메뉴 건너뛰기




Volumn 427, Issue 10, 2015, Pages 1934-1948

LRIG1 extracellular domain: Structure and function analysis

Author keywords

EGFR inhibition; leucine rich repeat domain; LINGO 1; stem cell marker

Indexed keywords

EGFR PROTEIN, HUMAN; EPIDERMAL GROWTH FACTOR RECEPTOR; LEUCINE-RICH REPEAT PROTEINS; LIGAND; LRIG1 PROTEIN, HUMAN; MEMBRANE PROTEIN; PROTEIN;

EID: 84939968448     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2015.03.001     Document Type: Article
Times cited : (13)

References (55)
  • 1
    • 84860507194 scopus 로고    scopus 로고
    • Lrig1: A new master regulator of epithelial stem cells
    • P. Ordonez-Moran, and J. Huelsken Lrig1: a new master regulator of epithelial stem cells EMBO J 31 2012 2064 2066
    • (2012) EMBO J , vol.31 , pp. 2064-2066
    • Ordonez-Moran, P.1    Huelsken, J.2
  • 2
    • 84859196824 scopus 로고    scopus 로고
    • The pan-ErbB negative regulator Lrig1 is an intestinal stem cell marker that functions as a tumor suppressor
    • A.E. Powell, Y. Wang, Y. Li, E.J. Poulin, A.L. Means, and M.K. Washington The pan-ErbB negative regulator Lrig1 is an intestinal stem cell marker that functions as a tumor suppressor Cell 149 2012 146 158
    • (2012) Cell , vol.149 , pp. 146-158
    • Powell, A.E.1    Wang, Y.2    Li, Y.3    Poulin, E.J.4    Means, A.L.5    Washington, M.K.6
  • 3
    • 84924898329 scopus 로고    scopus 로고
    • Adenovirus-mediated LRIG1 expression enhances the chemosensitivity of bladder cancer cells to cisplatin
    • Z. Yan, J. Jiang, F. Li, W. Yang, G. Xie, and C. Zhou Adenovirus-mediated LRIG1 expression enhances the chemosensitivity of bladder cancer cells to cisplatin Oncol Rep 33 2015 1791 1798
    • (2015) Oncol Rep , vol.33 , pp. 1791-1798
    • Yan, Z.1    Jiang, J.2    Li, F.3    Yang, W.4    Xie, G.5    Zhou, C.6
  • 4
    • 84859430024 scopus 로고    scopus 로고
    • Lrig1 controls intestinal stem-cell homeostasis by negative regulation of ErbB signalling
    • V.W. Wong, D.E. Stange, M.E. Page, S. Buczacki, A. Wabik, and S. Itami Lrig1 controls intestinal stem-cell homeostasis by negative regulation of ErbB signalling Nat Cell Biol 14 2012 401 408
    • (2012) Nat Cell Biol , vol.14 , pp. 401-408
    • Wong, V.W.1    Stange, D.E.2    Page, M.E.3    Buczacki, S.4    Wabik, A.5    Itami, S.6
  • 5
    • 0029829132 scopus 로고    scopus 로고
    • CDNA cloning of a novel membrane glycoprotein that is expressed specifically in glial cells in the mouse brain. LIG-1, a protein with leucine-rich repeats and immunoglobulin-like domains
    • Y. Suzuki, N. Sato, M. Tohyama, A. Wanaka, and T. Takagi cDNA cloning of a novel membrane glycoprotein that is expressed specifically in glial cells in the mouse brain. LIG-1, a protein with leucine-rich repeats and immunoglobulin-like domains J Biol Chem 271 1996 22522 22527
    • (1996) J Biol Chem , vol.271 , pp. 22522-22527
    • Suzuki, Y.1    Sato, N.2    Tohyama, M.3    Wanaka, A.4    Takagi, T.5
  • 6
    • 8744267487 scopus 로고    scopus 로고
    • The leucine-rich repeat protein LRIG1 is a negative regulator of ErbB family receptor tyrosine kinases
    • M.B. Laederich, M. Funes-Duran, L. Yen, E. Ingalla, X. Wu, and K.L. Carraway The leucine-rich repeat protein LRIG1 is a negative regulator of ErbB family receptor tyrosine kinases J Biol Chem 279 2004 47050 47056
    • (2004) J Biol Chem , vol.279 , pp. 47050-47056
    • Laederich, M.B.1    Funes-Duran, M.2    Yen, L.3    Ingalla, E.4    Wu, X.5    Carraway, K.L.6
  • 7
    • 20844462896 scopus 로고    scopus 로고
    • LRIG1 restricts growth factor signaling by enhancing receptor ubiquitylation and degradation
    • G. Gur, C. Rubin, M. Katz, I. Amit, A. Citri, and J. Nilsson LRIG1 restricts growth factor signaling by enhancing receptor ubiquitylation and degradation EMBO J 23 2004 3270 3281
    • (2004) EMBO J , vol.23 , pp. 3270-3281
    • Gur, G.1    Rubin, C.2    Katz, M.3    Amit, I.4    Citri, A.5    Nilsson, J.6
  • 9
    • 33846281874 scopus 로고    scopus 로고
    • A soluble ectodomain of LRIG1 inhibits cancer cell growth by attenuating basal and ligand-dependent EGFR activity
    • S. Goldoni, R. Iozzo, P. Kay, S. Campbell, A. McQuillan, and C. Agnew A soluble ectodomain of LRIG1 inhibits cancer cell growth by attenuating basal and ligand-dependent EGFR activity Oncogene 26 2007 368 381
    • (2007) Oncogene , vol.26 , pp. 368-381
    • Goldoni, S.1    Iozzo, R.2    Kay, P.3    Campbell, S.4    McQuillan, A.5    Agnew, C.6
  • 10
    • 84878611766 scopus 로고    scopus 로고
    • The soluble form of the tumor suppressor Lrig1 potently inhibits in vivo glioma growth irrespective of EGF receptor status
    • M. Johansson, A. Oudin, K. Tiemann, A. Bernard, A. Golebiewska, and O. Keunen The soluble form of the tumor suppressor Lrig1 potently inhibits in vivo glioma growth irrespective of EGF receptor status Neuro Oncol 15 2013 1200 1211
    • (2013) Neuro Oncol , vol.15 , pp. 1200-1211
    • Johansson, M.1    Oudin, A.2    Tiemann, K.3    Bernard, A.4    Golebiewska, A.5    Keunen, O.6
  • 11
    • 38149041753 scopus 로고    scopus 로고
    • Lrig1 is an endogenous inhibitor of Ret receptor tyrosine kinase activation, downstream signaling, and biological responses to GDNF
    • F. Ledda, O. Bieraugel, S.S. Fard, M. Vilar, and G. Paratcha Lrig1 is an endogenous inhibitor of Ret receptor tyrosine kinase activation, downstream signaling, and biological responses to GDNF J Neurosci 28 2008 39 49
    • (2008) J Neurosci , vol.28 , pp. 39-49
    • Ledda, F.1    Bieraugel, O.2    Fard, S.S.3    Vilar, M.4    Paratcha, G.5
  • 12
    • 84874046969 scopus 로고    scopus 로고
    • LRIG1 regulates cadherin-dependent contact inhibition directing epithelial homeostasis and pre-invasive squamous cell carcinoma development
    • L. Lu, V.H. Teixeira, Z. Yuan, T.A. Graham, D. Endesfelder, and K. Kolluri LRIG1 regulates cadherin-dependent contact inhibition directing epithelial homeostasis and pre-invasive squamous cell carcinoma development J Pathol 229 2013 608 620
    • (2013) J Pathol , vol.229 , pp. 608-620
    • Lu, L.1    Teixeira, V.H.2    Yuan, Z.3    Graham, T.A.4    Endesfelder, D.5    Kolluri, K.6
  • 14
    • 84891742197 scopus 로고    scopus 로고
    • Cbl-independent degradation of Met: Ways to avoid agonism of bivalent Met-targeting antibody
    • J.M. Lee, B. Kim, S.B. Lee, Y. Jeong, Y.M. Oh, and Y.J. Song Cbl-independent degradation of Met: ways to avoid agonism of bivalent Met-targeting antibody Oncogene 33 2014 34 43
    • (2014) Oncogene , vol.33 , pp. 34-43
    • Lee, J.M.1    Kim, B.2    Lee, S.B.3    Jeong, Y.4    Oh, Y.M.5    Song, Y.J.6
  • 16
    • 84919639057 scopus 로고    scopus 로고
    • The LRIG family: Enigmatic regulators of growth factor receptor signaling
    • C. Simion, M.E. Cedano-Prieto, and C. Sweeney The LRIG family: enigmatic regulators of growth factor receptor signaling Endocr Relat Cancer 21 2014 R431 R443
    • (2014) Endocr Relat Cancer , vol.21 , pp. R431-R443
    • Simion, C.1    Cedano-Prieto, M.E.2    Sweeney, C.3
  • 19
    • 33846009479 scopus 로고    scopus 로고
    • The structure of the Lingo-1 ectodomain, a module implicated in central nervous system repair inhibition
    • L. Mosyak, A. Wood, B. Dwyer, M. Buddha, M. Johnson, and A. Aulabaugh The structure of the Lingo-1 ectodomain, a module implicated in central nervous system repair inhibition J Biol Chem 281 2006 36378 36390
    • (2006) J Biol Chem , vol.281 , pp. 36378-36390
    • Mosyak, L.1    Wood, A.2    Dwyer, B.3    Buddha, M.4    Johnson, M.5    Aulabaugh, A.6
  • 20
    • 0022550599 scopus 로고
    • Production of transforming growth factors by human colon cancer lines
    • R.J. Coffey, G.D. Shipley, and H.L. Moses Production of transforming growth factors by human colon cancer lines Cancer Res 46 1986 1164 1169
    • (1986) Cancer Res , vol.46 , pp. 1164-1169
    • Coffey, R.J.1    Shipley, G.D.2    Moses, H.L.3
  • 21
    • 65349166258 scopus 로고    scopus 로고
    • Lrig1 expression defines a distinct multipotent stem cell population in mammalian epidermis
    • K.B. Jensen, C.A. Collins, E. Nascimento, D.W. Tan, M. Frye, and S. Itami Lrig1 expression defines a distinct multipotent stem cell population in mammalian epidermis Cell Stem Cell 4 2009 427 439
    • (2009) Cell Stem Cell , vol.4 , pp. 427-439
    • Jensen, K.B.1    Collins, C.A.2    Nascimento, E.3    Tan, D.W.4    Frye, M.5    Itami, S.6
  • 22
    • 84878598705 scopus 로고    scopus 로고
    • LRIG1 is a triple threat: ERBB negative regulator, intestinal stem cell marker and tumour suppressor
    • Y. Wang, E.J. Poulin, and R.J. Coffey LRIG1 is a triple threat: ERBB negative regulator, intestinal stem cell marker and tumour suppressor Br J Cancer 108 2013 1765 1770
    • (2013) Br J Cancer , vol.108 , pp. 1765-1770
    • Wang, Y.1    Poulin, E.J.2    Coffey, R.J.3
  • 23
    • 0025946333 scopus 로고
    • Development of multipotential haemopoietic stem cells to neutrophils is associated with increased expression of receptors for granulocyte macrophage colony-stimulating factor: Altered biological responses to GM-CSF during development
    • C.M. Heyworth, J. Hampson, T.M. Dexter, F. Walker, A.W. Burgess, and O. Kan Development of multipotential haemopoietic stem cells to neutrophils is associated with increased expression of receptors for granulocyte macrophage colony-stimulating factor: altered biological responses to GM-CSF during development Growth Factors 5 1991 87 98
    • (1991) Growth Factors , vol.5 , pp. 87-98
    • Heyworth, C.M.1    Hampson, J.2    Dexter, T.M.3    Walker, F.4    Burgess, A.W.5    Kan, O.6
  • 24
    • 8144221077 scopus 로고    scopus 로고
    • Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan
    • P.G. Scott, P.A. McEwan, C.M. Dodd, E.M. Bergmann, P.N. Bishop, and J. Bella Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan Proc Natl Acad Sci U S A 101 2004 15633 15638
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 15633-15638
    • Scott, P.G.1    McEwan, P.A.2    Dodd, C.M.3    Bergmann, E.M.4    Bishop, P.N.5    Bella, J.6
  • 25
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • B. Kobe, and A.V. Kajava The leucine-rich repeat as a protein recognition motif Curr Opin Struct Biol 11 2001 725 732
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 26
    • 34249058902 scopus 로고    scopus 로고
    • Structural diversity of the hagfish variable lymphocyte receptors
    • H.M. Kim, S.C. Oh, K.J. Lim, J. Kasamatsu, J.Y. Heo, and B.S. Park Structural diversity of the hagfish variable lymphocyte receptors J Biol Chem 282 2007 6726 6732
    • (2007) J Biol Chem , vol.282 , pp. 6726-6732
    • Kim, H.M.1    Oh, S.C.2    Lim, K.J.3    Kasamatsu, J.4    Heo, J.Y.5    Park, B.S.6
  • 28
    • 0038325765 scopus 로고    scopus 로고
    • Structure of the Nogo receptor ectodomain: A recognition module implicated in myelin inhibition
    • X.L. He, J.F. Bazan, G. McDermott, J.B. Park, K. Wang, and M. Tessier-Lavigne Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition Neuron 38 2003 177 185
    • (2003) Neuron , vol.38 , pp. 177-185
    • He, X.L.1    Bazan, J.F.2    McDermott, G.3    Park, J.B.4    Wang, K.5    Tessier-Lavigne, M.6
  • 30
    • 0002738505 scopus 로고
    • A year in the life of the immunoglobulin superfamily
    • A.F. Williams A year in the life of the immunoglobulin superfamily Immunol Today 8 1987 298 303
    • (1987) Immunol Today , vol.8 , pp. 298-303
    • Williams, A.F.1
  • 31
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • M.C. Lawrence, and P.M. Colman Shape complementarity at protein/protein interfaces J Mol Biol 234 1993 946 950
    • (1993) J Mol Biol , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 33
    • 0025324872 scopus 로고
    • Nonradioactive ligand binding assay for epidermal growth factor receptor
    • I.C. King, and J.J. Catino Nonradioactive ligand binding assay for epidermal growth factor receptor Anal Biochem 188 1990 97 100
    • (1990) Anal Biochem , vol.188 , pp. 97-100
    • King, I.C.1    Catino, J.J.2
  • 34
    • 3142657314 scopus 로고    scopus 로고
    • Identification of the epitope for the epidermal growth factor receptor-specific monoclonal antibody 806 reveals that it preferentially recognizes an untethered form of the receptor
    • T.G. Johns, T.E. Adams, J.R. Cochran, N.E. Hall, P.A. Hoyne, and M.J. Olsen Identification of the epitope for the epidermal growth factor receptor-specific monoclonal antibody 806 reveals that it preferentially recognizes an untethered form of the receptor J Biol Chem 279 2004 30375 30384
    • (2004) J Biol Chem , vol.279 , pp. 30375-30384
    • Johns, T.G.1    Adams, T.E.2    Cochran, J.R.3    Hall, N.E.4    Hoyne, P.A.5    Olsen, M.J.6
  • 35
    • 75149133723 scopus 로고    scopus 로고
    • In vivo molecular imaging of colorectal cancer with confocal endomicroscopy by targeting epidermal growth factor receptor
    • M. Goetz, A. Ziebart, S. Foersch, M. Vieth, M.J. Waldner, and P. Delaney In vivo molecular imaging of colorectal cancer with confocal endomicroscopy by targeting epidermal growth factor receptor Gastroenterology 138 2010 435 446
    • (2010) Gastroenterology , vol.138 , pp. 435-446
    • Goetz, M.1    Ziebart, A.2    Foersch, S.3    Vieth, M.4    Waldner, M.J.5    Delaney, P.6
  • 36
    • 0035979381 scopus 로고    scopus 로고
    • Identification of a determinant of epidermal growth factor receptor ligand-binding specificity using a truncated, high-affinity form of the ectodomain
    • T.C. Elleman, T. Domagala, N.M. McKern, M. Nerrie, B. Lönnqvist, and T.E. Adams Identification of a determinant of epidermal growth factor receptor ligand-binding specificity using a truncated, high-affinity form of the ectodomain Biochemistry 40 2001 8930 8939
    • (2001) Biochemistry , vol.40 , pp. 8930-8939
    • Elleman, T.C.1    Domagala, T.2    McKern, N.M.3    Nerrie, M.4    Lönnqvist, B.5    Adams, T.E.6
  • 37
    • 84863248798 scopus 로고    scopus 로고
    • LRIG1 modulates cancer cell sensitivity to Smac mimetics by regulating TNFalpha expression and receptor tyrosine kinase signaling
    • L. Bai, D. McEachern, C.Y. Yang, J. Lu, H. Sun, and S. Wang LRIG1 modulates cancer cell sensitivity to Smac mimetics by regulating TNFalpha expression and receptor tyrosine kinase signaling Cancer Res 72 2012 1229 1238
    • (2012) Cancer Res , vol.72 , pp. 1229-1238
    • Bai, L.1    McEachern, D.2    Yang, C.Y.3    Lu, J.4    Sun, H.5    Wang, S.6
  • 38
    • 84889016843 scopus 로고    scopus 로고
    • Restoration of LRIG1 suppresses bladder cancer cell growth by directly targeting EGFR activity
    • L. Chang, R. Shi, T. Yang, F. Li, G. Li, and Y. Guo Restoration of LRIG1 suppresses bladder cancer cell growth by directly targeting EGFR activity J Exp Clin Cancer Res 32 2013 101
    • (2013) J Exp Clin Cancer Res , vol.32 , pp. 101
    • Chang, L.1    Shi, R.2    Yang, T.3    Li, F.4    Li, G.5    Guo, Y.6
  • 39
    • 44149128380 scopus 로고    scopus 로고
    • The role of ErbB3 and its binding partners in breast cancer progression and resistance to hormone and tyrosine kinase directed therapies
    • A.W. Hamburger The role of ErbB3 and its binding partners in breast cancer progression and resistance to hormone and tyrosine kinase directed therapies J Mammary Gland Biol Neoplasia 13 2008 225 233
    • (2008) J Mammary Gland Biol Neoplasia , vol.13 , pp. 225-233
    • Hamburger, A.W.1
  • 41
    • 18444370552 scopus 로고    scopus 로고
    • Targeted disruption of LIG-1 gene results in psoriasiform epidermal hyperplasia
    • Y. Suzuki, H. Miura, A. Tanemura, K. Kobayashi, G. Kondoh, and S. Sano Targeted disruption of LIG-1 gene results in psoriasiform epidermal hyperplasia FEBS Lett 521 2002 67 71
    • (2002) FEBS Lett , vol.521 , pp. 67-71
    • Suzuki, Y.1    Miura, H.2    Tanemura, A.3    Kobayashi, K.4    Kondoh, G.5    Sano, S.6
  • 42
    • 84879264708 scopus 로고    scopus 로고
    • ZFN, TALEN, and CRISPR/Cas-based methods for genome engineering
    • T. Gaj, C.A. Gersbach, and C.F. Barbas ZFN, TALEN, and CRISPR/Cas-based methods for genome engineering Trends Biotechnol 31 2013 397 405
    • (2013) Trends Biotechnol , vol.31 , pp. 397-405
    • Gaj, T.1    Gersbach, C.A.2    Barbas, C.F.3
  • 43
    • 77954368725 scopus 로고    scopus 로고
    • Crystal structure of the entire ectodomain of gp130: Insights into the molecular assembly of the tall cytokine receptor complexes
    • Y. Xu, N.J. Kershaw, C.S. Luo, P. Soo, M.J. Pocock, and P.E. Czabotar Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes J Biol Chem 285 2010 21214 21218
    • (2010) J Biol Chem , vol.285 , pp. 21214-21218
    • Xu, Y.1    Kershaw, N.J.2    Luo, C.S.3    Soo, P.4    Pocock, M.J.5    Czabotar, P.E.6
  • 44
    • 0000167256 scopus 로고
    • A viral cleavage site cassette: Identification of amino acid sequences required for tobacco etch virus polyprotein processing
    • J.C. Carrington, and W.G. Dougherty A viral cleavage site cassette: identification of amino acid sequences required for tobacco etch virus polyprotein processing Proc Natl Acad Sci 85 1988 3391 3395
    • (1988) Proc Natl Acad Sci , vol.85 , pp. 3391-3395
    • Carrington, J.C.1    Dougherty, W.G.2
  • 45
    • 0023714467 scopus 로고
    • A short polypeptide marker sequence useful for recombinant protein identification and purification
    • T.P. Hopp, K.S. Prickett, V.L. Price, R.T. Libby, C.J. March, and D.P. Cerretti A short polypeptide marker sequence useful for recombinant protein identification and purification Biotechnology 6 1988 1204 1210
    • (1988) Biotechnology , vol.6 , pp. 1204-1210
    • Hopp, T.P.1    Prickett, K.S.2    Price, V.L.3    Libby, R.T.4    March, C.J.5    Cerretti, D.P.6
  • 46
    • 0027337969 scopus 로고
    • Translocation of pp60c-src from the plasma membrane to the cytosol after stimulation by platelet-derived growth factor
    • F. Walker, J. deBlaquiere, and A.W. Burgess Translocation of pp60c-src from the plasma membrane to the cytosol after stimulation by platelet-derived growth factor J Biol Chem 268 1993 19552 19558
    • (1993) J Biol Chem , vol.268 , pp. 19552-19558
    • Walker, F.1    Deblaquiere, J.2    Burgess, A.W.3
  • 47
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and post-refinement
    • W. Kabsch Integration, scaling, space-group assignment and post-refinement Acta Crystallogr D Biol Crystallogr 66 2010 133 144
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 133-144
    • Kabsch, W.1
  • 48
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • P.A. Karplus, and K. Diederichs Linking crystallographic model and data quality Science 336 2012 1030 1033
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 52
    • 0034886351 scopus 로고    scopus 로고
    • Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin
    • O. Mayans, J. Wuerges, S. Canela, M. Gautel, and M. Wilmanns Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin Structure 9 2001 331 340
    • (2001) Structure , vol.9 , pp. 331-340
    • Mayans, O.1    Wuerges, J.2    Canela, S.3    Gautel, M.4    Wilmanns, M.5
  • 53
    • 0020933452 scopus 로고
    • Biological effects in vitro of monoclonal antibodies to human epidermal growth factor receptors
    • J. Sato, T. Kawamoto, A. Le, J. Mendelsohn, J. Polikoff, and G. Sato Biological effects in vitro of monoclonal antibodies to human epidermal growth factor receptors Mol Biol Med 1 1983 511 529
    • (1983) Mol Biol Med , vol.1 , pp. 511-529
    • Sato, J.1    Kawamoto, T.2    Le, A.3    Mendelsohn, J.4    Polikoff, J.5    Sato, G.6
  • 54
    • 67651227763 scopus 로고    scopus 로고
    • A truncated soluble epidermal growth factor receptor-Fc fusion ligand trap displays anti-tumour activity in vivo
    • T.E. Adams, E.J. Koziolek, P.H. Hoyne, J.D. Bentley, L. Lu, and G. Lovrecz A truncated soluble epidermal growth factor receptor-Fc fusion ligand trap displays anti-tumour activity in vivo Growth Factors 27 2009 141 154
    • (2009) Growth Factors , vol.27 , pp. 141-154
    • Adams, T.E.1    Koziolek, E.J.2    Hoyne, P.H.3    Bentley, J.D.4    Lu, L.5    Lovrecz, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.