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Volumn 37, Issue 3, 2011, Pages 295-306

Granulovacuolar degeneration (GVD) bodies of Alzheimer's disease (AD) resemble late-stage autophagic organelles

Author keywords

Alzheimer's disease; Autophagy; Endocytosis; Granulovacuolar degeneration; Lysosome

Indexed keywords

CASEIN KINASE IDELTA; CATHEPSIN D; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1;

EID: 79951790558     PISSN: 03051846     EISSN: 13652990     Source Type: Journal    
DOI: 10.1111/j.1365-2990.2010.01135.x     Document Type: Article
Times cited : (89)

References (70)
  • 1
    • 0001719387 scopus 로고
    • Histologie und Histopathologische Arbeiten über die Grosshirnrinde
    • In Eds F Nissl, A Alzheimer. Jena, Germany: Fischer, -
    • Simchowicz T. Histologische studien uber die senile dementz. In Histologie und Histopathologische Arbeiten über die Grosshirnrinde. Eds F Nissl, A Alzheimer Jena, Germany: Fischer, 1911; 267-444
    • (1911) Histologische studien uber die senile dementz , pp. 267-444
    • Simchowicz, T.1
  • 2
    • 0018124169 scopus 로고
    • Topographic distribution of neurofibrillary tangles and granulovacuolar degeneration in hippocampal cortex of aging and demented patients. A quantitative study
    • Ball MJ. Topographic distribution of neurofibrillary tangles and granulovacuolar degeneration in hippocampal cortex of aging and demented patients. A quantitative study. Acta Neuropathol 1978; 42: 73-80
    • (1978) Acta Neuropathol , vol.42 , pp. 73-80
    • Ball, M.J.1
  • 4
    • 77953293462 scopus 로고    scopus 로고
    • Immunopositivity for ESCRT-III subunit CHMP2B in granulovacuolar degeneration of neurons in the Alzheimer's disease hippocampus
    • Yamazaki Y, Takahashi T, Hiji M, Kurashige T, Izumi Y, Yamawaki T, Matsumoto M. Immunopositivity for ESCRT-III subunit CHMP2B in granulovacuolar degeneration of neurons in the Alzheimer's disease hippocampus. Neurosci Lett 2010; 477: 86-90
    • (2010) Neurosci Lett , vol.477 , pp. 86-90
    • Yamazaki, Y.1    Takahashi, T.2    Hiji, M.3    Kurashige, T.4    Izumi, Y.5    Yamawaki, T.6    Matsumoto, M.7
  • 5
    • 33751256001 scopus 로고    scopus 로고
    • Relation of hippocampal phospho-SAPK/JNK granules in Alzheimer's disease and tauopathies to granulovacuolar degeneration bodies
    • Lagalwar S, Berry RW, Binder LI. Relation of hippocampal phospho-SAPK/JNK granules in Alzheimer's disease and tauopathies to granulovacuolar degeneration bodies. Acta Neuropathol 2007; 113: 63-73
    • (2007) Acta Neuropathol , vol.113 , pp. 63-73
    • Lagalwar, S.1    Berry, R.W.2    Binder, L.I.3
  • 6
    • 0017645498 scopus 로고
    • Granulovacuolar degeneration in the ageing brain and in dementia
    • Ball MJ, Lo P. Granulovacuolar degeneration in the ageing brain and in dementia. J Neuropathol Exp Neurol 1977; 36: 474-87
    • (1977) J Neuropathol Exp Neurol , vol.36 , pp. 474-487
    • Ball, M.J.1    Lo, P.2
  • 7
    • 0017358355 scopus 로고
    • Neuronal loss, neurofibrillary tangles and granulovacuolar degeneration in the hippocampus with ageing and dementia. A quantitative study
    • Ball MJ. Neuronal loss, neurofibrillary tangles and granulovacuolar degeneration in the hippocampus with ageing and dementia. A quantitative study. Acta Neuropathol 1977; 37: 111-18
    • (1977) Acta Neuropathol , vol.37 , pp. 111-118
    • Ball, M.J.1
  • 8
    • 0036434880 scopus 로고    scopus 로고
    • Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer's disease
    • Ghoshal N, Garcia-Sierra F, Wuu J, Leurgans S, Bennett DA, Berry RW, Binder LI. Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer's disease. Exp Neurol 2002; 177: 475-93
    • (2002) Exp Neurol , vol.177 , pp. 475-493
    • Ghoshal, N.1    Garcia-Sierra, F.2    Wuu, J.3    Leurgans, S.4    Bennett, D.A.5    Berry, R.W.6    Binder, L.I.7
  • 10
    • 0014359297 scopus 로고
    • Studies on cellular autophagocytosis. The formation of autophagic vacuoles in the liver after glucagon administration
    • Arstila AU, Trump BF. Studies on cellular autophagocytosis. The formation of autophagic vacuoles in the liver after glucagon administration. Am J Pathol 1968; 53: 687-733
    • (1968) Am J Pathol , vol.53 , pp. 687-733
    • Arstila, A.U.1    Trump, B.F.2
  • 13
    • 0025340880 scopus 로고
    • Studies on the mechanisms of autophagy: maturation of the autophagic vacuole
    • Dunn WA, Jr. Studies on the mechanisms of autophagy: maturation of the autophagic vacuole. J Cell Biol 1990; 110: 1935-45
    • (1990) J Cell Biol , vol.110 , pp. 1935-1945
    • Dunn Jr, W.A.1
  • 14
    • 26844531363 scopus 로고    scopus 로고
    • Maturation of autophagic vacuoles in Mammalian cells
    • Eskelinen EL. Maturation of autophagic vacuoles in Mammalian cells. Autophagy 2005; 1: 1-10
    • (2005) Autophagy , vol.1 , pp. 1-10
    • Eskelinen, E.L.1
  • 15
    • 57649195400 scopus 로고    scopus 로고
    • Autophagy and multivesicular bodies: two closely related partners
    • Fader CM, Colombo MI. Autophagy and multivesicular bodies: two closely related partners. Cell Death Differ 2009; 16: 70-8
    • (2009) Cell Death Differ , vol.16 , pp. 70-78
    • Fader, C.M.1    Colombo, M.I.2
  • 16
    • 49049096562 scopus 로고    scopus 로고
    • Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease
    • Boland B, Kumar A, Lee S, Platt FM, Wegiel J, Yu WH, Nixon RA. Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease. J Neurosci 2008; 28: 6926-37
    • (2008) J Neurosci , vol.28 , pp. 6926-6937
    • Boland, B.1    Kumar, A.2    Lee, S.3    Platt, F.M.4    Wegiel, J.5    Yu, W.H.6    Nixon, R.A.7
  • 17
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjorkoy G, Lamark T, Brech A, Outzen H, Perander M, Overvatn A, Stenmark H, Johansen T. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol 2005; 171: 603-14
    • (2005) J Cell Biol , vol.171 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 20
    • 33646234697 scopus 로고    scopus 로고
    • Casein kinase-1 isoforms differentially associate with neurofibrillary and granulovacuolar degeneration lesions
    • Kannanayakal TJ, Tao H, Vandre DD, Kuret J. Casein kinase-1 isoforms differentially associate with neurofibrillary and granulovacuolar degeneration lesions. Acta Neuropathol 2006; 111: 413-21
    • (2006) Acta Neuropathol , vol.111 , pp. 413-421
    • Kannanayakal, T.J.1    Tao, H.2    Vandre, D.D.3    Kuret, J.4
  • 21
    • 0025787549 scopus 로고
    • Sequestration of tau by granulovacuolar degeneration in Alzheimer's disease
    • Bondareff W, Wischik CM, Novak M, Roth M. Sequestration of tau by granulovacuolar degeneration in Alzheimer's disease. Am J Pathol 1991; 139: 641-7
    • (1991) Am J Pathol , vol.139 , pp. 641-647
    • Bondareff, W.1    Wischik, C.M.2    Novak, M.3    Roth, M.4
  • 22
    • 0023260938 scopus 로고
    • A monoclonal antibody that recognizes a phosphorylated epitope in Alzheimer neurofibrillary tangles, neurofilaments and tau proteins immunostains granulovacuolar degeneration
    • Dickson DW, Ksiezak-Reding H, Davies P, Yen SH. A monoclonal antibody that recognizes a phosphorylated epitope in Alzheimer neurofibrillary tangles, neurofilaments and tau proteins immunostains granulovacuolar degeneration. Acta Neuropathol 1987; 73: 254-8
    • (1987) Acta Neuropathol , vol.73 , pp. 254-258
    • Dickson, D.W.1    Ksiezak-Reding, H.2    Davies, P.3    Yen, S.H.4
  • 24
    • 0026717027 scopus 로고
    • New patterns of intraneuronal accumulation of the microtubular binding domain of tau in granulovacuolar degeneration
    • Mena R, Robitaille Y, Cuello AC. New patterns of intraneuronal accumulation of the microtubular binding domain of tau in granulovacuolar degeneration. J Geriatr Psychiatry Neurol 1992; 5: 132-41
    • (1992) J Geriatr Psychiatry Neurol , vol.5 , pp. 132-141
    • Mena, R.1    Robitaille, Y.2    Cuello, A.C.3
  • 26
    • 0025908356 scopus 로고
    • The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease
    • Mirra SS, Heyman A, McKeel D, Sumi SM, Crain BJ, Brownlee LM, Vogel FS, Hughes JP, van Belle G, Berg L. The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease. Neurology 1991; 41: 479-86
    • (1991) Neurology , vol.41 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3    Sumi, S.M.4    Crain, B.J.5    Brownlee, L.M.6    Vogel, F.S.7    Hughes, J.P.8    van Belle, G.9    Berg, L.10
  • 27
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H, Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 1991; 82: 239-59
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 28
    • 0031850680 scopus 로고    scopus 로고
    • Antigen retrieval in formaldehyde-fixed human brain tissue
    • Evers P, Uylings HB, Suurmeijer AJ. Antigen retrieval in formaldehyde-fixed human brain tissue. Methods 1998; 15: 133-40
    • (1998) Methods , vol.15 , pp. 133-140
    • Evers, P.1    Uylings, H.B.2    Suurmeijer, A.J.3
  • 29
    • 0033022410 scopus 로고    scopus 로고
    • Reduction of lipofuscin-like autofluorescence in fluorescently labeled tissue
    • Schnell SA, Staines WA, Wessendorf MW. Reduction of lipofuscin-like autofluorescence in fluorescently labeled tissue. J Histochem Cytochem 1999; 47: 719-30
    • (1999) J Histochem Cytochem , vol.47 , pp. 719-730
    • Schnell, S.A.1    Staines, W.A.2    Wessendorf, M.W.3
  • 30
    • 0032583107 scopus 로고    scopus 로고
    • Improved confidence intervals for the difference between binomial proportions based on paired data
    • Newcombe RG. Improved confidence intervals for the difference between binomial proportions based on paired data. Stat Med 1998; 17: 2635-50
    • (1998) Stat Med , vol.17 , pp. 2635-2650
    • Newcombe, R.G.1
  • 31
    • 4344712684 scopus 로고    scopus 로고
    • Methods for monitoring autophagy
    • Mizushima N. Methods for monitoring autophagy. Int J Biochem Cell Biol 2004; 36: 2491-502
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2491-2502
    • Mizushima, N.1
  • 32
    • 34548077575 scopus 로고    scopus 로고
    • Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3
    • Kimura S, Noda T, Yoshimori T. Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3. Autophagy 2007; 3: 452-60
    • (2007) Autophagy , vol.3 , pp. 452-460
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 33
    • 77952362726 scopus 로고    scopus 로고
    • Immunohistochemical evidence for macroautophagy in neurons and endothelial cells in Alzheimer's disease
    • Ma JF, Huang Y, Chen SD, Halliday G. Immunohistochemical evidence for macroautophagy in neurons and endothelial cells in Alzheimer's disease. Neuropathol Appl Neurobiol 2010; 36: 312-19
    • (2010) Neuropathol Appl Neurobiol , vol.36 , pp. 312-319
    • Ma, J.F.1    Huang, Y.2    Chen, S.D.3    Halliday, G.4
  • 34
    • 0035919837 scopus 로고    scopus 로고
    • Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies
    • Kuusisto E, Salminen A, Alafuzoff I. Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies. Neuroreport 2001; 12: 2085-90
    • (2001) Neuroreport , vol.12 , pp. 2085-2090
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 35
    • 0036284021 scopus 로고    scopus 로고
    • Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: possible role in tangle formation
    • Kuusisto E, Salminen A, Alafuzoff I. Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: possible role in tangle formation. Neuropathol Appl Neurobiol 2002; 28: 228-37
    • (2002) Neuropathol Appl Neurobiol , vol.28 , pp. 228-237
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 40
    • 0028886612 scopus 로고
    • Age-related changes in cellular localization and enzymatic activities of cathepsins B, L and D in the rat trigeminal ganglion neuron
    • Amano T, Nakanishi H, Kondo T, Tanaka T, Oka M, Yamamoto K. Age-related changes in cellular localization and enzymatic activities of cathepsins B, L and D in the rat trigeminal ganglion neuron. Mech Ageing Dev 1995; 83: 133-41
    • (1995) Mech Ageing Dev , vol.83 , pp. 133-141
    • Amano, T.1    Nakanishi, H.2    Kondo, T.3    Tanaka, T.4    Oka, M.5    Yamamoto, K.6
  • 41
    • 0026695737 scopus 로고
    • Lumenal labeling of rat hepatocyte endocytic compartments. Distribution of several acid hydrolases and membrane receptors
    • Casciola-Rosen LA, Renfrew CA, Hubbard AL. Lumenal labeling of rat hepatocyte endocytic compartments. Distribution of several acid hydrolases and membrane receptors. J Biol Chem 1992; 267: 11856-64
    • (1992) J Biol Chem , vol.267 , pp. 11856-11864
    • Casciola-Rosen, L.A.1    Renfrew, C.A.2    Hubbard, A.L.3
  • 42
    • 0025790486 scopus 로고
    • Acid hydrolases in early and late endosome fractions from rat liver
    • Runquist EA, Havel RJ. Acid hydrolases in early and late endosome fractions from rat liver. J Biol Chem 1991; 266: 22557-63
    • (1991) J Biol Chem , vol.266 , pp. 22557-22563
    • Runquist, E.A.1    Havel, R.J.2
  • 43
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • Raiborg C, Stenmark H. The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 2009; 458: 445-52
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 48
    • 53549113031 scopus 로고    scopus 로고
    • The role of TOR in autophagy regulation from yeast to plants and mammals
    • Diaz-Troya S, Perez-Perez ME, Florencio FJ, Crespo JL. The role of TOR in autophagy regulation from yeast to plants and mammals. Autophagy 2008; 4: 851-65
    • (2008) Autophagy , vol.4 , pp. 851-865
    • Diaz-Troya, S.1    Perez-Perez, M.E.2    Florencio, F.J.3    Crespo, J.L.4
  • 49
    • 23844457609 scopus 로고    scopus 로고
    • Levels of mTOR and its downstream targets 4E-BP1, eEF2, and eEF2 kinase in relationships with tau in Alzheimer's disease brain
    • Li X, Alafuzoff I, Soininen H, Winblad B, Pei JJ. Levels of mTOR and its downstream targets 4E-BP1, eEF2, and eEF2 kinase in relationships with tau in Alzheimer's disease brain. FEBS J 2005; 272: 4211-20
    • (2005) FEBS J , vol.272 , pp. 4211-4220
    • Li, X.1    Alafuzoff, I.2    Soininen, H.3    Winblad, B.4    Pei, J.J.5
  • 50
    • 77950900079 scopus 로고    scopus 로고
    • mTOR Ser-2481 autophosphorylation monitors mTORC-specific catalytic activity and clarifies rapamycin mechanism of action
    • Soliman GA, Acosta-Jaquez HA, Dunlop EA, Ekim B, Maj NE, Tee AR, Fingar DC. mTOR Ser-2481 autophosphorylation monitors mTORC-specific catalytic activity and clarifies rapamycin mechanism of action. J Biol Chem 2010; 285: 7866-79
    • (2010) J Biol Chem , vol.285 , pp. 7866-7879
    • Soliman, G.A.1    Acosta-Jaquez, H.A.2    Dunlop, E.A.3    Ekim, B.4    Maj, N.E.5    Tee, A.R.6    Fingar, D.C.7
  • 51
    • 0014276827 scopus 로고
    • The fine structure of some intraganglionic alterations. Neurofibrillary tangles, granulovacuolar bodies and 'rod-like' structures as seen in Guam amyotrophic lateral sclerosis and parkinsonism-dementia complex
    • Hirano A, Dembitzer HM, Kurland LT, Zimmerman HM. The fine structure of some intraganglionic alterations. Neurofibrillary tangles, granulovacuolar bodies and 'rod-like' structures as seen in Guam amyotrophic lateral sclerosis and parkinsonism-dementia complex. J Neuropathol Exp Neurol 1968; 27: 167-82
    • (1968) J Neuropathol Exp Neurol , vol.27 , pp. 167-182
    • Hirano, A.1    Dembitzer, H.M.2    Kurland, L.T.3    Zimmerman, H.M.4
  • 52
    • 68149159190 scopus 로고    scopus 로고
    • Phosphorylation-dependent TDP-43 antibody detects intraneuronal dot-like structures showing morphological characters of granulovacuolar degeneration
    • Kadokura A, Yamazaki T, Kakuda S, Makioka K, Lemere CA, Fujita Y, Takatama M, Okamoto K. Phosphorylation-dependent TDP-43 antibody detects intraneuronal dot-like structures showing morphological characters of granulovacuolar degeneration. Neurosci Lett 2009; 463: 87-92
    • (2009) Neurosci Lett , vol.463 , pp. 87-92
    • Kadokura, A.1    Yamazaki, T.2    Kakuda, S.3    Makioka, K.4    Lemere, C.A.5    Fujita, Y.6    Takatama, M.7    Okamoto, K.8
  • 54
    • 0015313489 scopus 로고
    • Granulovacuolar degeneration of hippocampal pyramidal cells
    • Tomlinson BE, Kitchener D. Granulovacuolar degeneration of hippocampal pyramidal cells. J Pathol 1972; 106: 165-85
    • (1972) J Pathol , vol.106 , pp. 165-185
    • Tomlinson, B.E.1    Kitchener, D.2
  • 55
    • 11444267601 scopus 로고    scopus 로고
    • Endosome function and dysfunction in Alzheimer's disease and other neurodegenerative diseases
    • Nixon RA. Endosome function and dysfunction in Alzheimer's disease and other neurodegenerative diseases. Neurobiol Aging 2005; 26: 373-82
    • (2005) Neurobiol Aging , vol.26 , pp. 373-382
    • Nixon, R.A.1
  • 56
    • 77950863406 scopus 로고    scopus 로고
    • Molecular mechanism of multivesicular body biogenesis by ESCRT complexes
    • Wollert T, Hurley JH. Molecular mechanism of multivesicular body biogenesis by ESCRT complexes. Nature 2010; 464: 864-9
    • (2010) Nature , vol.464 , pp. 864-869
    • Wollert, T.1    Hurley, J.H.2
  • 58
    • 66449123730 scopus 로고    scopus 로고
    • Rab7 regulates late endocytic trafficking downstream of multivesicular body biogenesis and cargo sequestration
    • Vanlandingham PA, Ceresa BP. Rab7 regulates late endocytic trafficking downstream of multivesicular body biogenesis and cargo sequestration. J Biol Chem 2009; 284: 12110-24
    • (2009) J Biol Chem , vol.284 , pp. 12110-12124
    • Vanlandingham, P.A.1    Ceresa, B.P.2
  • 60
    • 0034676037 scopus 로고    scopus 로고
    • The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway
    • Kirisako T, Ichimura Y, Okada H, Kabeya Y, Mizushima N, Yoshimori T, Ohsumi M, Takao T, Noda T, Ohsumi Y. The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway. J Cell Biol 2000; 151: 263-75
    • (2000) J Cell Biol , vol.151 , pp. 263-275
    • Kirisako, T.1    Ichimura, Y.2    Okada, H.3    Kabeya, Y.4    Mizushima, N.5    Yoshimori, T.6    Ohsumi, M.7    Takao, T.8    Noda, T.9    Ohsumi, Y.10
  • 62
    • 11144328933 scopus 로고    scopus 로고
    • Protein kinase CK1δ phosphorylates key sites in the acidic domain of murine double-minute clone 2 protein (MDM2) that regulate p53 turnover
    • Winter M, Milne D, Dias S, Kulikov R, Knippschild U, Blattner C, Meek D. Protein kinase CK1δ phosphorylates key sites in the acidic domain of murine double-minute clone 2 protein (MDM2) that regulate p53 turnover. Biochemistry 2004; 43: 16356-64
    • (2004) Biochemistry , vol.43 , pp. 16356-16364
    • Winter, M.1    Milne, D.2    Dias, S.3    Kulikov, R.4    Knippschild, U.5    Blattner, C.6    Meek, D.7
  • 64
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • Katzmann DJ, Odorizzi G, Emr SD. Receptor downregulation and multivesicular-body sorting. Nat Rev Mol Cell Biol 2002; 3: 893-905
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 66
    • 0034604290 scopus 로고    scopus 로고
    • Casein kinase I-dependent phosphorylation within a PEST sequence and ubiquitination at nearby lysines signal endocytosis of yeast uracil permease
    • Marchal C, Haguenauer-Tsapis R, Urban-Grimal D. Casein kinase I-dependent phosphorylation within a PEST sequence and ubiquitination at nearby lysines signal endocytosis of yeast uracil permease. J Biol Chem 2000; 275: 23608-14
    • (2000) J Biol Chem , vol.275 , pp. 23608-23614
    • Marchal, C.1    Haguenauer-Tsapis, R.2    Urban-Grimal, D.3
  • 69
    • 70849093011 scopus 로고    scopus 로고
    • The Rac1/MKK7/JNK pathway signals upregulation of Atg5 and subsequent autophagic cell death in response to oncogenic Ras
    • Byun JY, Yoon CH, An S, Park IC, Kang CM, Kim MJ, Lee SJ. The Rac1/MKK7/JNK pathway signals upregulation of Atg5 and subsequent autophagic cell death in response to oncogenic Ras. Carcinogenesis 2009; 30: 1880-8
    • (2009) Carcinogenesis , vol.30 , pp. 1880-1888
    • Byun, J.Y.1    Yoon, C.H.2    An, S.3    Park, I.C.4    Kang, C.M.5    Kim, M.J.6    Lee, S.J.7


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