메뉴 건너뛰기




Volumn 1, Issue 4, 2013, Pages 239-245

Autophagy Modulation in Disease Therapy: Where Do We Stand?

Author keywords

Alzheimer s disease; Autophagy; Cancer; Disease treatment; Ischemia reperfusion; Neurodegeneration; Neuropathology; Parkinson s disease; Pharmacological therapy; Stroke

Indexed keywords


EID: 84992225972     PISSN: None     EISSN: 2167485X     Source Type: Journal    
DOI: 10.1007/s40139-013-0032-9     Document Type: Review
Times cited : (13)

References (67)
  • 1
    • 84874529463 scopus 로고    scopus 로고
    • It’s a cell-eat-cell world: autophagy and phagocytosis
    • PID: 23369575, COI: 1:CAS:528:DC%2BC3sXivFyrtLk%3D
    • Oczypok E, Oury T, Chu C (2013) It’s a cell-eat-cell world: autophagy and phagocytosis. Am J Pathol 182(3):612–622
    • (2013) Am J Pathol , vol.182 , Issue.3 , pp. 612-622
    • Oczypok, E.1    Oury, T.2    Chu, C.3
  • 3
    • 84878943669 scopus 로고    scopus 로고
    • The mechanism and physiological function of macroautophagy
    • PID: 23774579, COI: 1:CAS:528:DC%2BC3sXhtFyhurfJ
    • Klionsky D, Codogno P (2013) The mechanism and physiological function of macroautophagy. J Innate Immun 5(5):427–433
    • (2013) J Innate Immun , vol.5 , Issue.5 , pp. 427-433
    • Klionsky, D.1    Codogno, P.2
  • 4
    • 84859161154 scopus 로고    scopus 로고
    • Microautophagy: lesser-known self-eating
    • PID: 22080117, COI: 1:CAS:528:DC%2BC38Xjslehs7o%3D
    • Li W-w, Li J, Bao J-k (2012) Microautophagy: lesser-known self-eating. Cell Mol Life Sci 69(7):1125–1136
    • (2012) Cell Mol Life Sci , vol.69 , Issue.7 , pp. 1125-1136
    • Li, W.-W.1    Li, J.2    Bao, J.-K.3
  • 5
    • 79954422997 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy in protein quality control
    • PID: 21094035, COI: 1:CAS:528:DC%2BC3MXkvFamtLc%3D
    • Arias E, Cuervo A (2011) Chaperone-mediated autophagy in protein quality control. Curr Opin Cell Biol 23(2):184–189
    • (2011) Curr Opin Cell Biol , vol.23 , Issue.2 , pp. 184-189
    • Arias, E.1    Cuervo, A.2
  • 6
    • 84884607950 scopus 로고    scopus 로고
    • Mitochondrial autophagy
    • Thomas R, Gustafsson A (2013) Mitochondrial autophagy. Circ J 77(10):2449–2454
    • (2013) Circ J , vol.77 , Issue.10 , pp. 2449-2454
    • Thomas, R.1    Gustafsson, A.2
  • 7
    • 84873436219 scopus 로고    scopus 로고
    • Autophagy: emerging roles in lipid homeostasis and metabolic control
    • PID: 23274236, COI: 1:CAS:528:DC%2BC3sXjtFWgtLg%3D
    • Christian P, Sacco J, Adeli K (2013) Autophagy: emerging roles in lipid homeostasis and metabolic control. Biochim Biophys Acta 1831(4):819–824
    • (2013) Biochim Biophys Acta , vol.1831 , Issue.4 , pp. 819-824
    • Christian, P.1    Sacco, J.2    Adeli, K.3
  • 8
    • 84881030026 scopus 로고    scopus 로고
    • Roles of autophagy in elimination of intracellular bacterial pathogens
    • Jo E-K et al (2013) Roles of autophagy in elimination of intracellular bacterial pathogens. Frontiers Immunol 4:97
    • (2013) Frontiers Immunol , vol.4 , pp. 97
    • Jo, E.-K.1
  • 9
    • 38949108670 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes
    • PID: 18188003, COI: 1:CAS:528:DC%2BD1cXksFGrtLg%3D
    • Klionsky DJ et al (2008) Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes. Autophagy 4(2):151–175
    • (2008) Autophagy , vol.4 , Issue.2 , pp. 151-175
    • Klionsky, D.J.1
  • 10
    • 84862295360 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy
    • PID: 22966490, COI: 1:CAS:528:DC%2BC38Xht1art7zK
    • •• Klionsky D et al (2012) Guidelines for the use and interpretation of assays for monitoring autophagy. Autophagy 8(4):445–544. This publication is especially significant, as it provides useful guidelines developed collaboratively for anyone considering, conducting, or reviewing autophagy research. The author would go as far as suggesting that it be required reading.
    • (2012) Autophagy , vol.8 , Issue.4 , pp. 445-544
    • Klionsky, D.1
  • 11
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • PID: 16625204, COI: 1:CAS:528:DC%2BD28XlvVGlsbc%3D
    • Hara T et al (2006) Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441(7095):885–889
    • (2006) Nature , vol.441 , Issue.7095 , pp. 885-889
    • Hara, T.1
  • 12
    • 33847295164 scopus 로고    scopus 로고
    • Autophagy and cell death
    • PID: 17338918, COI: 1:CAS:528:DC%2BD2sXmtFKlsbY%3D
    • Gozuacik D, Kimchi A (2007) Autophagy and cell death. Curr Top Dev Biol 78:217–245
    • (2007) Curr Top Dev Biol , vol.78 , pp. 217-245
    • Gozuacik, D.1    Kimchi, A.2
  • 13
    • 79956224883 scopus 로고    scopus 로고
    • Targeting autophagy during cancer therapy to improve clinical outcomes
    • PID: 21440002, COI: 1:CAS:528:DC%2BC3MXmsVyltLc%3D
    • Levy JM, Thorburn A (2011) Targeting autophagy during cancer therapy to improve clinical outcomes. Pharmacol Ther 131(1):130–141
    • (2011) Pharmacol Ther , vol.131 , Issue.1 , pp. 130-141
    • Levy, J.M.1    Thorburn, A.2
  • 14
    • 84884812963 scopus 로고    scopus 로고
    • Targeting autophagy as a potential therapeutic approach for melanoma therapy
    • Liu H., Z. He, H.-U. Simon (2013) Targeting autophagy as a potential therapeutic approach for melanoma therapy. Seminars in cancer biology
    • (2013) Seminars in Cancer Biology
    • Liu, H.Z.1    Hesimon, H.-U.2
  • 16
    • 84882781441 scopus 로고    scopus 로고
    • Pazopanib versus sunitinib in metastatic renal-cell carcinoma
    • PID: 23964934, COI: 1:CAS:528:DC%2BC3sXhtlCrsrbP
    • Motzer R et al (2013) Pazopanib versus sunitinib in metastatic renal-cell carcinoma. N Engl J Med 369(8):722–731
    • (2013) N Engl J Med , vol.369 , Issue.8 , pp. 722-731
    • Motzer, R.1
  • 17
    • 77949890945 scopus 로고    scopus 로고
    • Pazopanib in locally advanced or metastatic renal cell carcinoma: results of a randomized phase III trial
    • PID: 20100962, COI: 1:CAS:528:DC%2BC3cXktF2lt78%3D
    • Sternberg C et al (2010) Pazopanib in locally advanced or metastatic renal cell carcinoma: results of a randomized phase III trial. J Clin Oncol 28(6):1061–1068
    • (2010) J Clin Oncol , vol.28 , Issue.6 , pp. 1061-1068
    • Sternberg, C.1
  • 18
    • 84861098484 scopus 로고    scopus 로고
    • Pazopanib for metastatic soft-tissue sarcoma (PALETTE): a randomised, double-blind, placebo-controlled phase 3 trial
    • PID: 22595799
    • van der Graaf W et al (2012) Pazopanib for metastatic soft-tissue sarcoma (PALETTE): a randomised, double-blind, placebo-controlled phase 3 trial. Lancet 379(9829):1879–1886
    • (2012) Lancet , vol.379 , Issue.9829 , pp. 1879-1886
    • van der Graaf, W.1
  • 19
    • 78650353327 scopus 로고    scopus 로고
    • An indirect comparison analysis of pazopanib versus other agents in metastatic renal cell carcinoma (mRCC)
    • McCann L et al (2010) An indirect comparison analysis of pazopanib versus other agents in metastatic renal cell carcinoma (mRCC). J Clin Oncol 28(15 Suppl):e15128
    • (2010) J Clin Oncol , vol.28
    • McCann, L.1
  • 20
    • 84883156825 scopus 로고    scopus 로고
    • Pazopanib and sunitinib trigger autophagic and non-autophagic death of bladder tumour cells
    • Santoni M et al (2013) Pazopanib and sunitinib trigger autophagic and non-autophagic death of bladder tumour cells. Br J Cancer. doi:10.1038/bjc.2013.420
    • (2013) Br J Cancer
    • Santoni, M.1
  • 21
    • 76249108700 scopus 로고    scopus 로고
    • Cathepsin B-mediated autophagy flux facilitates the anthrax toxin receptor 2-mediated delivery of anthrax lethal factor into the cytoplasm
    • PID: 19858192, COI: 1:CAS:528:DC%2BC3cXjsVSqtg%3D%3D
    • Ha S-D et al (2010) Cathepsin B-mediated autophagy flux facilitates the anthrax toxin receptor 2-mediated delivery of anthrax lethal factor into the cytoplasm. J Biol Chem 285(3):2120–2129
    • (2010) J Biol Chem , vol.285 , Issue.3 , pp. 2120-2129
    • Ha, S.-D.1
  • 22
    • 84882468371 scopus 로고    scopus 로고
    • Synthetic polyamines activating autophagy: effects on cancer cell death
    • Minarini A et al (2013) Synthetic polyamines activating autophagy: effects on cancer cell death. Eur J Med Chem 67C:359–366
    • (2013) Eur J Med Chem , vol.67C , pp. 359-366
    • Minarini, A.1
  • 23
    • 33745727948 scopus 로고    scopus 로고
    • Initiation of apoptosis and autophagy by photodynamic therapy
    • PID: 16615135
    • Kessel D, Vicente M, Reiners J (2006) Initiation of apoptosis and autophagy by photodynamic therapy. Lasers Surg Med 38(5):482–488
    • (2006) Lasers Surg Med , vol.38 , Issue.5 , pp. 482-488
    • Kessel, D.1    Vicente, M.2    Reiners, J.3
  • 24
    • 84868588163 scopus 로고    scopus 로고
    • Direct and indirect photodynamic therapy effects on the cellular and molecular components of the tumor microenvironment
    • PID: 23046998, COI: 1:CAS:528:DC%2BC38XhvVKqurzN
    • Milla Sanabria L et al (2013) Direct and indirect photodynamic therapy effects on the cellular and molecular components of the tumor microenvironment. Biochim Biophys Acta 1835(1):36–45
    • (2013) Biochim Biophys Acta , vol.1835 , Issue.1 , pp. 36-45
    • Milla Sanabria, L.1
  • 25
    • 84872776017 scopus 로고    scopus 로고
    • Photodynamic treatment induces cell death by apoptosis or autophagy depending on the melanin content in two B16 melanoma cell lines
    • PID: 23242333, COI: 1:CAS:528:DC%2BC3sXktFSks7s%3D
    • Sparsa A et al (2013) Photodynamic treatment induces cell death by apoptosis or autophagy depending on the melanin content in two B16 melanoma cell lines. Oncol Rep 29(3):1196–1200
    • (2013) Oncol Rep , vol.29 , Issue.3 , pp. 1196-1200
    • Sparsa, A.1
  • 26
    • 84876477696 scopus 로고    scopus 로고
    • The HSP70 and autophagy inhibitor pifithrin-μ enhances the antitumor effects of TRAIL on human pancreatic cancer
    • PID: 23371857, COI: 1:CAS:528:DC%2BC3sXls12ru7c%3D
    • Monma H et al (2013) The HSP70 and autophagy inhibitor pifithrin-μ enhances the antitumor effects of TRAIL on human pancreatic cancer. Mol Cancer Ther 12(4):341–351
    • (2013) Mol Cancer Ther , vol.12 , Issue.4 , pp. 341-351
    • Monma, H.1
  • 27
    • 0030852889 scopus 로고    scopus 로고
    • HSP70 binding sites in the tumor suppressor protein p53
    • PID: 9235949, COI: 1:CAS:528:DyaK2sXltFSmsbc%3D
    • Fourie A et al (1997) HSP70 binding sites in the tumor suppressor protein p53. J Biol Chem 272(31):19471–19479
    • (1997) J Biol Chem , vol.272 , Issue.31 , pp. 19471-19479
    • Fourie, A.1
  • 28
    • 70349768075 scopus 로고    scopus 로고
    • A small molecule inhibitor of inducible heat shock protein 70
    • PID: 19818706, COI: 1:CAS:528:DC%2BD1MXhsVChtLnF
    • Leu J et al (2009) A small molecule inhibitor of inducible heat shock protein 70. Mol Cell 36(1):15–27
    • (2009) Mol Cell , vol.36 , Issue.1 , pp. 15-27
    • Leu, J.1
  • 29
    • 79960694363 scopus 로고    scopus 로고
    • HSP70 inhibition by the small-molecule 2-phenylethynesulfonamide impairs protein clearance pathways in tumor cells
    • PID: 21636681, COI: 1:CAS:528:DC%2BC3MXptVOktbw%3D
    • Leu J et al (2011) HSP70 inhibition by the small-molecule 2-phenylethynesulfonamide impairs protein clearance pathways in tumor cells. Mol Cancer Res 9(7):936–947
    • (2011) Mol Cancer Res , vol.9 , Issue.7 , pp. 936-947
    • Leu, J.1
  • 30
    • 84894065670 scopus 로고    scopus 로고
    • Regulation of HA14-1 mediated oxidative stress, toxic response, and autophagy by curcumin to enhance apoptotic activity in human embryonic kidney cells
    • Ranjan K et al (2013) Regulation of HA14-1 mediated oxidative stress, toxic response, and autophagy by curcumin to enhance apoptotic activity in human embryonic kidney cells. BioFactors (Oxford, England). doi:10.1002/biof.1098
    • (2013) BioFactors (Oxford, England)
    • Ranjan, K.1
  • 31
    • 34347238938 scopus 로고    scopus 로고
    • Evidence that curcumin suppresses the growth of malignant gliomas in vitro and in vivo through induction of autophagy: role of Akt and extracellular signal-regulated kinase signaling pathways
    • PID: 17395690, COI: 1:CAS:528:DC%2BD2sXnsVyjs7Y%3D
    • Aoki H et al (2007) Evidence that curcumin suppresses the growth of malignant gliomas in vitro and in vivo through induction of autophagy: role of Akt and extracellular signal-regulated kinase signaling pathways. Mol Pharmacol 72(1):29–39
    • (2007) Mol Pharmacol , vol.72 , Issue.1 , pp. 29-39
    • Aoki, H.1
  • 32
    • 33749505836 scopus 로고    scopus 로고
    • Efficacy and safety of sunitinib in patients with advanced gastrointestinal stromal tumour after failure of imatinib: a randomised controlled trial
    • PID: 17046465, COI: 1:CAS:528:DC%2BD28XhtVOrtL%2FL
    • Demetri G et al (2006) Efficacy and safety of sunitinib in patients with advanced gastrointestinal stromal tumour after failure of imatinib: a randomised controlled trial. Lancet 368(9544):1329–1338
    • (2006) Lancet , vol.368 , Issue.9544 , pp. 1329-1338
    • Demetri, G.1
  • 33
    • 33846181370 scopus 로고    scopus 로고
    • Sunitinib versus interferon alfa in metastatic renal-cell carcinoma
    • PID: 17215529, COI: 1:CAS:528:DC%2BD2sXksVGqsw%3D%3D
    • Motzer R et al (2007) Sunitinib versus interferon alfa in metastatic renal-cell carcinoma. N Engl J Med 356(2):115–124
    • (2007) N Engl J Med , vol.356 , Issue.2 , pp. 115-124
    • Motzer, R.1
  • 34
    • 82555189379 scopus 로고    scopus 로고
    • Lysosomal sequestration of sunitinib: a novel mechanism of drug resistance
    • PID: 21980135, COI: 1:CAS:528:DC%2BC3MXhsFCmtrjM
    • Gotink K et al (2011) Lysosomal sequestration of sunitinib: a novel mechanism of drug resistance. Clin Cancer Res 17(23):7337–7346
    • (2011) Clin Cancer Res , vol.17 , Issue.23 , pp. 7337-7346
    • Gotink, K.1
  • 35
    • 84860725460 scopus 로고    scopus 로고
    • Cationic amphiphilic drugs cause a marked expansion of apparent lysosomal volume: implications for an intracellular distribution-based drug interaction
    • PID: 22449202, COI: 1:CAS:528:DC%2BC38XksVymt7Y%3D
    • Funk R, Krise J (2012) Cationic amphiphilic drugs cause a marked expansion of apparent lysosomal volume: implications for an intracellular distribution-based drug interaction. Mol Pharm 9(5):1384–1395
    • (2012) Mol Pharm , vol.9 , Issue.5 , pp. 1384-1395
    • Funk, R.1    Krise, J.2
  • 36
    • 79952037605 scopus 로고    scopus 로고
    • A high content screening assay for identifying lysosomotropic compounds
    • COI: 1:CAS:528:DC%2BC3MXjsFahsb4%3D
    • Nadanaciva S et al (2011) A high content screening assay for identifying lysosomotropic compounds. Toxicol Vitro 25(3):715–723
    • (2011) Toxicol Vitro , vol.25 , Issue.3 , pp. 715-723
    • Nadanaciva, S.1
  • 37
    • 84858004799 scopus 로고    scopus 로고
    • Ischemic tolerance in the brain: endogenous adaptive machinery against ischemic stress
    • PID: 22302606, COI: 1:CAS:528:DC%2BC38XhvVShtrw%3D
    • Kitagawa K (2012) Ischemic tolerance in the brain: endogenous adaptive machinery against ischemic stress. J Neurosci Res 90(5):1043–1054
    • (2012) J Neurosci Res , vol.90 , Issue.5 , pp. 1043-1054
    • Kitagawa, K.1
  • 38
    • 84875232070 scopus 로고    scopus 로고
    • Tsc1 (hamartin) confers neuroprotection against ischemia by inducing autophagy
    • PID: 23435171, COI: 1:CAS:528:DC%2BC3sXivFyiu7g%3D
    • Papadakis M et al (2013) Tsc1 (hamartin) confers neuroprotection against ischemia by inducing autophagy. Nat Med 19(3):351–357
    • (2013) Nat Med , vol.19 , Issue.3 , pp. 351-357
    • Papadakis, M.1
  • 39
    • 78449241484 scopus 로고    scopus 로고
    • Resveratrol inhibits mTOR signaling by promoting the interaction between mTOR and DEPTOR
    • PID: 20851890, COI: 1:CAS:528:DC%2BC3cXhsVWgsr%2FP
    • Liu M et al (2010) Resveratrol inhibits mTOR signaling by promoting the interaction between mTOR and DEPTOR. J Biol Chem 285(47):36387–36394
    • (2010) J Biol Chem , vol.285 , Issue.47 , pp. 36387-36394
    • Liu, M.1
  • 40
    • 84888800151 scopus 로고    scopus 로고
    • Resveratrol modulates autophagy and NF-κB activity in a murine model for treating non-alcoholic fatty liver disease
    • Li L et al (2013) Resveratrol modulates autophagy and NF-κB activity in a murine model for treating non-alcoholic fatty liver disease. Food Chem Toxicol. doi:10.1016/j.fct.2013.08.036
    • (2013) Food Chem Toxicol
    • Li, L.1
  • 41
    • 33747781747 scopus 로고    scopus 로고
    • Inflammation in stroke and focal cerebral ischemia
    • PID: 16935624
    • Huang J, Upadhyay U, Tamargo R (2006) Inflammation in stroke and focal cerebral ischemia. Surg Neurol 66(3):232–245
    • (2006) Surg Neurol , vol.66 , Issue.3 , pp. 232-245
    • Huang, J.1    Upadhyay, U.2    Tamargo, R.3
  • 42
    • 84868709247 scopus 로고    scopus 로고
    • Tetracycline inhibits local inflammation induced by cerebral ischemia via modulating autophagy
    • Jiang Y et al (2012) Tetracycline inhibits local inflammation induced by cerebral ischemia via modulating autophagy. PloS One. doi:10.1371/journal.pone.0048672
    • (2012) PloS One
    • Jiang, Y.1
  • 43
    • 77952513645 scopus 로고    scopus 로고
    • Inflammatory mechanisms in ischemic stroke: role of inflammatory cells
    • PID: 20130219, COI: 1:CAS:528:DC%2BC3cXmvVCht74%3D
    • Jin R, Yang G, Li G (2010) Inflammatory mechanisms in ischemic stroke: role of inflammatory cells. J Leukoc Biol 87(5):779–789
    • (2010) J Leukoc Biol , vol.87 , Issue.5 , pp. 779-789
    • Jin, R.1    Yang, G.2    Li, G.3
  • 44
    • 33646591929 scopus 로고    scopus 로고
    • 15d-Prostaglandin J2 Protects Brain From Ischemia-Reperfusion Injury
    • PID: 16385084
    • Lin TN (2005) 15d-Prostaglandin J2 Protects Brain From Ischemia-Reperfusion Injury. Arterioscler Thromb Vasc Biol 26(3):481–487
    • (2005) Arterioscler Thromb Vasc Biol , vol.26 , Issue.3 , pp. 481-487
    • Lin, T.N.1
  • 45
    • 62649096776 scopus 로고    scopus 로고
    • Ligand-activated peroxisome proliferator-activated receptor-gamma protects against ischemic cerebral infarction and neuronal apoptosis by 14-3-3 epsilon upregulation
    • PID: 19221220, COI: 1:CAS:528:DC%2BD1MXitF2js7g%3D
    • Wu J-S et al (2009) Ligand-activated peroxisome proliferator-activated receptor-gamma protects against ischemic cerebral infarction and neuronal apoptosis by 14-3-3 epsilon upregulation. Circulation 119(8):1124–1134
    • (2009) Circulation , vol.119 , Issue.8 , pp. 1124-1134
    • Wu, J.-S.1
  • 46
    • 79955469799 scopus 로고    scopus 로고
    • The anti-inflammatory prostaglandin 15d-PGJ2 and its nuclear receptor PPARgamma are decreased in schizophrenia
    • PID: 21334179
    • Martínez-Gras I et al (2011) The anti-inflammatory prostaglandin 15d-PGJ2 and its nuclear receptor PPARgamma are decreased in schizophrenia. Schizophr Res 128(1–3):15–22
    • (2011) Schizophr Res , vol.128 , Issue.1-3 , pp. 15-22
    • Martínez-Gras, I.1
  • 47
    • 84872845566 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-γ agonist 15d-prostaglandin J2 mediates neuronal autophagy after cerebral ischemia-reperfusion injury
    • Xu F et al (2013) Peroxisome proliferator-activated receptor-γ agonist 15d-prostaglandin J2 mediates neuronal autophagy after cerebral ischemia-reperfusion injury. PloS One. doi:10.1371/journal.pone.0055080
    • (2013) PloS One
    • Xu, F.1
  • 48
    • 84857058225 scopus 로고    scopus 로고
    • Control of autophagy as a therapy for neurodegenerative disease
    • COI: 1:CAS:528:DC%2BC38XitFGru7c%3D
    • Harris H, Rubinsztein D (2012) Control of autophagy as a therapy for neurodegenerative disease. Nat Rev Neurol 8(2):108–117
    • (2012) Nat Rev Neurol , vol.8 , Issue.2 , pp. 108-117
    • Harris, H.1    Rubinsztein, D.2
  • 49
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein
    • PID: 17182613, COI: 1:CAS:528:DC%2BD2sXhvVait7o%3D
    • Sarkar S et al (2007) Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein. J Biol Chem 282(8):5641–5652
    • (2007) J Biol Chem , vol.282 , Issue.8 , pp. 5641-5652
    • Sarkar, S.1
  • 50
    • 4644236078 scopus 로고    scopus 로고
    • Role of trehalose phosphate synthase and trehalose during hypoxia: from flies to mammals
    • PID: 15299033, COI: 1:CAS:528:DC%2BD2cXovF2kur0%3D
    • Chen Q, Haddad G (2004) Role of trehalose phosphate synthase and trehalose during hypoxia: from flies to mammals. J Exp Biol 207(Pt 18):3125–3129
    • (2004) J Exp Biol , vol.207 , pp. 3125-3129
    • Chen, Q.1    Haddad, G.2
  • 51
    • 65249103439 scopus 로고    scopus 로고
    • Autophagy induction by trehalose counteracts cellular prion infection
    • PID: 19182537, COI: 1:CAS:528:DC%2BD1MXnvVyrsrw%3D
    • Aguib Y et al (2009) Autophagy induction by trehalose counteracts cellular prion infection. Autophagy 5(3):361–369
    • (2009) Autophagy , vol.5 , Issue.3 , pp. 361-369
    • Aguib, Y.1
  • 52
    • 84862285881 scopus 로고    scopus 로고
    • Autophagic degradation of tau in primary neurons and its enhancement by trehalose
    • PID: 22169203
    • Krüger U et al (2012) Autophagic degradation of tau in primary neurons and its enhancement by trehalose. Neurobiol Aging 33(10):2291–2305
    • (2012) Neurobiol Aging , vol.33 , Issue.10 , pp. 2291-2305
    • Krüger, U.1
  • 53
    • 84869386716 scopus 로고    scopus 로고
    • Stimulation of autophagy is neuroprotective in a mouse model of human tauopathy
    • PID: 22874558, COI: 1:CAS:528:DC%2BC3sXivFOjtrk%3D
    • Schaeffer V, Goedert M (2012) Stimulation of autophagy is neuroprotective in a mouse model of human tauopathy. Autophagy 8(11):1686–1687
    • (2012) Autophagy , vol.8 , Issue.11 , pp. 1686-1687
    • Schaeffer, V.1    Goedert, M.2
  • 54
    • 80255122786 scopus 로고    scopus 로고
    • Convergent pathogenic pathways in Alzheimer’s and Huntington’s diseases: shared targets for drug development
    • COI: 1:CAS:528:DC%2BC3MXhtlGhtbbJ
    • Ehrnhoefer D, Wong B, Hayden M (2011) Convergent pathogenic pathways in Alzheimer’s and Huntington’s diseases: shared targets for drug development. Nat Rev Drug Discovery 10(11):853–867
    • (2011) Nat Rev Drug Discovery , vol.10 , Issue.11 , pp. 853-867
    • Ehrnhoefer, D.1    Wong, B.2    Hayden, M.3
  • 55
    • 84883323560 scopus 로고    scopus 로고
    • Mammalian target of rapamycin (mTOR) pathways in neurological diseases
    • PID: 23644232
    • Wong M (2013) Mammalian target of rapamycin (mTOR) pathways in neurological diseases. Biomed J 36(2):40–50
    • (2013) Biomed J , vol.36 , Issue.2 , pp. 40-50
    • Wong, M.1
  • 56
    • 51549086469 scopus 로고    scopus 로고
    • Neuroprotection of rapamycin in lactacystin-induced neurodegeneration via autophagy enhancement
    • PID: 18640276, COI: 1:CAS:528:DC%2BD1cXhtFantbjF
    • Pan T et al (2008) Neuroprotection of rapamycin in lactacystin-induced neurodegeneration via autophagy enhancement. Neurobiol Dis 32(1):16–25
    • (2008) Neurobiol Dis , vol.32 , Issue.1 , pp. 16-25
    • Pan, T.1
  • 57
    • 25444483066 scopus 로고    scopus 로고
    • Lithium induces autophagy by inhibiting inositol monophosphatase
    • PID: 16186256, COI: 1:CAS:528:DC%2BD2MXhtVKnsbvP
    • Sarkar S et al (2005) Lithium induces autophagy by inhibiting inositol monophosphatase. J Cell Biol 170(7):1101–1111
    • (2005) J Cell Biol , vol.170 , Issue.7 , pp. 1101-1111
    • Sarkar, S.1
  • 58
    • 84868687820 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 inhibition promotes lysosomal biogenesis and autophagic degradation of the amyloid-β precursor protein
    • PID: 22927642, COI: 1:CAS:528:DC%2BC38Xhs1SiurzL
    • Parr C et al (2012) Glycogen synthase kinase 3 inhibition promotes lysosomal biogenesis and autophagic degradation of the amyloid-β precursor protein. Mol Cell Biol 32(21):4410–4418
    • (2012) Mol Cell Biol , vol.32 , Issue.21 , pp. 4410-4418
    • Parr, C.1
  • 59
    • 84874638938 scopus 로고    scopus 로고
    • Prions, prionoids and pathogenic proteins in Alzheimer disease
    • PID: 23208281, COI: 1:CAS:528:DC%2BC3sXksFWku7o%3D
    • Ashe K, Aguzzi A (2013) Prions, prionoids and pathogenic proteins in Alzheimer disease. Prion 7(1):55–59
    • (2013) Prion , vol.7 , Issue.1 , pp. 55-59
    • Ashe, K.1    Aguzzi, A.2
  • 60
    • 84876818146 scopus 로고    scopus 로고
    • Unique drug screening approach for prion diseases identifies tacrolimus and astemizole as antiprion agents
    • PID: 23576755, COI: 1:CAS:528:DC%2BC3sXot1Ghtb8%3D
    • • Karapetyan Y et al (2013) Unique drug screening approach for prion diseases identifies tacrolimus and astemizole as antiprion agents. Proc Natl Acad Sci USA 110(17):7044–7049. This publication, while very specific to prions, provides strong evidence that autophagy inhibition could be beneficial in treatment of neurodegenerative diseases with protein aggregate characteristics.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.17 , pp. 7044-7049
    • Karapetyan, Y.1
  • 61
    • 33746381549 scopus 로고    scopus 로고
    • A clinical drug library screen identifies astemizole as an antimalarial agent
    • PID: 16816845, COI: 1:CAS:528:DC%2BD28XmvFyqsrs%3D
    • Chong C et al (2006) A clinical drug library screen identifies astemizole as an antimalarial agent. Nat Chem Biol 2(8):415–416
    • (2006) Nat Chem Biol , vol.2 , Issue.8 , pp. 415-416
    • Chong, C.1
  • 62
    • 61849102412 scopus 로고    scopus 로고
    • Lithium induces clearance of protease resistant prion protein in prion-infected cells by induction of autophagy
    • PID: 19183256, COI: 1:CAS:528:DC%2BD1MXktVWhsb0%3D
    • Heiseke A et al (2009) Lithium induces clearance of protease resistant prion protein in prion-infected cells by induction of autophagy. J Neurochem 109(1):25–34
    • (2009) J Neurochem , vol.109 , Issue.1 , pp. 25-34
    • Heiseke, A.1
  • 63
    • 33645100369 scopus 로고    scopus 로고
    • Bafilomycin A1 inhibits chloroquine-induced death of cerebellar granule neurons
    • PID: 16391239, COI: 1:CAS:528:DC%2BD28XjtlKntrY%3D
    • Shacka J et al (2006) Bafilomycin A1 inhibits chloroquine-induced death of cerebellar granule neurons. Mol Pharmacol 69(4):1125–1136
    • (2006) Mol Pharmacol , vol.69 , Issue.4 , pp. 1125-1136
    • Shacka, J.1
  • 64
    • 0023503181 scopus 로고
    • Uptake, subcellular distribution and biotransformation of 3H-labelled astemizole in cultured rat hepatocytes
    • PID: 3120732, COI: 1:CAS:528:DyaL1cXkvVKltQ%3D%3D
    • Waterkeyn C et al (1987) Uptake, subcellular distribution and biotransformation of 3H-labelled astemizole in cultured rat hepatocytes. Biochem Pharmacol 36(23):4129–4136
    • (1987) Biochem Pharmacol , vol.36 , Issue.23 , pp. 4129-4136
    • Waterkeyn, C.1
  • 65
    • 71849117852 scopus 로고    scopus 로고
    • Dissecting the potential molecular mechanisms underlying alpha-synuclein cell-to-cell transfer in Parkinson’s disease
    • Angot E, Brundin P (2009) Dissecting the potential molecular mechanisms underlying alpha-synuclein cell-to-cell transfer in Parkinson’s disease. Parkinsonism Relat Disord 15(Suppl 3):7
    • (2009) Parkinsonism Relat Disord , vol.15 , pp. 7
    • Angot, E.1    Brundin, P.2
  • 66
    • 80054024011 scopus 로고    scopus 로고
    • Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
    • PID: 22028219, COI: 1:CAS:528:DC%2BC3MXhtlKjtLjE
    • Jucker M, Walker L (2011) Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders. Ann Neurol 70(4):532–540
    • (2011) Ann Neurol , vol.70 , Issue.4 , pp. 532-540
    • Jucker, M.1    Walker, L.2
  • 67
    • 79953287059 scopus 로고    scopus 로고
    • Amyloid oligomer neurotoxicity, calcium dysregulation, and lipid rafts
    • Malchiodi-Albedi F et al (2011) Amyloid oligomer neurotoxicity, calcium dysregulation, and lipid rafts. Int J Alzheimer’s Dis 2011:906964
    • (2011) Int J Alzheimer’s Dis , vol.2011 , pp. 906964
    • Malchiodi-Albedi, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.