/MCB.11.2.1009. PMC 359769. PMID 1990262. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC359769/. 
  6. ^ a b c Entrez Gene: DDIT3 DNA-damage-inducible transcript 3”. 2022年9月3日閲覧。
  7. ^ “Stress-induced binding of the transcriptional factor CHOP to a novel DNA control element”. Molecular and Cellular Biology 16 (4): 1479–89. (April 1996). doi:10.1128/MCB.16.4.1479. PMC 231132. PMID 8657121. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC231132/. 
  8. ^ “CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription”. Genes & Development 6 (3): 439–53. (March 1992). doi:10.1101/gad.6.3.439. PMID 1547942. 
  9. ^ “A non-canonical pathway regulates ER stress signaling and blocks ER stress-induced apoptosis and heart failure”. Nature Communications 8 (1): 133. (July 2017). Bibcode2017NatCo...8..133Y. doi:10.1038/s41467-017-00171-w. PMC 5527107. PMID 28743963. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5527107/. 
  10. ^ a b c “Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis”. The Journal of Cell Biology 186 (6): 783–92. (September 2009). doi:10.1083/jcb.200904060. PMC 2753154. PMID 19752026. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2753154/. 
  11. ^ “Roles of CHOP/GADD153 in endoplasmic reticulum stress”. Cell Death and Differentiation 11 (4): 381–9. (April 2004). doi:10.1038/sj.cdd.4401373. PMID 14685163. 
  12. ^ “ER stress and diseases”. The FEBS Journal 274 (3): 630–58. (February 2007). doi:10.1111/j.1742-4658.2007.05639.x. PMID 17288551. 
  13. ^ “GRP78 and CHOP modulate macrophage apoptosis and the development of bleomycin-induced pulmonary fibrosis”. The Journal of Pathology 239 (4): 411–25. (August 2016). doi:10.1002/path.4738. PMID 27135434. 
  14. ^ “Endoplasmic reticulum stress implicated in chronic traumatic encephalopathy”. Journal of Neurosurgery 124 (3): 687–702. (March 2016). doi:10.3171/2015.3.JNS141802. PMID 26381255. 
  15. ^ “Endoplasmic reticulum stress in the pathogenesis of fibrotic disease”. The Journal of Clinical Investigation 128 (1): 64–73. (January 2018). doi:10.1172/JCI93560. PMC 5749533. PMID 29293089. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5749533/. 
  16. ^ “The Role of the PERK/eIF2α/ATF4/CHOP Signaling Pathway in Tumor Progression During Endoplasmic Reticulum Stress”. Current Molecular Medicine 16 (6): 533–44. (2016). doi:10.2174/1566524016666160523143937. PMC 5008685. PMID 27211800. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5008685/. 
  17. ^ “ER stress-induced cell death mechanisms”. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1833 (12): 3460–3470. (December 2013). doi:10.1016/j.bbamcr.2013.06.028. PMC 3834229. PMID 23850759. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3834229/. 
  18. ^ “Antiapoptotic roles of ceramide-synthase-6-generated C16-ceramide via selective regulation of the ATF6/CHOP arm of ER-stress-response pathways”. FASEB Journal 24 (1): 296–308. (January 2010). doi:10.1096/fj.09-135087. PMC 2797032. PMID 19723703. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2797032/. 
  19. ^ “Apelin-13 Alleviates Early Brain Injury after Subarachnoid Hemorrhage via Suppression of Endoplasmic Reticulum Stress-mediated Apoptosis and Blood-Brain Barrier Disruption: Possible Involvement of ATF6/CHOP Pathway”. Neuroscience 388: 284–296. (September 2018). doi:10.1016/j.neuroscience.2018.07.023. PMID 30036660. 
  20. ^ “ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response”. Molecular and Cellular Biology 20 (18): 6755–67. (September 2000). doi:10.1128/mcb.20.18.6755-6767.2000. PMC 86199. PMID 10958673. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC86199/. 
  21. ^ “IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates”. Cell 138 (3): 562–75. (August 2009). doi:10.1016/j.cell.2009.07.017. PMC 2762408. PMID 19665977. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2762408/. 
  22. ^ “XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor”. Cell 107 (7): 881–91. (December 2001). doi:10.1016/s0092-8674(01)00611-0. PMID 11779464. 
  23. ^ “The unfolded protein response: integrating stress signals through the stress sensor IRE1α”. Physiological Reviews 91 (4): 1219–43. (October 2011). doi:10.1152/physrev.00001.2011. hdl:10533/135654. PMID 22013210. 
  24. ^ “Transcription Factor C/EBP Homologous Protein in Health and Diseases”. Frontiers in Immunology 8: 1612. (2017). doi:10.3389/fimmu.2017.01612. PMC 5712004. PMID 29230213. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5712004/. 
  25. ^ “Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities”. Nature Reviews. Drug Discovery 7 (12): 1013–30. (December 2008). doi:10.1038/nrd2755. PMID 19043451. 
  26. ^ “Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP Kinase”. Science 272 (5266): 1347–9. (May 1996). Bibcode1996Sci...272.1347W. doi:10.1126/science.272.5266.1347. PMID 8650547. 
  27. ^ “How IRE1 reacts to ER stress”. Cell 132 (1): 24–6. (January 2008). doi:10.1016/j.cell.2007.12.017. PMID 18191217. 
  28. ^ “Attenuation of CHOP-mediated myocardial apoptosis in pressure-overloaded dominant negative p38α mitogen-activated protein kinase mice”. Cellular Physiology and Biochemistry 27 (5): 487–96. (2011). doi:10.1159/000329970. PMID 21691066. 
  29. ^ a b “Tunicamycin enhances human colon cancer cells to TRAIL-induced apoptosis by JNK-CHOP-mediated DR5 upregulation and the inhibition of the EGFR pathway”. Anti-Cancer Drugs 28 (1): 66–74. (January 2017). doi:10.1097/CAD.0000000000000431. PMID 27603596. 
  30. ^ “UPR induces transient burst of apoptosis in islets of early lactating rats through reduced AKT phosphorylation via ATF4/CHOP stimulation of TRB3 expression”. American Journal of Physiology. Regulatory, Integrative and Comparative Physiology 300 (1): R92-100. (January 2011). doi:10.1152/ajpregu.00169.2010. PMID 21068199. https://lirias.kuleuven.be/handle/123456789/486415. 
  31. ^ “The transcription factor CHOP, a central component of the transcriptional regulatory network induced upon CCl4 intoxication in mouse liver, is not a critical mediator of hepatotoxicity”. Archives of Toxicology 88 (6): 1267–80. (June 2014). doi:10.1007/s00204-014-1240-8. hdl:10533/127482. PMID 24748426. 
  32. ^ “CHOP potentially co-operates with FOXO3a in neuronal cells to regulate PUMA and BIM expression in response to ER stress”. PLOS ONE 7 (6): e39586. (2012-06-28). Bibcode2012PLoSO...739586G. doi:10.1371/journal.pone.0039586. PMC 3386252. PMID 22761832. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3386252/. 
  33. ^ “Neuronal apoptosis induced by endoplasmic reticulum stress is regulated by ATF4-CHOP-mediated induction of the Bcl-2 homology 3-only member PUMA”. The Journal of Neuroscience 30 (50): 16938–48. (December 2010). doi:10.1523/JNEUROSCI.1598-10.2010. PMC 6634926. PMID 21159964. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6634926/. 
  34. ^ “Stress-induced binding of the transcriptional factor CHOP to a novel DNA control element”. Molecular and Cellular Biology 16 (4): 1479–89. (April 1996). doi:10.1128/mcb.16.4.1479. PMC 231132. PMID 8657121. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC231132/. 
  35. ^ “Cell death induced by endoplasmic reticulum stress”. The FEBS Journal 283 (14): 2640–52. (July 2016). doi:10.1111/febs.13598. PMID 26587781. 
  36. ^ “The endoplasmic reticulum stress-C/EBP homologous protein pathway-mediated apoptosis in macrophages contributes to the instability of atherosclerotic plaques”. Arteriosclerosis, Thrombosis, and Vascular Biology 30 (10): 1925–32. (October 2010). doi:10.1161/ATVBAHA.110.206094. PMID 20651282. 
  37. ^ “Interrogating the relevance of mitochondrial apoptosis for vertebrate development and postnatal tissue homeostasis”. Genes & Development 30 (19): 2133–2151. (October 2016). doi:10.1101/gad.289298.116. PMC 5088563. PMID 27798841. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5088563/. 
  38. ^ “TRB3 is stimulated in diabetic kidneys, regulated by the ER stress marker CHOP, and is a suppressor of podocyte MCP-1”. American Journal of Physiology. Renal Physiology 299 (5): F965-72. (November 2010). doi:10.1152/ajprenal.00236.2010. PMC 2980398. PMID 20660016. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2980398/. 
  39. ^ “Loss of C/EBP-β LIP drives cisplatin resistance in malignant pleural mesothelioma”. Lung Cancer 120: 34–45. (June 2018). doi:10.1016/j.lungcan.2018.03.022. PMID 29748013. 
  40. ^ “HDAC4 protects cells from ER stress induced apoptosis through interaction with ATF4”. Cellular Signalling 26 (3): 556–63. (March 2014). doi:10.1016/j.cellsig.2013.11.026. PMID 24308964. 
  41. ^ “TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death”. The EMBO Journal 24 (6): 1243–55. (March 2005). doi:10.1038/sj.emboj.7600596. PMC 556400. PMID 15775988. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC556400/. 
  42. ^ “TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver”. Science 300 (5625): 1574–7. (June 2003). Bibcode2003Sci...300.1574D. doi:10.1126/science.1079817. PMID 12791994. 
  43. ^ “TRB3 reverses chemotherapy resistance and mediates crosstalk between endoplasmic reticulum stress and AKT signaling pathways in MHCC97H human hepatocellular carcinoma cells”. Oncology Letters 15 (1): 1343–1349. (January 2018). doi:10.3892/ol.2017.7361. PMC 5769383. PMID 29391905. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5769383/. 
  44. ^ a b c “DDIT3 and KAT2A Proteins Regulate TNFRSF10A and TNFRSF10B Expression in Endoplasmic Reticulum Stress-mediated Apoptosis in Human Lung Cancer Cells”. The Journal of Biological Chemistry 290 (17): 11108–18. (April 2015). doi:10.1074/jbc.M115.645333. PMC 4409269. PMID 25770212. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4409269/. 
  45. ^ “Neddylation Inhibition Activates the Extrinsic Apoptosis Pathway through ATF4-CHOP-DR5 Axis in Human Esophageal Cancer Cells”. Clinical Cancer Research 22 (16): 4145–57. (August 2016). doi:10.1158/1078-0432.CCR-15-2254. PMID 26983464. 
  46. ^ “Opposing unfolded-protein-response signals converge on death receptor 5 to control apoptosis”. Science 345 (6192): 98–101. (July 2014). Bibcode2014Sci...345...98L. doi:10.1126/science.1254312. PMC 4284148. PMID 24994655. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4284148/. 
  47. ^ “Apoptosis: a review of programmed cell death”. Toxicologic Pathology 35 (4): 495–516. (June 2007). doi:10.1080/01926230701320337. PMC 2117903. PMID 17562483. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/. 
  48. ^ “CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum”. Genes & Development 18 (24): 3066–77. (December 2004). doi:10.1101/gad.1250704. PMC 535917. PMID 15601821. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC535917/. 
  49. ^ a b “Fusion of the EWS and CHOP genes in myxoid liposarcoma”. Oncogene 12 (3): 489–94. (February 1996). PMID 8637704. 
  50. ^ “NADPH oxidase links endoplasmic reticulum stress, oxidative stress, and PKR activation to induce apoptosis”. The Journal of Cell Biology 191 (6): 1113–25. (December 2010). doi:10.1083/jcb.201006121. PMC 3002036. PMID 21135141. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3002036/. 
  51. ^ a b “Targeting unfolded protein response in cancer and diabetes”. Endocrine-Related Cancer 22 (3): C1-4. (June 2015). doi:10.1530/ERC-15-0106. PMID 25792543. 
  52. ^ a b “GRP78 Interacting Partner Bag5 Responds to ER Stress and Protects Cardiomyocytes From ER Stress-Induced Apoptosis”. Journal of Cellular Biochemistry 117 (8): 1813–21. (August 2016). doi:10.1002/jcb.25481. PMC 4909508. PMID 26729625. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4909508/. 
  53. ^ “Bcl-2 associated athanogene 5 (Bag5) is overexpressed in prostate cancer and inhibits ER-stress induced apoptosis”. BMC Cancer 13: 96. (March 2013). doi:10.1186/1471-2407-13-96. PMC 3598994. PMID 23448667. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3598994/. 
  54. ^ “Analysis of ATF3, a transcription factor induced by physiological stresses and modulated by gadd153/Chop10”. Molecular and Cellular Biology 16 (3): 1157–68. (March 1996). doi:10.1128/MCB.16.3.1157. PMC 231098. PMID 8622660. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC231098/. 
  55. ^ a b c “CHOP enhancement of gene transcription by interactions with Jun/Fos AP-1 complex proteins”. Molecular and Cellular Biology 19 (11): 7589–99. (November 1999). doi:10.1128/MCB.19.11.7589. PMC 84780. PMID 10523647. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC84780/. 
  56. ^ “C/EBP homologous protein (CHOP) up-regulates IL-6 transcription by trapping negative regulating NF-IL6 isoform”. FEBS Letters 541 (1–3): 33–9. (April 2003). doi:10.1016/s0014-5793(03)00283-7. PMID 12706815. 
  57. ^ “Physical and functional association between GADD153 and CCAAT/enhancer-binding protein beta during cellular stress”. The Journal of Biological Chemistry 271 (24): 14285–9. (June 1996). doi:10.1074/jbc.271.24.14285. PMID 8662954. 
  58. ^ “CHOP transcription factor phosphorylation by casein kinase 2 inhibits transcriptional activation”. The Journal of Biological Chemistry 278 (42): 40514–20. (October 2003). doi:10.1074/jbc.M306404200. PMID 12876286. 
  59. ^ “Novel interaction between the transcription factor CHOP (GADD153) and the ribosomal protein FTE/S3a modulates erythropoiesis”. The Journal of Biological Chemistry 275 (11): 7591–6. (March 2000). doi:10.1074/jbc.275.11.7591. PMID 10713066. 
  60. ^ Song, Benbo; Scheuner, Donalyn; Ron, David; Pennathur, Subramaniam; Kaufman, Randal J. (October 2008). “Chop deletion reduces oxidative stress, improves beta cell function, and promotes cell survival in multiple mouse models of diabetes”. The Journal of Clinical Investigation 118 (10): 3378–3389. doi:10.1172/JCI34587. ISSN 0021-9738. PMC 2528909. PMID 18776938. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2528909/. 
  61. ^ Maris, M.; Overbergh, L.; Gysemans, C.; Waget, A.; Cardozo, A. K.; Verdrengh, E.; Cunha, J. P. M.; Gotoh, T. et al. (April 2012). “Deletion of C/EBP homologous protein (Chop) in C57Bl/6 mice dissociates obesity from insulin resistance” (英語). Diabetologia 55 (4): 1167–1178. doi:10.1007/s00125-011-2427-7. ISSN 0012-186X. PMID 22237685. http://link.springer.com/10.1007/s00125-011-2427-7. 
  62. ^ a b Yong, Jing; Parekh, Vishal S.; Reilly, Shannon M.; Nayak, Jonamani; Chen, Zhouji; Lebeaupin, Cynthia; Jang, Insook; Zhang, Jiangwei et al. (2021-07-28). “Chop/Ddit3 depletion in β cells alleviates ER stress and corrects hepatic steatosis in mice”. Science Translational Medicine 13 (604). doi:10.1126/scitranslmed.aba9796. ISSN 1946-6242. PMC 8557800. PMID 34321322. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8557800/. 
  63. ^ WO application 2017192820, Monia, Brett P.; Thazha P. Prakash & Garth A. Kinberger et al., "GLP-1 receptor ligand moiety conjugated oligonucleotides and uses thereof", published 2017-11-09, assigned to Ionis Pharmaceuticals Inc. and AstraZeneca AB 
  64. ^ Yong, Jing; Johnson, James D.; Arvan, Peter; Han, Jaeseok; Kaufman, Randal J. (August 2021). “Therapeutic opportunities for pancreatic β-cell ER stress in diabetes mellitus”. Nature Reviews. Endocrinology 17 (8): 455–467. doi:10.1038/s41574-021-00510-4. ISSN 1759-5037. PMC 8765009. PMID 34163039. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8765009/. 
  65. ^ a b “Porcine Circovirus 2 Deploys PERK Pathway and GRP78 for Its Enhanced Replication in PK-15 Cells”. Viruses 8 (2): 56. (February 2016). doi:10.3390/v8020056. PMC 4776210. PMID 26907328. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4776210/. 
  66. ^ “HIV Tat-Mediated Induction of Human Brain Microvascular Endothelial Cell Apoptosis Involves Endoplasmic Reticulum Stress and Mitochondrial Dysfunction”. Molecular Neurobiology 53 (1): 132–142. (January 2016). doi:10.1007/s12035-014-8991-3. PMC 4787264. PMID 25409632. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4787264/. 
  67. ^ “HIV-1 gp120 induces type-1 programmed cell death through ER stress employing IRE1α, JNK and AP-1 pathway”. Scientific Reports 6: 18929. (January 2016). Bibcode2016NatSR...618929S. doi:10.1038/srep18929. PMC 4703964. PMID 26740125. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4703964/. 
  68. ^ “Upregulation of CHOP/GADD153 during coronavirus infectious bronchitis virus infection modulates apoptosis by restricting activation of the extracellular signal-regulated kinase pathway”. Journal of Virology 87 (14): 8124–34. (July 2013). doi:10.1128/JVI.00626-13. PMC 3700216. PMID 23678184. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3700216/. 
  69. ^ “Endoplasmic reticulum stress pathway-mediated apoptosis in macrophages contributes to the survival of Mycobacterium tuberculosis”. PLOS ONE 6 (12): e28531. (2011). Bibcode2011PLoSO...628531L. doi:10.1371/journal.pone.0028531. PMC 3237454. PMID 22194844. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3237454/. 
  70. ^ “Induction of ER stress in macrophages of tuberculosis granulomas”. PLOS ONE 5 (9): e12772. (September 2010). Bibcode2010PLoSO...512772S. doi:10.1371/journal.pone.0012772. PMC 2939897. PMID 20856677. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2939897/. 
  71. ^ “Endoplasmic reticulum stress contributes to Helicobacter pylori VacA-induced apoptosis”. PLOS ONE 8 (12): e82322. (2013). Bibcode2013PLoSO...882322A. doi:10.1371/journal.pone.0082322. PMC 3862672. PMID 24349255. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3862672/. 
  72. ^ “Shiga toxin 1 induces apoptosis through the endoplasmic reticulum stress response in human monocytic cells”. Cellular Microbiology 10 (3): 770–80. (March 2008). doi:10.1111/j.1462-5822.2007.01083.x. PMID 18005243. 
  73. ^ “Shiga Toxins Induce Apoptosis and ER Stress in Human Retinal Pigment Epithelial Cells”. Toxins 9 (10): 319. (October 2017). doi:10.3390/toxins9100319. PMC 5666366. PMID 29027919. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5666366/. 
  74. ^ “Different induction of GRP78 and CHOP as a predictor of sensitivity to proteasome inhibitors in thyroid cancer cells”. Endocrinology 148 (7): 3258–70. (July 2007). doi:10.1210/en.2006-1564. PMID 17431003. 
  75. ^ “C/EBP homologous protein inhibits tissue repair in response to gut injury and is inversely regulated with chronic inflammation”. Mucosal Immunology 7 (6): 1452–66. (November 2014). doi:10.1038/mi.2014.34. PMID 24850428. 


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この記事は、ウィキペディアのDDIT3 (改訂履歴)の記事を複製、再配布したものにあたり、GNU Free Documentation Licenseというライセンスの下で提供されています。 Weblio辞書に掲載されているウィキペディアの記事も、全てGNU Free Documentation Licenseの元に提供されております。

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