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Volumn 19, Issue 1, 2013, Pages 263-275

Immunomodulatory and antibacterial effects of cystatin 9 against Francisella tularensis

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; IMMUNOMODULATING AGENT; MAMMALIAN TARGET OF RAPAMYCIN; RECOMBINANT CYSTATIN 9; UNCLASSIFIED DRUG;

EID: 84883257154     PISSN: 10761551     EISSN: None     Source Type: Journal    
DOI: 10.2119/molmed.2013.00081     Document Type: Article
Times cited : (12)

References (57)
  • 2
    • 79960153872 scopus 로고    scopus 로고
    • Biological role of matrix metalloproteinases: A critical balance
    • Loffek S, Schilling O, Franzke C-W. (2011) Biological role of matrix metalloproteinases: a critical balance. Eur. Respir. J. 38:191-208.
    • (2011) Eur. Respir. J , vol.38 , pp. 191-208
    • Loffek, S.1    Schilling, O.2    Franzke, C.-W.3
  • 3
    • 42549100331 scopus 로고    scopus 로고
    • Cystatin protease inhibitors and immune functions
    • Zavasnik-Bergant T. (2008) Cystatin protease inhibitors and immune functions. Front. Biosci. 4625-37.
    • (2008) Front. Biosci , pp. 4625-4637
    • Zavasnik-Bergant, T.1
  • 4
    • 33750984761 scopus 로고    scopus 로고
    • The role of cystatins in cells of the immune system
    • Kopitar-Jerala. (2006) The role of cystatins in cells of the immune system. FEBS Letters. 580:6295-301.
    • (2006) FEBS Letters , vol.580 , pp. 6295-6301
    • Kopitar-Jerala1
  • 5
    • 0026806875 scopus 로고
    • Cystatins-inhibitors of cysteine proteinases
    • Bobek LA, Levine MJ. (1992) Cystatins-inhibitors of cysteine proteinases. Crit. Rev. Oral Biol. Med. 4:307-32.
    • (1992) Crit. Rev. Oral Biol. Med , vol.4 , pp. 307-332
    • Bobek, L.A.1    Levine, M.J.2
  • 7
    • 0034446387 scopus 로고    scopus 로고
    • Cysteine proteinase inhibitor level in tumor and normal tissues in control and cured mice
    • Poteryaeva ON, et al. (2000) Cysteine proteinase inhibitor level in tumor and normal tissues in control and cured mice. Drugs Exp. Clin. Res. 26:301-6.
    • (2000) Drugs Exp. Clin. Res , vol.26 , pp. 301-306
    • Poteryaeva, O.N.1
  • 8
    • 77954658690 scopus 로고    scopus 로고
    • Cystatin B inhibition of TRAIL-induced apoptosis is associated with the protection of FLIPL from degradation by the E3 ligase itch in human melanoma cells
    • Yang F, et al. (2010) Cystatin B inhibition of TRAIL-induced apoptosis is associated with the protection of FLIPL from degradation by the E3 ligase itch in human melanoma cells. Cell Death Differ. 17:1354-67.
    • (2010) Cell Death Differ , vol.17 , pp. 1354-1367
    • Yang, F.1
  • 9
    • 76949097013 scopus 로고    scopus 로고
    • Cystatin E/M suppresses legumain activity and invasion of human melanoma
    • Briggs JJ, et al. (2010) Cystatin E/M suppresses legumain activity and invasion of human melanoma. BMC Cancer. 10:17.
    • (2010) BMC Cancer , vol.10 , pp. 17
    • Briggs, J.J.1
  • 10
    • 23244448732 scopus 로고    scopus 로고
    • Cystatin C modulates neurodegeneration and neurogenesis following status epilepticus in mouse
    • Pirttilä TJ, et al. (2005) Cystatin C modulates neurodegeneration and neurogenesis following status epilepticus in mouse. Neurobiol. Dis. 20:241-53.
    • (2005) Neurobiol. Dis , vol.20 , pp. 241-253
    • Pirttilä, T.J.1
  • 11
    • 79955958446 scopus 로고    scopus 로고
    • Protective mechanisms by cystatin C in neurodegenerative diseases
    • Gauthier S, Kaur G, Mi W, Tizon B, Levy E. (2011) Protective mechanisms by cystatin C in neurodegenerative diseases. Front. Biosci. 3:541-54.
    • (2011) Front. Biosci , vol.3 , pp. 541-554
    • Gauthier, S.1    Kaur, G.2    Mi, W.3    Tizon, B.4    Levy, E.5
  • 12
    • 77955629596 scopus 로고    scopus 로고
    • New therapeutic strategy for Parkinson's and Alzheimer's disease
    • Esposito E, Cuzzocrea S. (2010) New therapeutic strategy for Parkinson's and Alzheimer's disease. Curr. Med. Chem.17:2764-74.
    • (2010) Curr. Med. Chem , vol.17 , pp. 2764-2774
    • Esposito, E.1    Cuzzocrea, S.2
  • 13
    • 77956475769 scopus 로고    scopus 로고
    • Induction of autophagy by cystatin C: A mechanism that protects murine primary cortical neurons and neuronal cell lines
    • Tizon B, et al. (2010) Induction of autophagy by cystatin C: a mechanism that protects murine primary cortical neurons and neuronal cell lines. PLoS One. 5(3):e9819.
    • (2010) PLoS One , vol.5 , Issue.3
    • Tizon, B.1
  • 14
    • 84858647958 scopus 로고    scopus 로고
    • Inhibition of interferon response by cystatin B: Implication in HIV replication of macrophage reservoirs
    • Rivera-Rivera L, Perez-Laspiur J, Colón K, Meléndez LM. (2012) Inhibition of interferon response by cystatin B: implication in HIV replication of macrophage reservoirs. J. Neurovirol. 18:20-9.
    • (2012) J. Neurovirol , vol.18 , pp. 20-29
    • Rivera-Rivera, L.1    Perez-Laspiur, J.2    Colón, K.3    Meléndez, L.M.4
  • 15
    • 0035816032 scopus 로고    scopus 로고
    • Tularemia as a biological weapon: Medical and public health management
    • Dennis, DT, et al. (2001). Tularemia as a biological weapon: Medical and public health management. JAMA. 285:2763-73.
    • (2001) JAMA , vol.285 , pp. 2763-2773
    • Dennis, D.T.1
  • 18
    • 0035892911 scopus 로고    scopus 로고
    • Salmonella flagellin-dependent proinflammatory responses are localized to the conserved amino and carboxyl regions of the protein
    • Eaves-Pyles TD, Wong HR, Odoms K, Pyles RB. (2001) Salmonella flagellin-dependent proinflammatory responses are localized to the conserved amino and carboxyl regions of the protein. J. Immunol. 167:7009-16.
    • (2001) J. Immunol , vol.167 , pp. 7009-7016
    • Eaves-Pyles, T.D.1    Wong, H.R.2    Odoms, K.3    Pyles, R.B.4
  • 19
    • 51349110109 scopus 로고    scopus 로고
    • Enhanced nitrosative stress during Trypanosoma cruzi infection causes nitrotyrosine modification of host proteins: Implications in Chagas' disease
    • Dhiman M, et al. (2008) Enhanced nitrosative stress during Trypanosoma cruzi infection causes nitrotyrosine modification of host proteins: implications in Chagas' disease. Am. J. Pathol. 173:728-40.
    • (2008) Am. J. Pathol , vol.173 , pp. 728-740
    • Dhiman, M.1
  • 20
    • 84873348534 scopus 로고    scopus 로고
    • Proteomic analysis of Trypanosoma cruzi secretome: Characterization of two populations of extracellular vesicles and soluble proteins
    • Bayer-Santos E, et al. (2013) Proteomic analysis of Trypanosoma cruzi secretome: characterization of two populations of extracellular vesicles and soluble proteins. J. Proteome Res. 12:883-97.
    • (2013) J. Proteome Res , vol.12 , pp. 883-897
    • Bayer-Santos, E.1
  • 21
    • 34547637895 scopus 로고    scopus 로고
    • Role of primary human alveolar epithelial cells in host defense against Francisella tularensis infection
    • Gentry M, et al. (2007) Role of primary human alveolar epithelial cells in host defense against Francisella tularensis infection. Infect. Immun. 75:3969-78.
    • (2007) Infect. Immun , vol.75 , pp. 3969-3978
    • Gentry, M.1
  • 22
    • 84861888611 scopus 로고    scopus 로고
    • Hydrogen sulfide and nitric oxide are mutually dependent in the regulation of angiogenesis and endothelium-dependent vasorelaxation
    • Coletta C, et al. (2012) Hydrogen sulfide and nitric oxide are mutually dependent in the regulation of angiogenesis and endothelium-dependent vasorelaxation. Proc. Natl. Acad. Sci. U. S. A. 109:9161-6.
    • (2012) Proc. Natl. Acad. Sci. U. S. A , vol.109 , pp. 9161-9166
    • Coletta, C.1
  • 23
    • 84883226286 scopus 로고    scopus 로고
    • Burkholderia mallei and Burkholderia pseudomallei stimulate differential inflammatory responses from human alveolar type II cells (ATII) and macrophages
    • Lu R, Popov V, Patel J, Eaves-Pyles T. (2012) Burkholderia mallei and Burkholderia pseudomallei stimulate differential inflammatory responses from human alveolar type II cells (ATII) and macrophages. Front. Cell. Infect. Microbiol. 2:165.
    • (2012) Front. Cell. Infect. Microbiol , vol.2 , pp. 165
    • Lu, R.1    Popov, V.2    Patel, J.3    Eaves-Pyles, T.4
  • 24
    • 84881288420 scopus 로고    scopus 로고
    • Cystatins in immune system
    • Magister S, Kos J. (2013) Cystatins in immune system. Cancer. 4:45-56.
    • (2013) Cancer , vol.4 , pp. 45-56
    • Magister, S.1    Kos, J.2
  • 25
    • 52049096824 scopus 로고    scopus 로고
    • Cystatins: Biochemical and structural properties, and medical relevance
    • Turk V, Stoka V, Turk D. (2008) Cystatins: biochemical and structural properties, and medical relevance. Front. Biosci. 13:5406-20.
    • (2008) Front. Biosci , vol.13 , pp. 5406-5420
    • Turk, V.1    Stoka, V.2    Turk, D.3
  • 26
    • 66249098899 scopus 로고    scopus 로고
    • VEGF-A induces angiogenesis by perturbing the cathepsin-cysteine protease inhibitor balance in venules, causing basement membrane degradation and mother vessel formation
    • Chang SH, et al. (2009) VEGF-A induces angiogenesis by perturbing the cathepsin-cysteine protease inhibitor balance in venules, causing basement membrane degradation and mother vessel formation. Cancer Res. 69:4537-44.
    • (2009) Cancer Res , vol.69 , pp. 4537-4544
    • Chang, S.H.1
  • 27
    • 2542552050 scopus 로고    scopus 로고
    • Virulent and avirulent strains of Francisella tularensis prevent acidification and maturation of their phagosomes and escape into the cytoplasm in human macrophages
    • Clemens DL, Lee BY, Horwitz MA. (2004) Virulent and avirulent strains of Francisella tularensis prevent acidification and maturation of their phagosomes and escape into the cytoplasm in human macrophages. Infect. Immun. 72:3204-17.
    • (2004) Infect. Immun , vol.72 , pp. 3204-3217
    • Clemens, D.L.1    Lee, B.Y.2    Horwitz, M.A.3
  • 28
    • 6344269866 scopus 로고    scopus 로고
    • Factors affecting the escape of Francisella tularensis from the phagolysosome
    • Lindgren H, et al. (2004) Factors affecting the escape of Francisella tularensis from the phagolysosome. J. Med. Microbiol. 53:953-8.
    • (2004) J. Med. Microbiol , vol.53 , pp. 953-958
    • Lindgren, H.1
  • 29
    • 0013887127 scopus 로고
    • Glycopeptide transpeptidase and D-alanine carboxypeptidase: Penicillin-sensitive enzymatic reactions
    • Izaki K, Matsuhashi M, Strominger JL. (1966) Glycopeptide transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reactions. PNAS. 55:656-63.
    • (1966) PNAS , vol.55 , pp. 656-663
    • Izaki, K.1    Matsuhashi, M.2    Strominger, J.L.3
  • 30
    • 0010535578 scopus 로고
    • Mechanism of penicillin action: Penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases
    • Rogers R, Yogum DJ, Waxman JRR, Stominger JL. (1979) Mechanism of penicillin action: Penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases. PNAS. 76:2730-4.
    • (1979) PNAS , vol.76 , pp. 2730-2734
    • Rogers, R.1    Yogum, D.J.2    Waxman, J.R.R.3    Stominger, J.L.4
  • 31
    • 0038387873 scopus 로고    scopus 로고
    • Conserved microtubule-actin interactions in cell movement and morphogenesis
    • Rodriguez OC, et al. (2003) Conserved microtubule-actin interactions in cell movement and morphogenesis. Nat. Cell. Biol. 5:599-609.
    • (2003) Nat. Cell. Biol , vol.5 , pp. 599-609
    • Rodriguez, O.C.1
  • 32
    • 0033374588 scopus 로고    scopus 로고
    • Co-loss of profiling I, II and cofilin with actin from maturing phagosomes in Dictyostelium discoideum
    • Yuan A, Cia CP. (1999) Co-loss of profiling I, II and cofilin with actin from maturing phagosomes in Dictyostelium discoideum. Protoplasma. 209:214-225.
    • (1999) Protoplasma , vol.209 , pp. 214-225
    • Yuan, A.1    Cia, C.P.2
  • 33
    • 77955631174 scopus 로고    scopus 로고
    • Glutaredoxin 1 regulates cigarette smokemediated lung inflammation through differential modulation of I{kappa}B kinases in mice: Impact on histone acetylation
    • Chung S, Sundar IK, Yao H, Ho YS, Rahman I. (2010) Glutaredoxin 1 regulates cigarette smokemediated lung inflammation through differential modulation of I{kappa}B kinases in mice: impact on histone acetylation. Am. J. Physiol. Lung Cell Mol. Physiol. 299:L192-203.
    • (2010) Am. J. Physiol. Lung Cell Mol. Physiol , vol.299
    • Chung, S.1    Sundar, I.K.2    Yao, H.3    Ho, Y.S.4    Rahman, I.5
  • 34
    • 84892673381 scopus 로고    scopus 로고
    • Vimentin suppresses the production of reactive oxygen species and the antimicrobial response via p47phox [abstract]
    • Mor-Vaknin N, et al. (2011) Vimentin suppresses the production of reactive oxygen species and the antimicrobial response via p47phox [abstract]. Arthritis Rheum. 63 Suppl 10:1003.
    • (2011) Arthritis Rheum , vol.63 , Issue.SUPPL. 10 , pp. 1003
    • Mor-Vaknin, N.1
  • 35
    • 80355129706 scopus 로고    scopus 로고
    • Vimentin is sufficient and required for wound repair and remodeling in alveolar epithelial cells
    • Rogel MR, et. al. (2011) Vimentin is sufficient and required for wound repair and remodeling in alveolar epithelial cells. FASEB J. 25:3873-83.
    • (2011) FASEB J , vol.25 , pp. 3873-3883
    • Rogel, M.R.1
  • 36
    • 77950220938 scopus 로고    scopus 로고
    • Tolllike receptor 3 agonist protection against experimental Francisella tularensis respiratory tract infection
    • Pyles RB, Jezek GE, Eaves-Pyles TD. (2010) Tolllike receptor 3 agonist protection against experimental Francisella tularensis respiratory tract infection. Infect. Immun. 78:1700-10.
    • (2010) Infect. Immun , vol.78 , pp. 1700-1710
    • Pyles, R.B.1    Jezek, G.E.2    Eaves-Pyles, T.D.3
  • 37
    • 33749017931 scopus 로고    scopus 로고
    • Cysteine cathepsins: Multifunctional enzymes in cancer
    • Mohamed MM, Sloane BF. (2006) Cysteine cathepsins: multifunctional enzymes in cancer. Nature Cancer. 6:764-75.
    • (2006) Nature Cancer , vol.6 , pp. 764-775
    • Mohamed, M.M.1    Sloane, B.F.2
  • 38
    • 84872320531 scopus 로고    scopus 로고
    • Cathepsin B and cystatin B in HIV-seropositive women are associated with infection and HIV-1-associated neurocognitive disorders
    • Cantres-Rosario Y, et al. (2013) Cathepsin B and cystatin B in HIV-seropositive women are associated with infection and HIV-1-associated neurocognitive disorders. AIDS. 27:347-56.
    • (2013) AIDS , vol.27 , pp. 347-356
    • Cantres-Rosario, Y.1
  • 39
    • 77956933931 scopus 로고    scopus 로고
    • Serum cystatin C is an early predictive biomarker of acute kidney injury after pediatric cardiopulmonary bypass
    • Krawczeski CD, et al. (2010) Serum cystatin C is an early predictive biomarker of acute kidney injury after pediatric cardiopulmonary bypass. Clin. J. Am. Soc. Nephrol. 5:1552-7.
    • (2010) Clin. J. Am. Soc. Nephrol , vol.5 , pp. 1552-1557
    • Krawczeski, C.D.1
  • 40
    • 84864281320 scopus 로고    scopus 로고
    • Predictive power of serum cystatin C to detect acute kidney injury and pediatric-modified RIFLE class in children undergoing cardiac surgery
    • Hassinger AB, et al. (2012) Predictive power of serum cystatin C to detect acute kidney injury and pediatric-modified RIFLE class in children undergoing cardiac surgery. Pediatr. Crit. Care Med. 13:435-40.
    • (2012) Pediatr. Crit. Care Med , vol.13 , pp. 435-440
    • Hassinger, A.B.1
  • 41
    • 84867651873 scopus 로고    scopus 로고
    • Cystatin C and asymptomatic coronary artery disease in patients with metabolic syndrome and normal glomerular filtration rate
    • Qing X, et al. (2012) Cystatin C and asymptomatic coronary artery disease in patients with metabolic syndrome and normal glomerular filtration rate. Cardiovasc. Diabetol. 11:108.
    • (2012) Cardiovasc. Diabetol , vol.11 , pp. 108
    • Qing, X.1
  • 42
    • 79955598011 scopus 로고    scopus 로고
    • Features of sepsis caused by pulmonary infection with Francisella tularensis Type A strain
    • Sharma J, Mares CA, Li Q, Morris EG, Teale JM. (2011) Features of sepsis caused by pulmonary infection with Francisella tularensis Type A strain. Microb. Pathog. 51:39-47.
    • (2011) Microb. Pathog , vol.51 , pp. 39-47
    • Sharma, J.1    Mares, C.A.2    Li, Q.3    Morris, E.G.4    Teale, J.M.5
  • 43
    • 2542552050 scopus 로고    scopus 로고
    • Virulent and avirulent strains of Francisella tularensis prevent acidification and maturation of their phagosomes and escape into the cytoplasm in human macrophages
    • Clemens DL, Lee BY, Horwitz MA. (2004) Virulent and avirulent strains of Francisella tularensis prevent acidification and maturation of their phagosomes and escape into the cytoplasm in human macrophages. Infect. Immun. 72:3204-17.
    • (2004) Infect. Immun , vol.72 , pp. 3204-3217
    • Clemens, D.L.1    Lee, B.Y.2    Horwitz, M.A.3
  • 44
    • 48849105040 scopus 로고    scopus 로고
    • MglA and Igl proteins contribute to the modulation of Francisella tularensis live vaccine strain-containing phagosomes in murine macrophages
    • Bönquist L, Lindgren H, Golovliov I, Guina T, Sjöstedt A. (2008) MglA and Igl proteins contribute to the modulation of Francisella tularensis live vaccine strain-containing phagosomes in murine macrophages. Infect. Immun. 76:3502-10.
    • (2008) Infect. Immun , vol.76 , pp. 3502-3510
    • Bönquist, L.1    Lindgren, H.2    Golovliov, I.3    Guina, T.4    Sjöstedt, A.5
  • 45
    • 33749264796 scopus 로고    scopus 로고
    • Autophagy-mediated reentry of Francisella tularensis in to the endocytic compartment after cytoplasmic replication
    • Checroun C, Whrly TD, Rishcher DR, Hayes SF, Celli J. (2006) Autophagy-mediated reentry of Francisella tularensis in to the endocytic compartment after cytoplasmic replication. Proc. Natl. Acad. Sci. U. S. A. 103:14578-83.
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 14578-14583
    • Checroun, C.1    Whrly, T.D.2    Rishcher, D.R.3    Hayes, S.F.4    Celli, J.5
  • 46
    • 34548703962 scopus 로고    scopus 로고
    • Francisella tularensis: Activation of the inflammasome
    • Weiss DS, Henry T, Monack DM. (2007) Francisella tularensis: Activation of the inflammasome. Ann. NY Acad. Sci. 1105:219-37.
    • (2007) Ann. NY Acad. Sci , vol.1105 , pp. 219-237
    • Weiss, D.S.1    Henry, T.2    Monack, D.M.3
  • 47
    • 84857128486 scopus 로고    scopus 로고
    • Innate immune recognition of Francisella tularensis: Activation of type-I interferons and the inflammasome
    • Jones JW, Broz P, Monack DM. (2011) Innate immune recognition of Francisella tularensis: activation of type-I interferons and the inflammasome. Front. Micro. 2:1-10.
    • (2011) Front. Micro , vol.2 , pp. 1-10
    • Jones, J.W.1    Broz, P.2    Monack, D.M.3
  • 48
    • 26844452231 scopus 로고    scopus 로고
    • Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis
    • Mariathasan S, Weiss DS, Dixit VM, Monack DM. (2005) Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis. J. Exp. Med. 202:1043-9.
    • (2005) J. Exp. Med , vol.202 , pp. 1043-1049
    • Mariathasan, S.1    Weiss, D.S.2    Dixit, V.M.3    Monack, D.M.4
  • 49
    • 33846232732 scopus 로고    scopus 로고
    • Matrix metalloproteinase 9 activity enhances host susceptibility to pulmonary infection with type A and B strains of Francisella tularensis
    • Malik M, et al. (2007) Matrix metalloproteinase 9 activity enhances host susceptibility to pulmonary infection with type A and B strains of Francisella tularensis. J. Immunol. 178:1013-20.
    • (2007) J. Immunol , vol.178 , pp. 1013-1020
    • Malik, M.1
  • 50
    • 0035170189 scopus 로고    scopus 로고
    • Susceptibility to secondary Francisella tularensis live vaccine strain infection in B-cell-deficient mice is associated with neutrophilia but not with defects in specific T-cell-mediated immunity
    • Bosio CM, Elkins KL. (2001) Susceptibility to secondary Francisella tularensis live vaccine strain infection in B-cell-deficient mice is associated with neutrophilia but not with defects in specific T-cell-mediated immunity. Infect. Immun. 69:194-203.
    • (2001) Infect. Immun , vol.69 , pp. 194-203
    • Bosio, C.M.1    Elkins, K.L.2
  • 51
    • 84879684349 scopus 로고    scopus 로고
    • Mucosal immunology: Autophagy helps man the barriers
    • Leavy O. (2013) Mucosal immunology: autophagy helps man the barriers. Nat. Rev. Immunol. 13:470-1.
    • (2013) Nat. Rev. Immunol , vol.13 , pp. 470-471
    • Leavy, O.1
  • 52
    • 84871916907 scopus 로고    scopus 로고
    • Regulation and functional significance of autophagy in respiratory cell biology and disease
    • Patel AS, Morse D, Choi AM. (2013) Regulation and functional significance of autophagy in respiratory cell biology and disease. Am. J. Respir. Cell Mol. Biol. 48:1-9.
    • (2013) Am. J. Respir. Cell Mol. Biol , vol.48 , pp. 1-9
    • Patel, A.S.1    Morse, D.2    Choi, A.M.3
  • 53
    • 84865309771 scopus 로고    scopus 로고
    • Autophagy as a macrophage response to bacterial infection
    • Gong L, Devenish RJ, Prescott M. (2012) Autophagy as a macrophage response to bacterial infection. IUBMB Life. 64:740-7.
    • (2012) IUBMB Life , vol.64 , pp. 740-747
    • Gong, L.1    Devenish, R.J.2    Prescott, M.3
  • 54
    • 84863116629 scopus 로고    scopus 로고
    • Class III PI3K Vps34 plays an essential role in autophagy and in heart and liver function
    • Jaber N, et al. (2012) Class III PI3K Vps34 plays an essential role in autophagy and in heart and liver function. Proc. Natl. Acad. Sci. U. S. A. 109:2003-8.
    • (2012) Proc. Natl. Acad. Sci. U. S. A , vol.109 , pp. 2003-2008
    • Jaber, N.1
  • 55
    • 84861448736 scopus 로고    scopus 로고
    • TGF--induced activation of mTOR complex 2 drives epithelial-mesenchymal transition and cell invasion
    • Lamouille S, Connolly E, Smyth JW, Akhurst RJ, Derynck R. (2012) TGF--induced activation of mTOR complex 2 drives epithelial-mesenchymal transition and cell invasion. J. Cell Sci. 125:1259-73.
    • (2012) J. Cell Sci , vol.125 , pp. 1259-1273
    • Lamouille, S.1    Connolly, E.2    Smyth, J.W.3    Akhurst, R.J.4    Derynck, R.5
  • 57
    • 84869778050 scopus 로고    scopus 로고
    • Antimicrobial activity and molecular mechanism of the CRES protein
    • Wang L, et al. (2012) Antimicrobial activity and molecular mechanism of the CRES protein. PLoS One. 7:e48368.
    • (2012) PLoS One , vol.7
    • Wang, L.1


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