메뉴 건너뛰기




Volumn 37, Issue 7, 2010, Pages 707-712

SUMOylation and PML NBs formation

Author keywords

FRET; PML NBs; RNF4; SUMOylation

Indexed keywords

MAMMALIA;

EID: 77958472355     PISSN: 10003282     EISSN: None     Source Type: Journal    
DOI: 10.3724/SP.J.1206.2010.00017     Document Type: Review
Times cited : (1)

References (48)
  • 1
    • 0033561797 scopus 로고    scopus 로고
    • Deconstructing a disease: RARα, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia
    • Melnick A, Licht J D. Deconstructing a desease: RARa, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia. Blood, 1999, 93(10): 3167-3215 (Pubitemid 29220886)
    • (1999) Blood , vol.93 , Issue.10 , pp. 3167-3215
    • Melnick, A.1    Licht, J.D.2
  • 2
    • 67651180759 scopus 로고    scopus 로고
    • Targeting promyelocytic leukemia protein: A means to regulating PML nuclear bodies
    • Reineke E L, Kao H Y. Targeting promyelocytic leukemia protein: a means to regulating PML nuclear bodies. Int J Biol Sci, 2009, 5(4): 366-376
    • (2009) Int J Biol Sci , vol.5 , Issue.4 , pp. 366-376
    • Reineke, E.L.1    Kao, H.Y.2
  • 3
    • 77449089538 scopus 로고    scopus 로고
    • A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics
    • Damme E V, Laukens K, Dang T H, et al. A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics. Int J Biol Sci, 2010, 6(1): 51-67
    • (2010) Int J Biol Sci , vol.6 , Issue.1 , pp. 51-67
    • Damme, E.V.1    Laukens, K.2    Dang, T.H.3
  • 4
    • 77956202370 scopus 로고    scopus 로고
    • Assembly dynamics of PML nuclear bodies in living cells
    • Brand P, Lenser T, Peter Hemmerich. Assembly dynamics of PML nuclear bodies in living cells. PMC Biophysics, 2010, 3: 3
    • (2010) PMC Biophysics , vol.3 , pp. 3
    • Brand, P.1    Lenser, T.2    Hemmerich, P.3
  • 5
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodies: Dynamic sensors of DNA damage and cellular stress
    • DOI 10.1002/bies.20089
    • Dellaire G, Bazett-Jones D P. PML nuclear bodies: dynamic sensors of DNA damage and celluar stress. Bioessays, 2004, 26(9): 963-977 (Pubitemid 39273070)
    • (2004) BioEssays , vol.26 , Issue.9 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 6
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • DOI 10.1038/nrm2277, PII NRM2277
    • Bernardi R, Pandolfi P P. Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat Rev Mol Cell Biol, 2007, 8(10): 1006-1016 (Pubitemid 350174636)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.12 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 7
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of posttranslational glycosylation and phosphorylation of proteins from the amino acid sequence
    • Blom N, Sicheritz-Pontén T, Gupta R, et al. Prediction of posttranslational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics, 2004, (4): 1633-1649
    • (2004) Proteomics , vol.4 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Pontén, T.2    Gupta, R.3
  • 8
    • 69949164620 scopus 로고    scopus 로고
    • PML: An emerging tumor suppressor and a target with therapeutic potential
    • Reineke E L, Kao H Y. PML: An emerging tumor suppressor and a target with therapeutic potential. Cancer Ther, 2009, 7(A): 219-226
    • (2009) Cancer Ther , vol.7 , pp. 219-226
    • Reineke, E.L.1    Kao, H.Y.2
  • 9
    • 0036170782 scopus 로고    scopus 로고
    • Metabolic-energydependent movement of PML bodies within the mammalian cell nucleus
    • Muratani M, Gerlich D, Janicki S M, et al. Metabolic-energydependent movement of PML bodies within the mammalian cell nucleus. Nature Cell Biol, 2002, 4(2): 106-110
    • (2002) Nature Cell Biol , vol.4 , Issue.2 , pp. 106-110
    • Muratani, M.1    Gerlich, D.2    Janicki, S.M.3
  • 10
    • 1542304599 scopus 로고    scopus 로고
    • Chromatin Contributes to Structural Integrity of Promyelocytic Leukemia Bodies through a SUMO-1-independent Mechanism
    • DOI 10.1074/jbc.M312580200
    • Eskiw C H, Dellaire G, Bazett-Jones D P. Chromatin contributes to structural integrity of promyelocytic leukemia bodies through a SUMO-1 independent mechanism. Biol Chem, 2004, 279 (10): 9577-9585 (Pubitemid 38296026)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.10 , pp. 9577-9585
    • Eskiw, C.H.1    Dellaire, G.2    Bazett-Jones, D.P.3
  • 11
    • 0242550970 scopus 로고    scopus 로고
    • Size, position and dynamic behavior of PML nuclear bodies following cell stress as a paradigm for supramolecular trafficking and assembly
    • Eskiw C H, Dellaire G, Mymryk J, et al. Size, position and dynamic behavior of PML nuclear bodies following cell stress as a paradigm for supramolecular trafficking and assembly. Cell Sci, 2003, 116(part21): 4455-4466
    • (2003) Cell Sci , vol.116 , Issue.PART 21 , pp. 4455-4466
    • Eskiw, C.H.1    Dellaire, G.2    Mymryk, J.3
  • 12
    • 63849264460 scopus 로고    scopus 로고
    • Expanding PML's functional repertoire through post-translational mechanisms
    • Nichol J N, Petruccelli L A, Miller W H. Expanding PML's functional repertoire through post-translational mechanisms. Frontiers in Bioscience, 2009, 14: 2293-2306
    • (2009) Frontiers in Bioscience , vol.14 , pp. 2293-2306
    • Nichol, J.N.1    Petruccelli, L.A.2    Miller, W.H.3
  • 13
    • 0142106346 scopus 로고    scopus 로고
    • Cellular stress and DNA damage invoke temporally distinct Mdm2, P53, and PML complexes and damage-specific nuclear relocalization
    • Kurki S, Latonen L, Laiho M. Cellular stress and DNA damage invoke temporally distinct Mdm2, P53, and PML complexes and damage-specific nuclear relocalization. Cell Sci, 2003, 116(part19): 3917-3925
    • (2003) Cell Sci , vol.116 , Issue.PART 19 , pp. 3917-3925
    • Kurki, S.1    Latonen, L.2    Laiho, M.3
  • 14
    • 33645731002 scopus 로고    scopus 로고
    • The number of PML nuclear bodies increases in early S phase by a fission mechanism
    • Dellaire G, Ching R W, Dehghani H, et al. The number of PML nuclear bodies increases in early S phase by a fission mechanism. Cell Sci, 2006, 119(part6): 1026-1033
    • (2006) Cell Sci , vol.119 , Issue.PART 6 , pp. 1026-1033
    • Dellaire, G.1    Ching, R.W.2    Dehghani, H.3
  • 15
    • 33645749156 scopus 로고    scopus 로고
    • Mitotic accumulations of PML protein contribute to the re-establishment of PML nuclear bodies in G1
    • Dellaire G, Eskiw C H, Dehghani H, et al. Mitotic accumulations of PML protein contribute to the re-establishment of PML nuclear bodies in G1. Cell Sci, 2006, 119(part6): 1034-1042
    • (2006) Cell Sci , vol.119 , Issue.PART 6 , pp. 1034-1042
    • Dellaire, G.1    Eskiw, C.H.2    Dehghani, H.3
  • 16
    • 0037255042 scopus 로고    scopus 로고
    • The Nuclear Protein Database (NPD): Sub-nuclear localisation and functional annotation of the nuclear proteome
    • DOI 10.1093/nar/gkg018
    • Dellaire G, Farrall R, Bickmore W A. The nuclear protein database (NPD): sub-nuclear localization and functional annotation of the nuclear proteome. Nucl Acids Res, 2003, 31(1): 328-330 (Pubitemid 36157283)
    • (2003) Nucleic Acids Research , vol.31 , Issue.1 , pp. 328-330
    • Dellaire, G.1    Farrall, R.2    Bickmore, W.A.3
  • 17
    • 0343776952 scopus 로고    scopus 로고
    • Roel of SUMO-1 modified PML in nuclear body formation
    • Zhong S, Müller S, Ronchetti S, et al. Roel of SUMO-1 modified PML in nuclear body formation. Blood, 2000, 95(9): 2748-2752
    • (2000) Blood , vol.95 , Issue.9 , pp. 2748-2752
    • Zhong, S.1    Müller, S.2    Ronchetti, S.3
  • 18
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • Rodriguez M S, Dargemont C, Hay R T. SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J Biol Chem, 2001, 276: 12654-12659
    • (2001) J Biol Chem , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 19
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • Hay R T. SUMO: a history of modification. Mol Cell, 2005, 18(1): 1-12
    • (2005) Mol Cell , vol.18 , Issue.1 , pp. 1-12
    • Hay, R.T.1
  • 20
    • 33748525164 scopus 로고    scopus 로고
    • Role of desumoylation in the development if prostate cancer
    • Cheng J, Bawa T, Leey P, et al. Role of desumoylation in the development if prostate cancer. Neoplasia, 2006, 8(8): 667-676
    • (2006) Neoplasia , vol.8 , Issue.8 , pp. 667-676
    • Cheng, J.1    Bawa, T.2    Leey, P.3
  • 21
    • 72449163470 scopus 로고    scopus 로고
    • The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress
    • Morris J R, Boutell C, Keppler M, et al. The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress. Nature, 2009, 462: 886-892
    • (2009) Nature , vol.462 , pp. 886-892
    • Morris, J.R.1    Boutell, C.2    Keppler, M.3
  • 22
    • 40749131181 scopus 로고    scopus 로고
    • Emerging roles of the SUMO pathway in mitosis
    • Dasso M. Emerging roles of the SUMO pathway in mitosis. Cell Division, 2008, 3: 5
    • (2008) Cell Division , vol.3 , pp. 5
    • Dasso, M.1
  • 23
    • 4444301185 scopus 로고    scopus 로고
    • SUMO and ubiquitin in the nucleus: Different functions, similar mechanisms?
    • DOI 10.1101/gad.1214604
    • Gill G. SUMO and ubiquitin in the nucleus: different functions, similar mechanisms?. Genes Dev, 2004, 18: 2046-2059 (Pubitemid 39166622)
    • (2004) Genes and Development , vol.18 , Issue.17 , pp. 2046-2059
    • Gill, G.1
  • 24
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • Rodriguez M S, Dargemont C, Hay R T. SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. Biol Chem, 2001, 276(16): 12654-12659
    • (2001) Biol Chem , vol.276 , Issue.16 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 25
    • 24644522876 scopus 로고    scopus 로고
    • Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3
    • Fu C H, Ahmed K, Ding H S, et al. Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3. Oncogene, 2005, 24(35): 5401-5413
    • (2005) Oncogene , vol.24 , Issue.35 , pp. 5401-5413
    • Fu, C.H.1    Ahmed, K.2    Ding, H.S.3
  • 26
    • 0035929557 scopus 로고    scopus 로고
    • Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9
    • Tatham M H, Jaffray E, Vaughan O A, et al. Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. Biol Chem, 2001, 276(38): 35368-35364
    • (2001) Biol Chem , vol.276 , Issue.38 , pp. 35368-135364
    • Tatham, M.H.1    Jaffray, E.2    Vaughan, O.A.3
  • 27
    • 33847372862 scopus 로고    scopus 로고
    • A fluorescenceresonance-energy-transfer- Based protease activity assay and its use to monitor paralog-specific small ubiquitin-like modifier processing
    • Martin S F, Hattersley N, Samuel I D W, et al. A fluorescenceresonance- energy-transfer- based protease activity assay and its use to monitor paralog-specific small ubiquitin-like modifier processing. Anal Biochem, 2007, 363(1): 38-45
    • (2007) Anal Biochem , vol.363 , Issue.1 , pp. 38-45
    • Martin, S.F.1    Hattersley, N.2    Samuel, I.D.W.3
  • 28
    • 27644557275 scopus 로고    scopus 로고
    • A fluorescence resonance energy transfer-based assay to study SUMO modification in solution
    • DOI 10.1016/S0076-6879(05)98003-8, PII S0076687905980038, Ubiquitin and Protein Degradation (Part A)
    • Bossis G, Chmielarska K, Gartner U. A fluorescence resonance energy transfer-based assay to study SUMO modification in solution. Methods Enzymol, 2005, 398: 20-32 (Pubitemid 41578871)
    • (2005) Methods in Enzymology , vol.398 , pp. 20-32
    • Bossis, G.1    Chmielarska, K.2    Gartner, U.3    Pichler, A.4    Stieger, E.5    Melchior, F.6
  • 29
    • 33748990136 scopus 로고    scopus 로고
    • SUSP1 antagonizes formation of highly SUMO2/3-conjugated species
    • Mukhopadhyay D, Ayaydin F, Kolli N, et al. SUSP1 antagonizes formation of highly SUMO2/3-conjugated species. J Cell Biol, 2006, 174(7): 939-949
    • (2006) J Cell Biol , vol.174 , Issue.7 , pp. 939-949
    • Mukhopadhyay, D.1    Ayaydin, F.2    Kolli, N.3
  • 30
    • 28444448039 scopus 로고    scopus 로고
    • The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice
    • Nacerddine K, Lehembre F, Bhaumik M, et al. The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice. Dev Cell, 2005, 9(6): 769-779
    • (2005) Dev Cell , vol.9 , Issue.6 , pp. 769-779
    • Nacerddine, K.1    Lehembre, F.2    Bhaumik, M.3
  • 31
    • 0036809116 scopus 로고    scopus 로고
    • SUMO-1 protease-1 regulates gene transcription through PML
    • Best J L, Ganiatsas S, Agarwal S, et al. SUMO-1 protease-1 regulates gene transcription through PML. Mol Cell, 2002, 10(4): 843-855
    • (2002) Mol Cell , vol.10 , Issue.4 , pp. 843-855
    • Best, J.L.1    Ganiatsas, S.2    Agarwal, S.3
  • 32
    • 33744940842 scopus 로고    scopus 로고
    • Specification of SUMO1- And SUMO2- interacting motifs
    • Hecker C M, Rabiller M, Haglund K, et al. Specification of SUMO1- and SUMO2- interacting motifs. Biol Chem, 2006, 281(23): 16117-16127
    • (2006) Biol Chem , vol.281 , Issue.23 , pp. 16117-16127
    • Hecker, C.M.1    Rabiller, M.2    Haglund, K.3
  • 33
    • 5144219680 scopus 로고    scopus 로고
    • Identification of a SUMO-binding motif that recognizes SUMO-modified proteins
    • Song J, Durrin L K, Wilkinson T A, et al: Identification of a SUMO-binding motif that recognizes SUMO-modified proteins. Proc Natl Acad Sci USA, 2004, 101(40): 14373-14378
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.40 , pp. 14373-14378
    • Song, J.1    Durrin, L.K.2    Wilkinson, T.A.3
  • 34
    • 33750447586 scopus 로고    scopus 로고
    • The mechanisms of PML-nuclear body formation
    • Shen T H, Lin H K, Scaglioni P P, et al: The mechanisms of PML-nuclear body formation. Mol Cell, 2006, 24(3): 331-339
    • (2006) Mol Cell , vol.24 , Issue.3 , pp. 331-339
    • Shen, T.H.1    Lin, H.K.2    Scaglioni, P.P.3
  • 35
    • 14044278774 scopus 로고    scopus 로고
    • Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein
    • Takahashi H, Hatakeyama S, Saitoh H, et al. Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein. Biol Chem, 2005, 280(7): 5611-5621
    • (2005) Biol Chem , vol.280 , Issue.7 , pp. 5611-5621
    • Takahashi, H.1    Hatakeyama, S.2    Saitoh, H.3
  • 36
  • 37
    • 0036715589 scopus 로고    scopus 로고
    • How acute promyelocytic leukaemia revived arsenic
    • Zhu J, Chen Z, Lallemand-Breitenbach V, et al. How acute promyelocytic leukaemia revived arsenic. Nature Rev Cancer, 2002, 2(9): 705-713
    • (2002) Nature Rev Cancer , vol.2 , Issue.9 , pp. 705-713
    • Zhu, J.1    Chen, Z.2    Lallemand-Breitenbach, V.3
  • 38
    • 43049093756 scopus 로고    scopus 로고
    • RNF4 is a poly-SUMOspecific E3 ubiquitin ligase required for arsenic-induced PML degradation
    • Tatham M H, Geoffroy M C, Shen L, et al. RNF4 is a poly-SUMOspecific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat Cell Bio, 2008, 10(5): 538-547
    • (2008) Nat Cell Bio , vol.10 , Issue.5 , pp. 538-547
    • Tatham, M.H.1    Geoffroy, M.C.2    Shen, L.3
  • 39
    • 43049147640 scopus 로고    scopus 로고
    • Marked for death
    • Petrie K, Zelent A. Marked for death. Nature Cell Bio, 2008, 10(5): 507-509
    • (2008) Nature Cell Bio , vol.10 , Issue.5 , pp. 507-509
    • Petrie, K.1    Zelent, A.2
  • 40
    • 43049096803 scopus 로고    scopus 로고
    • Arsenic degrades PML or PML-RARa through a SUMO-triggered RNF4/ ubiquitin-mediated pathway
    • Lanllemand-Breitenbach V, Jeanne M, Benhenda S, et al. Arsenic degrades PML or PML-RARa through a SUMO-triggered RNF4/ ubiquitin-mediated pathway. Nat Cell Bio, 2008, 10(5): 547-556
    • (2008) Nat Cell Bio , vol.10 , Issue.5 , pp. 547-556
    • Lanllemand-Breitenbach, V.1    Jeanne, M.2    Benhenda, S.3
  • 41
    • 13544254439 scopus 로고    scopus 로고
    • SUMO-1 promotes association of SNURF (RNF4) with PML nuclear bodies
    • Häkli M, Karvonen U, Jänne O A, et al. SUMO-1 promotes association of SNURF (RNF4) with PML nuclear bodies. Exp Cell Res, 2005, 304(1): 224-233
    • (2005) Exp Cell Res , vol.304 , Issue.1 , pp. 224-233
    • Häkli, M.1    Karvonen, U.2    Jänne, O.A.3
  • 42
    • 51249085621 scopus 로고    scopus 로고
    • Arsenic trioxide stimulates SUMO-2/3 modification leading to RNF4-dependent proteolytic targeting of PML
    • Weisshaar S R, Keusekotten K, Krause A, et al. Arsenic trioxide stimulates SUMO-2/3 modification leading to RNF4-dependent proteolytic targeting of PML. FEBS Lett, 2008, 582(21-22): 3174-3178
    • (2008) FEBS Lett , vol.582 , Issue.21-22 , pp. 3174-3178
    • Weisshaar, S.R.1    Keusekotten, K.2    Krause, A.3
  • 43
    • 67650239825 scopus 로고    scopus 로고
    • Role of SUMO in RNF4-mediated PML degradation: PML sumoylation and phospho-switch control of its SUMO Binding Domain dissected in living cells
    • Percherancier Y, Germain-Desprez D, Galisson F, et al. Role of SUMO in RNF4-mediated PML degradation: PML sumoylation and phospho-switch control of its SUMO Binding Domain dissected in living cells. Biol Chem, 2009, 284(24): 16595-16608
    • (2009) Biol Chem , vol.284 , Issue.24 , pp. 16595-16608
    • Percherancier, Y.1    Germain-Desprez, D.2    Galisson, F.3
  • 44
    • 33947387001 scopus 로고    scopus 로고
    • FRETing for a more detailed interactsome
    • Kaganman I. FRETing for a more detailed interactsome. Nat Methods, 2007, 4(2): 112-113
    • (2007) Nat Methods , vol.4 , Issue.2 , pp. 112-113
    • Kaganman, I.1
  • 45
    • 15244362074 scopus 로고    scopus 로고
    • Quantitative imaging of protein interactions in the cell nucleus
    • Voss T C, Demarco I A, Day R N. Quantitative imaging of protein interactions in the cell nucleus. Biotechniques, 2005, 38(3): 413-424
    • (2005) Biotechniques , vol.38 , Issue.3 , pp. 413-424
    • Voss, T.C.1    Demarco, I.A.2    Day, R.N.3
  • 46
    • 0036966365 scopus 로고    scopus 로고
    • Mobile foci of Sp 100 do not contain PML: PML bodies are immobile but PML and Sp100 proteins are not
    • Wiesmeijer K, Molenaar C, Bekeer I M L A, et al. Mobile foci of Sp 100 do not contain PML: PML bodies are immobile but PML and Sp100 proteins are not. Struct Biol, 2002, 140(1-3): 180-188
    • (2002) Struct Biol , vol.140 , Issue.1-3 , pp. 180-188
    • Wiesmeijer, K.1    Molenaar, C.2    Bekeer, I.M.L.A.3
  • 47
    • 33748545640 scopus 로고    scopus 로고
    • Imaging molecular interactions in living cells by FRET microscopy
    • DOI 10.1016/j.cbpa.2006.08.021, PII S1367593106001281, Analytical Techniques/Mechanisms
    • Jares-Erijman E A, Jovin T M. Imaging molecular interactions in living cells by FRET microscopy. Curr Opin Chem Biol, 2006, 10(5): 409-416 (Pubitemid 44375073)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 409-416
    • Jares-Erijman, E.A.1    Jovin, T.M.2
  • 48
    • 13844297577 scopus 로고    scopus 로고
    • Imaging protein molecules using FRET and FLIM microscopy
    • DOI 10.1016/j.copbio.2004.12.002, PII S0958166904001673
    • Wallrabe H, Periasamy A. Imaging protein molecules using FRET and FLIM microscopy. Curr Opin Biotechnol, 2005, 16(1): 19-27 (Pubitemid 40249755)
    • (2005) Current Opinion in Biotechnology , vol.16 , Issue.1 , pp. 19-27
    • Wallrabe, H.1    Periasamy, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.