The stress-responsive protein REDD1 and its pathophysiological functions

참고문헌 (165)

1. Alvarez-Garcia, O., "Regulated in development and DNA damage response 1deficiency impairs autophagy and mitochondrial biogenesis in articular cartilage and increases the severity of experimental osteoarthritis", Arthritis Rheumatol, 69, pp.1418~1428 (2017)
2. Qiao, S., "A REDD1", TXNIP pro-oxidant complex regulates ATG4B activity to control stress-induced autophagy and sustain exercise capacity, 2015, pp.6, 7014~
3. Molitoris, J. K., "Glucocorticoid elevation of dexamethasone-induced gene 2(Dig2", RTP801, J. Biol. Chem, pp.2011, 286[DOI]
4. Britto, F. A., "REDD1 deletion prevents dexamethasone-induced skeletal muscle atrophy", Am. J. Physiol. Endocrinol. Metab, 307, pp.E983~E993 (2014)
5. Britto, F. A., "Glucocorticoid-dependent REDD1 expression reduces muscle metabolism to enable adaptation under energetic stress", BMC Biol, 16, pp.65~ (2018)
6. Lee, D. K., "REDD1 promotes obesity-induced metabolic dysfunction via atypical NF-κB activation", Nat. Commun, 13, pp.6303~ (2022)
7. Dumas, K., "REDD1 deficiency protects against nonalcoholic hepatic steatosis induced by high-fat diet", FASEB J, 34, pp.5046~5060 (2020)
8. Wenes, M., "Macrophage metabolism controls tumor blood vessel morphogenesis and metastasis", Cell Metab, 24, pp.701~715 (2016)
9. Williamson, D. L., "Altered nutrient response of mTORC1 as a result of changes in REDD1 expression: effect of obesity vs. REDD1 deficiency", J. Appl. Physiol, 117, pp.246~256 (2014)
10. Miller, W. P., "The stress response protein REDD1 as a causal factor for oxidative stress in diabetic retinopathy", Free Radic. Biol. Med, 165, pp.127~136 (2021)
11. Brafman, A., "Inhibition of oxygen-induced retinopathy in RTP801-defi-cient mice", Invest. Ophthalmol. Vis. Sci, 45, pp.3796~3805 (2004)
12. Ota, K. T., "REDD1 is essential for stress-induced synaptic loss and depressive behavior", Nat. Med, 20, pp.531~535 (2014)
13. Miller, W. P., "Müller glial expression of REDD1 is required for retinal neurodegeneration and visual dysfunction in diabetic mice", Diabetes, 71, pp.1051~1062 (2022)
14. Yoshida, T., "Rtp801, a suppressor of mTOR signaling, is an essential mediator of cigarette smoke-induced pulmonary injury and emphysema", Nat. Med, 16, pp.767~773 (2010)
15. DeYoung, M. P., "Hypoxia regulates TSC1", 2-mTOR signaling and tumor suppression through REDD1-mediated 14-3-3 shuttling, 2008, pp.22, 239~251
16. Chang, B., "REDD1 is required for RAS-mediated transformation of human ovarian epithelial cells", Cell Cycle, 8, pp.780~786 (2009)
17. Horak, P., "Negative feedback control of HIF-1 through REDD1-regulated ROS suppresses tumorigenesis", Proc. Natl Acad. Sci. USA, 107, pp.4675~4680 (2010)
18. Park Minsik, "REDD1 is a determinant of low-dose metronomic doxorubicin-elicited endothelial cell dysfunction through downregulation of VEGFR-2", 3 expression, 2021, pp.53, 1~11[DOI]
19. Shoshani, T., "Identification of a novel hypoxia-inducible factor 1-responsive gene, RTP801, involved in apoptosis", Mol. Cell. Biol, 22, pp.2283~2293 (2002)
20. Ellisen, L. W., "REDD1, a developmentally regulated transcriptional target of p63 and p53, links p63 to regulation of reactive oxygen species", Mol. Cell, 10, pp.995~1005 (2002)
21. Wang, Z., "Dexamethasone-induced gene 2(dig2)is a novel pro-survival stress gene induced rapidly by diverse apoptotic signals", J. Biol. Chem, 278, pp.27053~27058 (2003)
22. Knowles, L. M., "Inhibition of fatty-acid synthase induces caspase-8-mediated tumor cell apoptosis by up-regulating DDIT4", J. Biol. Chem, 283, pp.31378~31384 (2008)
23. Kim, M. Y., "Gadd45β is a novel mediator of cardiomyocyte apoptosis induced by ischaemia", hypoxia, 2010, pp.87, 119~126
24. Cho, S. S., "Induction of REDD1 via AP-1 prevents oxidative stress-mediated injury in hepatocytes", Free Radic. Biol. Med, 124, pp.221~231 (2018)
25. Jin, H. O., "TXNIP potentiates Redd1-induced mTOR suppression through stabilization of Redd1", Oncogene, 30, pp.3792~3801 (2011)
26. Dennis, M. D., "Regulated in development and DNA damage 1 is necessary for hyperglycemia-induced vascular endothelial growth factor expression in the retina of diabetic rodents", J. Biol. Chem, 290, pp.3865~3874 (2015)
27. Sofer, A., "Regulation of mTOR and cell growth in response to energy stress by REDD1", Mol. Cell. Biol, 25, pp.5834~5845 (2005)
28. Sunilkumar, S., "Stress response protein REDD1 promotes diabetes-induced retinal inflammation by sustaining canonical NF-κB signaling", J. Biol. Chem, 298, pp.102638~ (2022)
29. Jin, H. O., "Amino acid deprivation induces AKT activation by inducing GCN2", ATF4, Cell Death Dis, pp.2021, 12[DOI]
30. Qi, Y., "Sphingosine kinase 1 protects hepatocytes from lipotoxicity via downregulation of IRE1α protein expression", J. Biol. Chem, 290, pp.23282~23290 (2015)
31. Stevens, S. A., "PERK", ATF4-dependent expression of the stress response protein REDD1 promotes pro-inflammatory cytokine expression in the heart of obese mice, 2023, pp.324, E62~E72
32. Schupp, M., "Metabolite and transcriptome analysis during fasting suggest a role for the p53-Ddit4 axis in major metabolic tissues", BMC Genomics, 14, pp.758~ (2013)
33. McGhee, N. K., "Elevated corticosterone associated with food deprivation upregulates expression in rat skeletal muscle of the mTORC1 repressor, REDD1", J. Nutr, 139, pp.828~834 (2009)
34. Dennis, M. D., "Regulated in DNA damage and development 1(REDD1)promotes cell survival during serum deprivation by sustaining repression of signaling through the mechanistic target of rapamycin in complex 1(mTORC1)", Cell. Signal, 25, pp.2709~2716 (2013)
35. Dai, W., "Deletion of the stress-response protein REDD1 promotes ceramideinduced retinal cell death and JNK activation", FASEB J, 19, pp.32~ (2018)
36. Miller, W. P., "Deletion of the Akt", mTORC1 repressor REDD1 prevents visual dysfunction in a rodent model of type 1 diabetes, 2018, pp.67, 110~119
37. Vaughan, O. R., "Glucocorticoid regulation of amino acid transport in primary human trophoblast cells", J. Mol. Endocrinol, 63, pp.239~248 (2019)
38. Regazzetti, C., "Insulin induces REDD1 expression through hypoxia-inducible factor 1 activation in adipocytes", J. Biol. Chem, 285, pp.5157~5164 (2010)
39. Regazzetti, C., "Regulated in development and DNA damage responses-1(REDD1)protein contributes to insulin signaling pathway in adipocytes", PLoS ONE, 7, pp.e52154~ (2012)
40. Frost, R. A., "Regulation of REDD1 by insulinlike growth factor-I in skeletal muscle and myotubes", J. Cell. Biochem, 108, pp.1192~1202 (2009)
41. Yanagawa, Y., "Rapid induction of REDD1gene expression in macrophages in response to stress-related catecholamines", Immunol. Lett, 158, pp.109~115 (2014)
42. Saracino, P. G., "Hormonal regulation of core clock gene expression in skeletal muscle following acute aerobic exercise", Biochem. Biophys. Res. Commun, 508, pp.871~876 (2019)
43. Baida, G., "Sexual dimorphism in atrophic effects of topical glucocorticoids is driven by differential regulation of atrophogene REDD1 in male and female skin", Oncotarget, 11, pp.409~418 (2020)
44. Quigley, M., "Vitamin D modulation of mitochondrial oxidative metabolism and mTOR enforces stress adaptations and anticancer responses", JBMR, 6, pp.e10572~ (2021)
45. Lisse, T. S., "Gene targeting by the vitamin D response element binding protein reveals a role for vitamin D in osteoblast mTOR signaling", FASEB J, 25, pp.937~947 (2011)
46. Yun, S. M., "Melatonin enhances arsenic trioxide-induced cell death via sustained upregulation of Redd1 expression in breast cancer cells", Mol. Cell. Endocrinol, 422, pp.64~73 (2016)
47. Wu, Y., "REDD1 is a major target of testosterone action in preventing dexamethasone-induced muscle loss", Endocrinology, 151, pp.1050~1059 (2010)
48. Vadysirisack, D. D., "Feedback control of p53 translation by REDD1 and mTORC1 limits the p53-dependent DNA damage response", Mol. Cell. Biol, 31, pp.4356~4365 (2011)
49. Lan, Y. C., "Zoledronic acid-induced cytotoxicity through endoplasmic reticulum stress triggered REDD1-mTOR pathway in breast cancer cells", Anticancer Res, 33, pp.3807~3814 (2013)
50. Lin, L., "Arsenite induces a cell stress-response gene, RTP801, through reactive oxygen species and transcription factors Elk-1and CCAAT", enhancer-binding protein, 2005, pp.392, 93~102
51. Whitney, M. L., "ATF4 is necessary and sufficient for ER stress-induced upregulation of REDD1 expression", Biochem. Biophys. Res. Commun, 379, pp.451~455 (2009)
52. Lang, C. H., "Acute alcohol intoxication increases REDD1 in skeletal muscle", Alcohol. Clin. Exp. Res, 32, pp.796~805 (2008)
53. Jae-RyongKim, "Identification of amyloid β-peptide responsive genes by cDNA microarray technology: Involvement of RTP801 in amyloid β-peptide toxicity", Experimental and Molecular Medicine, 35(5), pp.403~411 (2003), 생화학분자생물학회
54. Ohyashiki, J. H., "The oral iron chelator deferasirox represses signaling through the mTOR in myeloid leukemia cells by enhancing expression of REDD1", Cancer Sci, 100, pp.970~977 (2009)
55. Watson, A., "Iron depletion suppresses mTORC1-directed signalling in intestinal Caco-2 cells via induction of REDD1", Cell. Signal, 28, pp.412~424 (2016)
56. Murakami, T., "Rapid induction of REDD1 expression by endurance exercise in rat skeletal muscle", Biochem. Biophys. Res. Commun, 405, pp.615~619 (2011)
57. Hayasaka, M., "Endurance exercise induces REDD1 expression and transiently decreases mTORC1 signaling in rat skeletal muscle", Physiol. Rep, 2, pp.e12254~ (2014)
58. Choi, H. S., "Age-dependent changes in the protein expression levels of Redd1 and mTOR in the gerbil hippocampus during normal aging", Mol. Med. Rep, 13, pp.2409~2414 (2016)
59. Huang, P., "Redd1 knockdown prevents doxorubicin-induced cardiac senescence", Aging, 13, pp.13788~13806 (2021)
60. Lee, D. K., "Lipopolysaccharide induction of REDD1 is mediated by two distinct CREB-dependent mechanisms in macrophages", FEBS Lett, 589, pp.2859~2865 (2015)
61. Lee, D. K., "REDD-1 aggravates endotoxin-induced inflammation via atypical NF-κB activation", FASEB J, 32, pp.4585~4599 (2018)
62. Pastor, F., "Implication of REDD1 in the activation of inflammatory pathways", Sci. Rep, 7, pp.7023~ (2017)
63. Li, P., "REDD1 knockdown protects H9c2 cells against myocardial ischemia", reperfusion injury through Akt, Nrf2 pathway-ameliorated oxidative stress : an in vitro study, pp.Biochem. Biophys. Res. Commun, 2019[DOI]
64. Cam, H., "mTORC1 signaling under hypoxic conditions is controlled by ATM-dependent phosphorylation of HIF-1α", Mol. Cell, 40, pp.509~520 (2010)
65. Desantis, A., "Che-1-induced inhibition of mTOR pathway enables stressinduced autophagy", EMBO J, 34, pp.1214~1230 (2015)
66. Cam, M., "p53", TAp63 and AKT regulate mammalian target of rapamycin complex 1(mTORC1)signaling through two independent parallel pathways in the presence of DNA damage, 2014, pp.289, 4083~4094
67. Jones, R. G., "AMP-activated protein kinase induces a p53-dependent metabolic checkpoint", Mol. Cell, 18, pp.283~293 (2005)
68. Assaily, W., "ROS-mediated p53 induction of Lpin1 regulates fatty acid oxidation in response to nutritional stress", Mol. Cell, 44, pp.491~501 (2011)
69. Jin, H. O., "Activating transcription factor 4 and CCAAT", enhancer-binding protein-β negatively regulate the mammalian target of rapamycin via Redd1expression in response to oxidative and endoplasmic reticulum stress, 2009, pp.46, 1158~1167
70. Cho, S. S., "REDD1 attenuates hepatic stellate cell activation and liver fibrosis via inhibiting of TGF-β", Smad signaling pathway, 2021, pp.176, 246~256
71. Miller, W. P., "REDD1 activates a ROSgenerating feedback loop in the retina of diabetic mice", Invest. Ophthalmol. Vis. Sci, 60, pp.2369~2379 (2019)
72. Gordon, B. S., "REDD1 induction regulates the skeletal muscle gene expression signature following acute aerobic exercise", Am. J. Physiol. Endocrinol. Metab, 313, pp.E737~E747 (2017)
73. Michel, G., "Plasma membrane translocation of REDD1 governed by GPCRs contributes to mTORC1 activation", J. Cell Sci, 127, pp.773~787 (2014)
74. Vega-Rubin-de-Celis, S., "Structural analysis and functional implications of the negative mTORC1 regulator REDD1", Biochemistry, 49, pp.2491~2501 (2010)
75. Kimball, S. R., "Rapid turnover of the mTOR complex 1(mTORC1)repressor REDD1 and activation of mTORC1 signaling following inhibition of protein synthesis", J. Biol. Chem, 283, pp.3465~3475 (2008)
76. Tan, C. Y., "mTORC1 dependent regulation of REDD1 protein stability", PLoS ONE, 8, pp.e63970~ (2013)
77. Katiyar, S., "REDD1, an inhibitor of mTOR signalling, is regulated by the CUL4A-DDB1 ubiquitin ligase", EMBO Rep, 10, pp.866~872 (2009)
78. Kim, J., "mTOR as a central hub of nutrient signalling and cell growth", Nat. Cell Biol, 21, pp.63~71 (2019)
79. Inoki, K., "TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling", Nat. Cell Biol, 4, pp.648~657 (2002)
80. Brugarolas, J., "Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1", TSC2 tumor suppressor complex, 2004, pp.18, 2893~2904
81. Cai, S. L., "Activity of TSC2 is inhibited by AKT-mediated phosphorylation and membrane partitioning", J. Cell. Biol, 173, pp.279~289 (2006)
82. Benvenuto, G., "The tuberous sclerosis-1(TSC1)gene product hamartin suppresses cell growth and augments the expression of the TSC2 product tuberin by inhibiting its ubiquitination", Oncogene, 19, pp.6306~6316 (2000)
83. Zhang, Y., "Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins", Nat. Cell Biol, 5, pp.578~581 (2003)
84. Rosner, M., "The mTOR pathway and its role in human genetic diseases", Mutat. Res, 659, pp.284~292 (2008)
85. Huang, J., "The TSC1-TSC2 complex: a molecular switchboard controlling cell growth", Biochem. J, 412, pp.179~190 (2008)
86. Manning, B. D., "Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase", akt pathway, 2002, pp.10, 151~162
87. Shaw, R. J., "Ras, PI(3)K and mTOR signalling controls tumour cell growth", Nature, 441, pp.424~430 (2006)
88. Gardino, A. K., "14-3-3 proteins as signaling integration points for cell cycle control and apoptosis", Semin. Cell Dev. Biol, 22, pp.688~695 (2011)
89. Dennis, M. D., "REDD1 enhances protein phosphatase 2A-mediated dephosphorylation of Akt to repress mTORC1signaling", Sci. Signal, 7, pp.ra68~ (2014)
90. Sun, S. C., "The non-canonical NF-κB pathway in immunity and inflammation", Nat. Rev. Immunol, 17, pp.545~558 (2017)
91. Canty, T. G., "Oxidative stress induces NF-κB nuclear translocation without degradation of IκBα", Circulation, 100, pp.II361~II364 (1999)
92. Janssens, S., "Signals from within : the DNA-damage-induced NF-κB response", Cell Death Differ, 13, pp.773~784 (2006)
93. Kriete, A., "Atypical pathways of NF-κB activation and aging", Exp. Gerontol, 44, pp.250~255 (2009)
94. Nadon, A. M., "Rtp801 suppression of epithelial mTORC1 augments endotoxin-induced lung inflammation", Am. J. Pathol, 184, pp.2382~2389 (2014)
95. Weichhart, T., "The TSC-mTOR signaling pathway regulates the innate inflammatory response", Immunity, 29, pp.565~577 (2008)
96. Hotamisligil, G. S., "Inflammation, metaflammation and immunometabolic disorders", Nature, 542, pp.177~185 (2017)
97. Saltiel, A. R., "Inflammatory mechanisms linking obesity and metabolic disease", J. Clin. Invest, 127, pp.1~4 (2017)
98. Morgan, M. J., "Crosstalk of reactive oxygen species and NF-κB signaling", Cell Res, 21, pp.103~115 (2011)
99. Jacobs, M. D., "Structure of an IκBα", NF-κB complex, 1998, pp.95, 749~758
100. Zheng, X., "The protease activity of human ATG4B is regulated by reversible oxidative modification", Autophagy, 16, pp.1838~1850 (2020)
101. Scherz-Shouval, R., "Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4", EMBO J, 26, pp.1749~1760 (2007)
102. Tanida, I., "HsAtg4B", HsApg4B, J. Biol. Chem, pp.2004, 279[DOI]
103. Gao, C., "TXNIP", Redd1 signalling and excessive autophagy : a novel mechanism of myocardial ischaemia, Cardiovasc. Res, pp.2020, 116[DOI]
104. Elgort, M. G., "Transcriptional and translational downregulation of thioredoxin interacting protein is required for metabolic reprogramming during G1", Genes Cancer, 1, pp.893~907 (2010)
105. Forrester, M. T., "Thioredoxin-interacting protein(Txnip)is a feedback regulator of S-nitrosylation", J. Biol. Chem, 284, pp.36160~36166 (2009)
106. Lee, J. M., "Control of protein stability by post-translational modifications", Nat. Commun, 14, pp.201~ (2023)
107. Zhang, P., "The ubiquitin ligase itch regulates apoptosis by targeting thioredoxin-interacting protein for ubiquitin-dependent degradation", J. Biol. Chem, 285, pp.8869~8879 (2010)
108. Singh, L. P, "Thioredoxin interacting protein(TXNIP)and pathogenesis of diabetic retinopathy", J. Clin. Exp. Ophthalmol, 5, pp.4~ (2013)
109. Rieusset, J., "The role of endoplasmic reticulum-mitochondria contact sites in the control of glucose homeostasis : an update", Cell Death Dis, 9, pp.388~ (2018)
110. Zorov, D. B., "Mitochondrial reactive oxygen species (ROS) and ROS-induced ROS release", Physiol. Rev, 94, pp.909~950 (2014)
111. Um, S. H., "Absence of S6K1 protects against age-and diet-induced obesity while enhancing insulin sensitivity", Nature, 431, pp.200~205 (2004)
112. Lee, P. L., "Raptor", mTORC1 loss in adipocytes causes progressive lipodystrophy and fatty liver disease, 2016, pp.5, 422~432
113. Ricoult, S. J., "The multifaceted role of mTORC1 in the control of lipid metabolism", EMBO Rep, 14, pp.242~251 (2013)
114. Rivera-Gonzalez, G. C., "Regulated in development and DNA damage responses 1 prevents dermal adipocyte differentiation and is required for hair cycle-dependent dermal adipose expansion", J. Invest. Dermatol, 140, pp.1698~1705 (2020)
115. Helsley, R. N., "Targeting IκB kinase β in adipocyte lineage cells for treatment of obesity and metabolic dysfunctions", Stem Cells, 34, pp.1883~1895 (2016)
116. Wang, D., "NF-κB p50 regulates C", EBPα expression and inflammatory cytokine-induced neutrophil production, 2009, pp.182, 5757~5762
117. Gordon, B. S., "Reduced REDD1 expression contributes to activation of mTORC1 following electrically induced muscle contraction", Am. J. Physiol. Endocrinol. Metab, 307, pp.E703~E711 (2014)
118. Gordon, B. S., "Nutrient-induced stimulation of protein synthesis in mouse skeletal muscle is limited by the mTORC1 repressor REDD1", J. Nutr, 145, pp.708~713 (2015)
119. Nissinen, T. A., "Systemic blockade of ACVR2B ligands prevents chemotherapy-induced muscle wasting by restoring muscle protein synthesis without affecting oxidative capacity or atrogenes", Sci. Rep, 6, pp.32695~ (2016)
120. Hain, B. A., "Loss of REDD1 prevents chemotherapyinduced muscle atrophy and weakness in mice", J. Cachexia Sarcopenia Muscle, 12, pp.1597~1612 (2021)
121. Shimizu, N., "Crosstalk between glucocorticoid receptor and nutritional sensor mTOR in skeletal muscle", Cell Metab, 13, pp.170~182 (2011)
122. Hosokawa, N., "Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy", Mol. Biol. Cell, 20, pp.1981~1991 (2009)
123. Troncoso, R., "Dexamethasone-induced autophagy mediates muscle atrophy through mitochondrial clearance", Cell Cycle, 13, pp.2281~2295 (2014)
124. Fry, C. S., "Aging impairs contraction-induced human skeletal muscle mTORC1 signaling and protein synthesis", Skelet. Muscle, 1, pp.11~ (2011)
125. Francaux, M., "Aging reduces the activation of the mTORC1 pathway after resistance exercise and protein intake in human skeletal muscle : Potential role of REDD1 and impaired anabolic sensitivity", Nutrients, 8, pp.47~ (2016)
126. Hotamisligil, G. S., "Adipose expression of tumor necrosis factor-α: direct role in obesity-linked insulin resistance", Science, 259, pp.87~91 (1993)
127. Yuan, M., "Reversal of obesity-and diet-induced insulin resistance with salicylates or targeted disruption of Ikkβ", Science, 293, pp.1673~1677 (2001)
128. Arkan, M. C., "IKK-β links inflammation to obesity-induced insulin resistance", Nat. Med, 11, pp.191~198 (2005)
129. Hundal, R. S., "Mechanism by which high-dose aspirin improves glucose metabolism in type 2 diabetes", J. Clin. Invest, 109, pp.1321~1326 (2002)
130. Han, M. S., "JNK expression by macrophages promotes obesity-induced insulin resistance and inflammation", Science, 339, pp.218~222 (2013)
131. Peng, J., "IRS posttranslational modifications in regulating insulin signaling", J. Mol. Endocrinol, 60, pp.R1~R8 (2018)
132. Williamson, D. L., "Aberrant REDD1-mTORC1 responses to insulin in skeletal muscle from Type 2 diabetics", Am. J. Physiol. Regul. Integr. Comp. Physiol, 309, pp.R855~R863 (2015)
133. Osaadon, P., "A review of anti-VEGF agents for proliferative diabetic retinopathy", Eye, 28, pp.510~520 (2014)
134. Nguyen, Q. D., "Phase 1 dose-escalation study of a siRNA targeting the RTP801gene in age-related macular degeneration patients", Eye, 26, pp.1099~1105 (2012)
135. Nguyen, Q. D., "Dose-ranging evaluation of intravitreal siRNA PF-04523655for diabetic macular edema(the DEGAS study)", Invest. Ophthalmol. Vis. Sci, 53, pp.7666~7674 (2012)
136. Maiese, K., "Targeting molecules to medicine with mTOR, autophagy and neurodegenerative disorders", Br. J. Clin. Pharmacol, 82, pp.1245~1266 (2016)
137. Bové, J., "Fighting neurodegeneration with rapamycin : mechanistic insights", Nat. Rev. Neurosci, 12, pp.437~452 (2011)
138. Ravikumar, B., "Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease", Nat. Genet, 36, pp.585~595 (2004)
139. Canal, M., "RTP801", REDD1 : a stress coping regulator that turns into a troublemaker in neurodegenerative disorders, 2014, pp.8, 313~
140. de Vries, P. J., "TSC-associated neuropsychiatric disorders(TAND) : findings from the TOSCA natural history study", Orphanet. J. Rare. Dis, 13, pp.157~ (2018)
141. Yi, J. H., "REDD1 is involved in amyloid β-induced synaptic dysfunction and memory impairment", Int. J. Mol. Sci, 21, pp.9482~ (2020)
142. Yang, P. F., "RTP801 is a critical factor in the neurodegeneration process of A53T α-synuclein in a mouse model of Parkinson’s disease under chronic restraint stress", Br. J. Pharmacol, 175, pp.590~605 (2018)
143. Damjanac, M., "PKR, a cognitive decline biomarker, can regulate translation via two consecutive molecular targets p53 and Redd1 in lymphocytes of AD patients", J. Cell. Mol. Med, 13, pp.1823~1832 (2009)
144. Pérez-Sisqués, L., "RTP801", REDD1 contributes to neuroinflammation severity and memory impairments in Alzheimer’s disease, 2021, pp.12, 616~
145. Malagelada, C., "RTP801 is elevated in Parkinson brain substantia nigral neurons and mediates death in cellular models of Parkinson′s disease by a mechanism involving mammalian target of rapamycin inactivation", J. Neurosci, 26, pp.9996~10005 (2006)
146. Malagelada, C., "RTP801 is induced in Parkinson′s disease and mediates neuron death by inhibiting Akt phosphorylation", activation, 2008, pp.28, 14363~14371
147. Nasoohi, S., "Thioredoxin-interacting protein(TXNIP)in cerebrovascular and neurodegenerative diseases : regulation and implication", Mol. Neurobiol, 55, pp.7900~7920 (2018)
148. Glass, C. K., "Mechanisms underlying inflammation in neurodegeneration", Cell, 140, pp.918~934 (2010)
149. Easton, J. B, "mTOR and cancer therapy", Oncogene, 25, pp.6436~6446 (2006)
150. Qiao, S., "REDD1 loss reprograms lipid metabolism to drive progression of RAS mutant tumors", Genes Dev, 34, pp.751~766 (2020)
151. Ho, D. W. H., "TSC1", 2 mutations define a molecular subset of HCC with aggressive behaviour and treatment implication, 2017, pp.66, 1496~1506
152. Chang, B., "Overexpression of the recently identified oncogene REDD1correlates with tumor progression and is an independent unfavorable prognostic factor for ovarian carcinoma", Diagn. Pathol, 13, pp.87~ (2018)
153. Feng, Y., "REDD1 overexpression in oral squamous cell carcinoma may predict poor prognosis and correlates with high microvessel density", Oncol. Lett, 19, pp.431~441 (2020)
154. Britto, F. A., "Is REDD1 a metabolic double agent? Lessons from physiology and pathology", Am. J. Physiol. Cell. Physiol, 319, pp.C807~C824 (2020)
155. Zhidkova, E. M., "Nutritional sensor REDD1 in cancer and inflammation : friend or foe? Int", J. Mol. Sci, 23, pp.9686~ (2022)
156. Pinto, J. A., "In silico evaluation of DNA Damage Inducible Transcript 4 gene(DDIT4)as prognostic biomarker in several malignancies", Sci. Rep, 7, pp.1526~ (2017)
157. Gil, Z., "Crosstalk between macrophages and endothelial cells in the tumor microenvironment", Mol. Ther, 29, pp.895~896 (2021)
158. Minsik Park, "Low-dose metronomic doxorubicin inhibits mobilization and differentiation of endothelial progenitor cells through REDD1-mediated VEGFR-2 downregulation", BMB Reports, 54(9), pp.470~475 (2021), 생화학분자생물학회
159. Hou, X., "Blocking the REDD1", TXNIP axis ameliorates LPSinduced vascular endothelial cell injury through repressing oxidative stress and apoptosis, 2019, pp.316, C104~C110
160. Reuschel, E. L., "REDD1 is essential for optimal T cell proliferation and survival", PLoS ONE, 10, pp.e0136323~ (2015)
161. Clarke, A. J., "Autophagy is activated in systemic lupus erythematosus and required for plasmablast development", Ann. Rheum. Dis, 74, pp.912~920 (2015)
162. Frangou, E., "REDD1", autophagy pathway promotes thromboinflammation and fibrosis in human systemic lupus erythematosus(SLE)through NETs decorated with tissue factor(TF)and interleukin-17A(IL-17A), 2019, pp.78, 238~248
163. Chrysanthopoulou, A., "REDD1", autophagy-driven NETosis promotes IL-1β-mediated inflammation in active ulcerative colitis, 2018, pp.12, S125~S126
164. Goldring, M. B., "Osteoarthritis and cartilage : the role of cytokines", Curr. Rheumatol. Rep, 2, pp.459~465 (2000)
165. Alvarez-Garcia, O., "Suppression of REDD1 in osteoarthritis cartilage, a novel mechanism for dysregulated mTOR signaling and defective autophagy", Osteoarthr. Cartil, 24, pp.1639~1647 (2016)