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Volumn 26, Issue 10, 2005, Pages 523-528

Autophagy in innate and adaptive immunity

Author keywords

[No Author keywords available]

Indexed keywords

AUTOANTIGEN; COMPLEMENT COMPONENT C5; EPSTEIN BARR VIRUS ANTIGEN; GAMMA INTERFERON; GLUTAMATE DECARBOXYLASE; HUMAN IMMUNOGLOBULIN; IMMUNOGLOBULIN KAPPA CHAIN; INTERLEUKIN 13; KANAMYCIN KINASE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MUCIN 1;

EID: 24744463111     PISSN: 14714906     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.it.2005.08.003     Document Type: Review
Times cited : (187)

References (61)
  • 1
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: A double-edged sword
    • T. Shintani, and D.J. Klionsky Autophagy in health and disease: a double-edged sword Science 306 2004 990 995
    • (2004) Science , vol.306 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 2
    • 12944308330 scopus 로고    scopus 로고
    • Eating oneself and uninvited guests; Autophagy-related pathways in cellular defense
    • B. Levine Eating oneself and uninvited guests; autophagy-related pathways in cellular defense Cell 120 2005 159 162
    • (2005) Cell , vol.120 , pp. 159-162
    • Levine, B.1
  • 3
    • 11144245626 scopus 로고    scopus 로고
    • The role of autophagy during the early neonatal starvation period
    • A. Kuma The role of autophagy during the early neonatal starvation period Nature 432 2004 1032 1036
    • (2004) Nature , vol.432 , pp. 1032-1036
    • Kuma, A.1
  • 4
    • 0033747489 scopus 로고    scopus 로고
    • Autophagy in the epithelial cells of murine seminal vesicle in vitro. Formation of large sheets of nascent isolation membranes, sequestration of the nucleus and inhibition by wortmannin and 3-ethyladenine
    • A.L. Kovacs Autophagy in the epithelial cells of murine seminal vesicle in vitro. Formation of large sheets of nascent isolation membranes, sequestration of the nucleus and inhibition by wortmannin and 3-ethyladenine Cell Tissue Res. 302 2000 253 261
    • (2000) Cell Tissue Res. , vol.302 , pp. 253-261
    • Kovacs, A.L.1
  • 5
    • 2642553881 scopus 로고    scopus 로고
    • Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8
    • L. Yu Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8 Science 304 2004 1500 1502
    • (2004) Science , vol.304 , pp. 1500-1502
    • Yu, L.1
  • 6
    • 10344262564 scopus 로고    scopus 로고
    • Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes
    • S. Shimizu Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes Nat. Cell Biol. 6 2004 1221 1228
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1221-1228
    • Shimizu, S.1
  • 7
    • 12944303650 scopus 로고    scopus 로고
    • Growth factor regulation of autophagy and cell survival in the absence of apoptosis
    • J.J. Lum Growth factor regulation of autophagy and cell survival in the absence of apoptosis Cell 120 2005 237 248
    • (2005) Cell , vol.120 , pp. 237-248
    • Lum, J.J.1
  • 8
    • 19944434059 scopus 로고    scopus 로고
    • Inhibition of macroautophagy triggers apoptosis
    • P. Boya Inhibition of macroautophagy triggers apoptosis Mol. Cell. Biol. 25 2005 1025 1040
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1025-1040
    • Boya, P.1
  • 9
    • 4544385218 scopus 로고    scopus 로고
    • Autophagy: Many paths to the same end
    • A.M. Cuervo Autophagy: many paths to the same end Mol. Cell. Biochem. 263 2004 55 72
    • (2004) Mol. Cell. Biochem. , vol.263 , pp. 55-72
    • Cuervo, A.M.1
  • 10
    • 8344247016 scopus 로고    scopus 로고
    • Autophagy defends cells against invading group a Streptococcus
    • I. Nakagawa Autophagy defends cells against invading group A Streptococcus Science 306 2004 1037 1040
    • (2004) Science , vol.306 , pp. 1037-1040
    • Nakagawa, I.1
  • 11
    • 13244256806 scopus 로고    scopus 로고
    • Escape of intracellular Shigella from autophagy
    • M. Ogawa Escape of intracellular Shigella from autophagy Science 307 2005 727 731
    • (2005) Science , vol.307 , pp. 727-731
    • Ogawa, M.1
  • 12
    • 10944253145 scopus 로고    scopus 로고
    • Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages
    • M.G. Gutierrez Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages Cell 119 2004 753 766
    • (2004) Cell , vol.119 , pp. 753-766
    • Gutierrez, M.G.1
  • 13
    • 12844275079 scopus 로고    scopus 로고
    • Endogenous MHC class II processing of a viral nuclear antigen after autophagy
    • C. Paludan Endogenous MHC class II processing of a viral nuclear antigen after autophagy Science 307 2005 593 596
    • (2005) Science , vol.307 , pp. 593-596
    • Paludan, C.1
  • 14
    • 20344361954 scopus 로고    scopus 로고
    • From the cover: Autophagy promotes MHC class II presentation of peptides from intracellular source proteins
    • J. Dengjel From the cover: autophagy promotes MHC class II presentation of peptides from intracellular source proteins Proc. Natl. Acad. Sci. U. S. A. 102 2005 7922 7927
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 7922-7927
    • Dengjel, J.1
  • 15
    • 20344402819 scopus 로고    scopus 로고
    • Autophagy and intracellular surveillance: Modulating MHC class II antigen presentation with stress
    • V.L. Crotzer, and J.S. Blum Autophagy and intracellular surveillance: modulating MHC class II antigen presentation with stress Proc. Natl. Acad. Sci. U. S. A. 102 2005 7779 7780
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 7779-7780
    • Crotzer, V.L.1    Blum, J.S.2
  • 16
    • 17044381835 scopus 로고    scopus 로고
    • Processing and presentation of HLA class I and II epitopes by dendritic cells after transfection with in vitro-transcribed MUC1 RNA
    • D. Dorfel Processing and presentation of HLA class I and II epitopes by dendritic cells after transfection with in vitro-transcribed MUC1 RNA Blood 105 2005 3199 3205
    • (2005) Blood , vol.105 , pp. 3199-3205
    • Dorfel, D.1
  • 17
    • 0037193474 scopus 로고    scopus 로고
    • DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death
    • B. Inbal DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death J. Cell Biol. 157 2002 455 468
    • (2002) J. Cell Biol. , vol.157 , pp. 455-468
    • Inbal, B.1
  • 18
    • 0036463736 scopus 로고    scopus 로고
    • Autophagy in the eukaryotic cell
    • F. Reggiori, and D.J. Klionsky Autophagy in the eukaryotic cell Eukaryot. Cell 1 2002 11 21
    • (2002) Eukaryot. Cell , vol.1 , pp. 11-21
    • Reggiori, F.1    Klionsky, D.J.2
  • 19
    • 2442482810 scopus 로고    scopus 로고
    • Autophagy as a cell death and tumor suppressor mechanism
    • D. Gozuacik, and A. Kimchi Autophagy as a cell death and tumor suppressor mechanism Oncogene 23 2004 2891 2906
    • (2004) Oncogene , vol.23 , pp. 2891-2906
    • Gozuacik, D.1    Kimchi, A.2
  • 20
    • 0347626252 scopus 로고    scopus 로고
    • Autophagy: A regulated bulk degradation process inside cells
    • T. Yoshimori Autophagy: a regulated bulk degradation process inside cells Biochem. Biophys. Res. Commun. 313 2004 453 458
    • (2004) Biochem. Biophys. Res. Commun. , vol.313 , pp. 453-458
    • Yoshimori, T.1
  • 21
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • B. Levine, and D.J. Klionsky Development by self-digestion: molecular mechanisms and biological functions of autophagy Dev. Cell 6 2004 463 477
    • (2004) Dev. Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 22
    • 19344368318 scopus 로고    scopus 로고
    • Autophagy regulates programmed cell death during the plant innate immune response
    • Y. Liu Autophagy regulates programmed cell death during the plant innate immune response Cell 121 2005 567 577
    • (2005) Cell , vol.121 , pp. 567-577
    • Liu, Y.1
  • 23
    • 10744225487 scopus 로고    scopus 로고
    • A unified nomenclature for yeast autophagy-related genes
    • D.J. Klionsky A unified nomenclature for yeast autophagy-related genes Dev. Cell 5 2003 539 545
    • (2003) Dev. Cell , vol.5 , pp. 539-545
    • Klionsky, D.J.1
  • 24
    • 4344624322 scopus 로고    scopus 로고
    • LC3 conjugation system in mammalian autophagy
    • I. Tanida LC3 conjugation system in mammalian autophagy Int. J. Biochem. Cell Biol. 36 2004 2503 2518
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2503-2518
    • Tanida, I.1
  • 25
    • 24044513985 scopus 로고    scopus 로고
    • Endothelial nitric-oxide synthase antisense (NOS3AS) gene encodes an autophagy-related protein (APG9-like2) highly expressed in trophoblast
    • T. Yamada Endothelial nitric-oxide synthase antisense (NOS3AS) gene encodes an autophagy-related protein (APG9-like2) highly expressed in trophoblast J. Biol. Chem. 280 2005 18283 18290
    • (2005) J. Biol. Chem. , vol.280 , pp. 18283-18290
    • Yamada, T.1
  • 26
    • 0034727876 scopus 로고    scopus 로고
    • Interaction of the Unc-51-like kinase and microtubule-associated protein light chain 3 related proteins in the brain: Possible role of vesicular transport in axonal elongation
    • N. Okazaki Interaction of the Unc-51-like kinase and microtubule- associated protein light chain 3 related proteins in the brain: possible role of vesicular transport in axonal elongation Brain Res. Mol. Brain Res. 85 2000 1 12
    • (2000) Brain Res. Mol. Brain Res. , vol.85 , pp. 1-12
    • Okazaki, N.1
  • 27
    • 0001488499 scopus 로고    scopus 로고
    • Protection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein
    • X.H. Liang Protection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein J. Virol. 72 1998 8586 8596
    • (1998) J. Virol. , vol.72 , pp. 8586-8596
    • Liang, X.H.1
  • 28
    • 0000906170 scopus 로고    scopus 로고
    • Induction of autophagy and inhibition of tumorigenesis by beclin 1
    • X.H. Liang Induction of autophagy and inhibition of tumorigenesis by beclin 1 Nature 402 1999 672 676
    • (1999) Nature , vol.402 , pp. 672-676
    • Liang, X.H.1
  • 29
    • 8044257699 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rat hepatocytes
    • E.F. Blommaart The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rat hepatocytes Eur. J. Biochem. 243 1997 240 246
    • (1997) Eur. J. Biochem. , vol.243 , pp. 240-246
    • Blommaart, E.F.1
  • 30
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3′-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells
    • A. Petiot Distinct classes of phosphatidylinositol 3′-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells J. Biol. Chem. 275 2000 992 998
    • (2000) J. Biol. Chem. , vol.275 , pp. 992-998
    • Petiot, A.1
  • 31
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant α-synuclein by chaperone-mediated autophagy
    • A.M. Cuervo Impaired degradation of mutant α-synuclein by chaperone-mediated autophagy Science 305 2004 1292 1295
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1
  • 32
    • 0021322401 scopus 로고
    • Glycogen autophagosomes in polymorphonuclear leukocytes induced by rickettsiae
    • Y. Rikihisa Glycogen autophagosomes in polymorphonuclear leukocytes induced by rickettsiae Anat. Rec. 208 1984 319 327
    • (1984) Anat. Rec. , vol.208 , pp. 319-327
    • Rikihisa, Y.1
  • 33
    • 0037039442 scopus 로고    scopus 로고
    • Regulation of starvation- and virus-induced autophagy by the eIF2α kinase signaling pathway
    • Z. Talloczy Regulation of starvation- and virus-induced autophagy by the eIF2α kinase signaling pathway Proc. Natl. Acad. Sci. U. S. A. 99 2002 190 195
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 190-195
    • Talloczy, Z.1
  • 34
    • 0037711625 scopus 로고    scopus 로고
    • Cytoplasmic bacteria can be targets for autophagy
    • K.A. Rich Cytoplasmic bacteria can be targets for autophagy Cell. Microbiol. 5 2003 455 468
    • (2003) Cell. Microbiol. , vol.5 , pp. 455-468
    • Rich, K.A.1
  • 35
    • 0029155737 scopus 로고
    • Association of Legionella pneumophila with the macrophage endoplasmic reticulum
    • M.S. Swanson, and R.R. Isberg Association of Legionella pneumophila with the macrophage endoplasmic reticulum Infect. Immun. 63 1995 3609 3620
    • (1995) Infect. Immun. , vol.63 , pp. 3609-3620
    • Swanson, M.S.1    Isberg, R.R.2
  • 36
    • 0034876410 scopus 로고    scopus 로고
    • Porphyromonas gingivalis traffics to autophagosomes in human coronary artery endothelial cells
    • B.R. Dorn Porphyromonas gingivalis traffics to autophagosomes in human coronary artery endothelial cells Infect. Immun. 69 2001 5698 5708
    • (2001) Infect. Immun. , vol.69 , pp. 5698-5708
    • Dorn, B.R.1
  • 37
    • 0031797897 scopus 로고    scopus 로고
    • Brucella abortus transits through the autophagic pathway and replicates in the endoplasmic reticulum of nonprofessional phagocytes
    • J. Pizarro-Cerda Brucella abortus transits through the autophagic pathway and replicates in the endoplasmic reticulum of nonprofessional phagocytes Infect. Immun. 66 1998 5711 5724
    • (1998) Infect. Immun. , vol.66 , pp. 5711-5724
    • Pizarro-Cerda, J.1
  • 38
    • 3342927582 scopus 로고    scopus 로고
    • Interaction of Chlamydia trachomatis serovar L2 with the host autophagic pathway
    • H.M. Al-Younes Interaction of Chlamydia trachomatis serovar L2 with the host autophagic pathway Infect. Immun. 72 2004 4751 4762
    • (2004) Infect. Immun. , vol.72 , pp. 4751-4762
    • Al-Younes, H.M.1
  • 39
    • 0036784707 scopus 로고    scopus 로고
    • Coxiella burnetii localizes in a Rab7-labeled compartment with autophagic characteristics
    • W. Beron Coxiella burnetii localizes in a Rab7-labeled compartment with autophagic characteristics Infect. Immun. 70 2002 5816 5821
    • (2002) Infect. Immun. , vol.70 , pp. 5816-5821
    • Beron, W.1
  • 40
    • 0346849709 scopus 로고    scopus 로고
    • A Salmonella protein causes macrophage cell death by inducing autophagy
    • L.D. Hernandez A Salmonella protein causes macrophage cell death by inducing autophagy J. Cell Biol. 163 2003 1123 1131
    • (2003) J. Cell Biol. , vol.163 , pp. 1123-1131
    • Hernandez, L.D.1
  • 41
    • 1642280930 scopus 로고    scopus 로고
    • Coronavirus replication complex formation utilizes components of cellular autophagy
    • E. Prentice Coronavirus replication complex formation utilizes components of cellular autophagy J. Biol. Chem. 279 2004 10136 10141
    • (2004) J. Biol. Chem. , vol.279 , pp. 10136-10141
    • Prentice, E.1
  • 42
    • 3242877218 scopus 로고    scopus 로고
    • Rab7 is required for the normal progression of the autophagic pathway in mammalian cells
    • M.G. Gutierrez Rab7 is required for the normal progression of the autophagic pathway in mammalian cells J. Cell Sci. 117 2004 2687 2697
    • (2004) J. Cell Sci. , vol.117 , pp. 2687-2697
    • Gutierrez, M.G.1
  • 43
    • 0032563798 scopus 로고    scopus 로고
    • A protein conjugation system essential for autophagy
    • N. Mizushima A protein conjugation system essential for autophagy Nature 395 1998 395 398
    • (1998) Nature , vol.395 , pp. 395-398
    • Mizushima, N.1
  • 44
    • 0032545292 scopus 로고    scopus 로고
    • A new protein conjugation system in human. the counterpart of the yeast Apg12p conjugation system essential for autophagy
    • N. Mizushima A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy J. Biol. Chem. 273 1998 33889 33892
    • (1998) J. Biol. Chem. , vol.273 , pp. 33889-33892
    • Mizushima, N.1
  • 45
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Y. Kabeya LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing EMBO J. 19 2000 5720 5728
    • (2000) EMBO J. , vol.19 , pp. 5720-5728
    • Kabeya, Y.1
  • 46
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • N. Mizushima In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker Mol. Biol. Cell 15 2004 1101 1111
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1
  • 47
    • 14044277429 scopus 로고    scopus 로고
    • The molecular machinery of autophagy: Unanswered questions
    • D.J. Klionsky The molecular machinery of autophagy: unanswered questions J. Cell Sci. 118 2005 7 18
    • (2005) J. Cell Sci. , vol.118 , pp. 7-18
    • Klionsky, D.J.1
  • 48
    • 1842407189 scopus 로고    scopus 로고
    • Excessive degradation of intracellular protein in macrophages prevents presentation in the context of major histocompatibility complex class II molecules
    • M.I. Brazil Excessive degradation of intracellular protein in macrophages prevents presentation in the context of major histocompatibility complex class II molecules Eur. J. Immunol. 27 1997 1506 1514
    • (1997) Eur. J. Immunol. , vol.27 , pp. 1506-1514
    • Brazil, M.I.1
  • 49
    • 0037960005 scopus 로고    scopus 로고
    • Major histocompatibility complex class II-restricted presentation of a cytosolic antigen by autophagy
    • F. Nimmerjahn Major histocompatibility complex class II-restricted presentation of a cytosolic antigen by autophagy Eur. J. Immunol. 33 2003 1250 1259
    • (2003) Eur. J. Immunol. , vol.33 , pp. 1250-1259
    • Nimmerjahn, F.1
  • 50
    • 19344373577 scopus 로고    scopus 로고
    • Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens
    • D. Zhou Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens Immunity 22 2005 571 581
    • (2005) Immunity , vol.22 , pp. 571-581
    • Zhou, D.1
  • 51
    • 0037530637 scopus 로고    scopus 로고
    • + T cells that were isolated from a melanoma patient vaccinated with a MAGE-3 protein
    • + T cells that were isolated from a melanoma patient vaccinated with a MAGE-3 protein J. Immunol. 171 2003 219 225
    • (2003) J. Immunol. , vol.171 , pp. 219-225
    • Zhang, Y.1
  • 52
    • 0036838610 scopus 로고    scopus 로고
    • HLA-DR4 molecules in neuroendocrine epithelial cells associate to a heterogeneous repertoire of cytoplasmic and surface self peptides
    • A. Muntasell HLA-DR4 molecules in neuroendocrine epithelial cells associate to a heterogeneous repertoire of cytoplasmic and surface self peptides J. Immunol. 169 2002 5052 5060
    • (2002) J. Immunol. , vol.169 , pp. 5052-5060
    • Muntasell, A.1
  • 53
    • 20144381544 scopus 로고    scopus 로고
    • Essential roles of Atg5 and FADD in autophagic cell death: Dissection of autophagic cell death into vacuole formation and cell death
    • J.O. Pyo Essential roles of Atg5 and FADD in autophagic cell death: dissection of autophagic cell death into vacuole formation and cell death J. Biol. Chem. 280 2005 20722 20729
    • (2005) J. Biol. Chem. , vol.280 , pp. 20722-20729
    • Pyo, J.O.1
  • 54
    • 0041402773 scopus 로고    scopus 로고
    • Immune evasion by Mycobacterium tuberculosis: Living with the enemy
    • J.L. Flynn, and J. Chan Immune evasion by Mycobacterium tuberculosis: living with the enemy Curr. Opin. Immunol. 15 2003 450 455
    • (2003) Curr. Opin. Immunol. , vol.15 , pp. 450-455
    • Flynn, J.L.1    Chan, J.2
  • 55
    • 0142240338 scopus 로고    scopus 로고
    • Immune control of tuberculosis by IFN-γ-inducible LRG-47
    • J.D. MacMicking Immune control of tuberculosis by IFN-γ-inducible LRG-47 Science 302 2003 654 659
    • (2003) Science , vol.302 , pp. 654-659
    • MacMicking, J.D.1
  • 56
    • 1142298755 scopus 로고    scopus 로고
    • P47 GTPases: Regulators of immunity to intracellular pathogens
    • G.A. Taylor p47 GTPases: regulators of immunity to intracellular pathogens Nat. Rev. Immunol. 4 2004 100 109
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 100-109
    • Taylor, G.A.1
  • 57
    • 0141780844 scopus 로고    scopus 로고
    • Stimulation of signal transducer and activator of transcription-1 (STAT1)-dependent gene transcription by lipopolysaccharide and interferon-γ is regulated by mammalian target of rapamycin
    • A.S. Kristof Stimulation of signal transducer and activator of transcription-1 (STAT1)-dependent gene transcription by lipopolysaccharide and interferon-γ is regulated by mammalian target of rapamycin J. Biol. Chem. 278 2003 33637 33644
    • (2003) J. Biol. Chem. , vol.278 , pp. 33637-33644
    • Kristof, A.S.1
  • 58
    • 0035064073 scopus 로고    scopus 로고
    • The bare lymphocyte syndrome and the regulation of MHC expression
    • W. Reith, and B. Mach The bare lymphocyte syndrome and the regulation of MHC expression Annu. Rev. Immunol. 19 2001 331 373
    • (2001) Annu. Rev. Immunol. , vol.19 , pp. 331-373
    • Reith, W.1    MacH, B.2
  • 59
    • 0031050035 scopus 로고    scopus 로고
    • Regulation of transcription of MHC class II genes
    • J.M. Boss Regulation of transcription of MHC class II genes Curr. Opin. Immunol. 9 1997 107 113
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 107-113
    • Boss, J.M.1
  • 60
    • 0030946256 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol 3-kinase by interleukin-13. An inhibitory signal for inducible nitric-oxide synthase expression in epithelial cell line HT-29
    • K. Wright Activation of phosphatidylinositol 3-kinase by interleukin-13. An inhibitory signal for inducible nitric-oxide synthase expression in epithelial cell line HT-29 J. Biol. Chem. 272 1997 12626 12633
    • (1997) J. Biol. Chem. , vol.272 , pp. 12626-12633
    • Wright, K.1
  • 61
    • 0035929650 scopus 로고    scopus 로고
    • The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3-kinase/protein kinase B pathway
    • S. Arico The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3-kinase/protein kinase B pathway J. Biol. Chem. 276 2001 35243 35246
    • (2001) J. Biol. Chem. , vol.276 , pp. 35243-35246
    • Arico, S.1


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