메뉴 건너뛰기




Volumn 68, Issue 1, 2016, Pages 117-126

Cysteine-Mediated Redox Regulation of Cell Signaling in Chondrocytes Stimulated with Fibronectin Fragments

Author keywords

[No Author keywords available]

Indexed keywords

5,5 DIMETHYL 1,3 CYCLOHEXANEDIONE; COLLAGENASE 3; CYSTEINE; FIBRONECTIN; PROTEIN TYROSINE KINASE; SULFENIC ACID DERIVATIVE; CYCLOHEXANONE DERIVATIVE; MMP13 PROTEIN, HUMAN; PEPTIDE FRAGMENT;

EID: 84952024552     PISSN: 23265191     EISSN: 23265205     Source Type: Journal    
DOI: 10.1002/art.39326     Document Type: Article
Times cited : (36)

References (54)
  • 1
    • 38149052992 scopus 로고    scopus 로고
    • Estimates of the prevalence of arthritis and other rheumatic conditions in the United States: Part II
    • for the National Arthritis Data Workgroup
    • Lawrence RC, Felson DT, Helmick CG, Arnold LM, Choi H, Deyo RA, et al, for the National Arthritis Data Workgroup. Estimates of the prevalence of arthritis and other rheumatic conditions in the United States: part II. Arthritis Rheum 2008; 58: 26-35.
    • (2008) Arthritis Rheum , vol.58 , pp. 26-35
    • Lawrence, R.C.1    Felson, D.T.2    Helmick, C.G.3    Arnold, L.M.4    Choi, H.5    Deyo, R.A.6
  • 2
    • 77951430461 scopus 로고    scopus 로고
    • A claims-based view of health care charges and utilization for commercially insured patients with osteoarthritis
    • Dunn JD, Pill MW., A claims-based view of health care charges and utilization for commercially insured patients with osteoarthritis. Manag Care 2009; 18: 44-50.
    • (2009) Manag Care , vol.18 , pp. 44-50
    • Dunn, J.D.1    Pill, M.W.2
  • 4
    • 84861994775 scopus 로고    scopus 로고
    • Effects of aging on articular cartilage homeostasis
    • Lotz M, Loeser RF., Effects of aging on articular cartilage homeostasis. Bone 2012; 51: 241-8.
    • (2012) Bone , vol.51 , pp. 241-248
    • Lotz, M.1    Loeser, R.F.2
  • 5
    • 70349260481 scopus 로고    scopus 로고
    • Fibronectin fragments mediate matrix metalloproteinase upregulation and cartilage damage through proline rich tyrosine kinase 2, c-Src, NF-κB and protein kinase Cδ
    • Ding L, Guo D, Homandberg GA., Fibronectin fragments mediate matrix metalloproteinase upregulation and cartilage damage through proline rich tyrosine kinase 2, c-Src, NF-κB and protein kinase Cδ. Osteoarthritis Cartilage 2009; 17: 1385-92.
    • (2009) Osteoarthritis Cartilage , vol.17 , pp. 1385-1392
    • Ding, L.1    Guo, D.2    Homandberg, G.A.3
  • 6
    • 0027445393 scopus 로고
    • Intraarticular injection of fibronectin fragments causes severe depletion of cartilage proteoglycans in vivo
    • Homandberg GA, Meyers R, Williams JM., Intraarticular injection of fibronectin fragments causes severe depletion of cartilage proteoglycans in vivo. J Rheumatol 1993; 20: 1378-82.
    • (1993) J Rheumatol , vol.20 , pp. 1378-1382
    • Homandberg, G.A.1    Meyers, R.2    Williams, J.M.3
  • 7
    • 0026699536 scopus 로고
    • Fibronectin fragments in osteoarthritic synovial fluid
    • Xie DL, Meyers R, Homandberg GA., Fibronectin fragments in osteoarthritic synovial fluid. J Rheumatol 1992; 19: 1448-52.
    • (1992) J Rheumatol , vol.19 , pp. 1448-1452
    • Xie, D.L.1    Meyers, R.2    Homandberg, G.A.3
  • 8
    • 0026731793 scopus 로고
    • Fibronectin fragments cause chondrolysis of bovine articular cartilage slices in culture
    • Homandberg GA, Meyers R, Xie DL., Fibronectin fragments cause chondrolysis of bovine articular cartilage slices in culture. J Biol Chem 1992; 267: 3597-604.
    • (1992) J Biol Chem , vol.267 , pp. 3597-3604
    • Homandberg, G.A.1    Meyers, R.2    Xie, D.L.3
  • 9
    • 50949116784 scopus 로고    scopus 로고
    • The cartilage chondrolytic mechanism of fibronectin fragments involves MAP kinases: Comparison of three fragments and native fibronectin
    • Ding L, Guo D, Homandberg GA., The cartilage chondrolytic mechanism of fibronectin fragments involves MAP kinases: comparison of three fragments and native fibronectin. Osteoarthritis Cartilage 2008; 16: 1253-62.
    • (2008) Osteoarthritis Cartilage , vol.16 , pp. 1253-1262
    • Ding, L.1    Guo, D.2    Homandberg, G.A.3
  • 10
    • 0036900562 scopus 로고    scopus 로고
    • Fibronectin fragments active in chondrocytic chondrolysis can be chemically cross-linked to the α5 integrin receptor subunit
    • Homandberg GA, Costa V, Wen C., Fibronectin fragments active in chondrocytic chondrolysis can be chemically cross-linked to the α5 integrin receptor subunit. Osteoarthritis Cartilage 2002; 10: 938-49.
    • (2002) Osteoarthritis Cartilage , vol.10 , pp. 938-949
    • Homandberg, G.A.1    Costa, V.2    Wen, C.3
  • 11
    • 17844363020 scopus 로고    scopus 로고
    • NF-κB mediates the stimulation of cytokine and chemokine expression by human articular chondrocytes in response to fibronectin fragments
    • Pulai JI, Chen H, Im HJ, Kumar S, Hanning C, Hegde PS, et al., NF-κB mediates the stimulation of cytokine and chemokine expression by human articular chondrocytes in response to fibronectin fragments. J Immunol 2005; 174: 5781-8.
    • (2005) J Immunol , vol.174 , pp. 5781-5788
    • Pulai, J.I.1    Chen, H.2    Im, H.J.3    Kumar, S.4    Hanning, C.5    Hegde, P.S.6
  • 12
    • 0036746088 scopus 로고    scopus 로고
    • Fibronectin fragments and blocking antibodies to α2β1 and α5β1 integrins stimulate mitogen-activated protein kinase signaling and increase collagenase 3 (matrix metalloproteinase 13) production by human articular chondrocytes
    • Forsyth CB, Pulai J, Loeser RF., Fibronectin fragments and blocking antibodies to α2β1 and α5β1 integrins stimulate mitogen-activated protein kinase signaling and increase collagenase 3 (matrix metalloproteinase 13) production by human articular chondrocytes. Arthritis Rheum 2002; 46: 2368-76.
    • (2002) Arthritis Rheum , vol.46 , pp. 2368-2376
    • Forsyth, C.B.1    Pulai, J.2    Loeser, R.F.3
  • 13
    • 33947511182 scopus 로고    scopus 로고
    • Endogenous production of reactive oxygen species is required for stimulation of human articular chondrocyte matrix metalloproteinase production by fibronectin fragments
    • Del Carlo M, Schwartz D, Erickson EA, Loeser RF., Endogenous production of reactive oxygen species is required for stimulation of human articular chondrocyte matrix metalloproteinase production by fibronectin fragments. Free Radic Biol Med 2007; 42: 1350-8.
    • (2007) Free Radic Biol Med , vol.42 , pp. 1350-1358
    • Del Carlo, M.1    Schwartz, D.2    Erickson, E.A.3    Loeser, R.F.4
  • 14
    • 84898413435 scopus 로고    scopus 로고
    • NADPH oxidases in redox regulation of cell adhesion and migration
    • Schroder K., NADPH oxidases in redox regulation of cell adhesion and migration. Antioxid Redox Signal 2014; 20: 2043-58.
    • (2014) Antioxid Redox Signal , vol.20 , pp. 2043-2058
    • Schroder, K.1
  • 15
    • 84872831805 scopus 로고    scopus 로고
    • Cysteine oxidative posttranslational modifications: Emerging regulation in the cardiovascular system
    • Chung HS, Wang SB, Venkatraman V, Murray CI, van Eyk JE., Cysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system. Circ Res 2013; 112: 382-92.
    • (2013) Circ Res , vol.112 , pp. 382-392
    • Chung, H.S.1    Wang, S.B.2    Venkatraman, V.3    Murray, C.I.4    Van Eyk, J.E.5
  • 18
    • 78650078496 scopus 로고    scopus 로고
    • Quantitative reactivity profiling predicts functional cysteines in proteomes
    • Weerapana E, Wang C, Simon GM, Richter F, Khare S, Dillon MB, et al., Quantitative reactivity profiling predicts functional cysteines in proteomes. Nature 2010; 468: 790-5.
    • (2010) Nature , vol.468 , pp. 790-795
    • Weerapana, E.1    Wang, C.2    Simon, G.M.3    Richter, F.4    Khare, S.5    Dillon, M.B.6
  • 19
    • 79959340042 scopus 로고    scopus 로고
    • Protein sulfenic acid formation: From cellular damage to redox regulation
    • Roos G, Messens J., Protein sulfenic acid formation: from cellular damage to redox regulation. Free Radic Biol Med 2011; 51: 314-26.
    • (2011) Free Radic Biol Med , vol.51 , pp. 314-326
    • Roos, G.1    Messens, J.2
  • 20
    • 84898416421 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphatase oxidation in cell adhesion and migration
    • Frijhoff J, Dagnell M, Godfrey R, Ostman A., Regulation of protein tyrosine phosphatase oxidation in cell adhesion and migration. Antioxid Redox Signal 2014; 20: 1994-2010.
    • (2014) Antioxid Redox Signal , vol.20 , pp. 1994-2010
    • Frijhoff, J.1    Dagnell, M.2    Godfrey, R.3    Ostman, A.4
  • 21
    • 0037780966 scopus 로고    scopus 로고
    • Reactive oxygen species as essential mediators of cell adhesion: The oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion
    • Chiarugi P, Pani G, Giannoni E, Taddei L, Colavitti R, Raugei G, et al., Reactive oxygen species as essential mediators of cell adhesion: the oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion. J Cell Biol 2003; 161: 933-44.
    • (2003) J Cell Biol , vol.161 , pp. 933-944
    • Chiarugi, P.1    Pani, G.2    Giannoni, E.3    Taddei, L.4    Colavitti, R.5    Raugei, G.6
  • 22
    • 84898478868 scopus 로고    scopus 로고
    • Redox-relevant aspects of the extracellular matrix and its cellular contacts via integrins
    • Eble JA, de Rezende FF., Redox-relevant aspects of the extracellular matrix and its cellular contacts via integrins. Antioxid Redox Signal 2014; 20: 1977-93.
    • (2014) Antioxid Redox Signal , vol.20 , pp. 1977-1993
    • Eble, J.A.1    De Rezende, F.F.2
  • 23
    • 84898471569 scopus 로고    scopus 로고
    • Redox circuitries driving SRC regulation
    • Giannoni E, Chiarugi P., Redox circuitries driving SRC regulation. Antioxid Redox Signal 2014; 20: 2011-25.
    • (2014) Antioxid Redox Signal , vol.20 , pp. 2011-2025
    • Giannoni, E.1    Chiarugi, P.2
  • 24
    • 84880105471 scopus 로고    scopus 로고
    • Cysteine-mediated redox signaling: Chemistry, biology, and tools for discovery
    • Paulsen CE, Carroll KS., Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery. Chem Rev 2013; 113: 4633-79.
    • (2013) Chem Rev , vol.113 , pp. 4633-4679
    • Paulsen, C.E.1    Carroll, K.S.2
  • 25
    • 84893738731 scopus 로고    scopus 로고
    • Chemical approaches to detect and analyze protein sulfenic acids
    • Furdui CM., Poole LB., Chemical approaches to detect and analyze protein sulfenic acids. Mass Spectrom Rev 2014; 33: 126-46.
    • (2014) Mass Spectrom Rev , vol.33 , pp. 126-146
    • Furdui, C.M.1    Poole, L.B.2
  • 26
    • 70450274965 scopus 로고    scopus 로고
    • Oxidative stress inhibits insulin-like growth factor-I induction of chondrocyte proteoglycan synthesis through differential regulation of phosphatidylinositol 3-kinase-Akt and MEK-ERK MAPK signaling pathways
    • Yin W, Park JI, Loeser RF., Oxidative stress inhibits insulin-like growth factor-I induction of chondrocyte proteoglycan synthesis through differential regulation of phosphatidylinositol 3-kinase-Akt and MEK-ERK MAPK signaling pathways. J Biol Chem 2009; 284: 31972-81.
    • (2009) J Biol Chem , vol.284 , pp. 31972-31981
    • Yin, W.1    Park, J.I.2    Loeser, R.F.3
  • 27
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy DJ, Aukhil I, Erickson HP., 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 1996; 84: 155-64.
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 29
    • 84905985074 scopus 로고    scopus 로고
    • Epidermal growth factor stimulates nuclear factor-κB activation and heme oxygenase-1 expression via c-Src, NADPH oxidase, PI3K, and Akt in human colon cancer cells
    • Lien GS, Wu MS, Bien MY, Chen CH, Lin CH, Chen BC., Epidermal growth factor stimulates nuclear factor-κB activation and heme oxygenase-1 expression via c-Src, NADPH oxidase, PI3K, and Akt in human colon cancer cells. PLoS One 2014; 9: e104891.
    • (2014) PLoS One , vol.9 , pp. e104891
    • Lien, G.S.1    Wu, M.S.2    Bien, M.Y.3    Chen, C.H.4    Lin, C.H.5    Chen, B.C.6
  • 30
    • 84907339922 scopus 로고    scopus 로고
    • Site-specific mapping and quantification of protein S-sulphenylation in cells
    • Yang J, Gupta V, Carroll KS, Liebler DC., Site-specific mapping and quantification of protein S-sulphenylation in cells. Nat Commun 2014; 5: 4776.
    • (2014) Nat Commun , vol.5 , pp. 4776
    • Yang, J.1    Gupta, V.2    Carroll, K.S.3    Liebler, D.C.4
  • 32
    • 40949158747 scopus 로고    scopus 로고
    • Human articular chondrocytes produce IL-7 and respond to IL-7 with increased production of matrix metalloproteinase-13
    • Long D, Blake S, Song XY, Lark M, Loeser RF., Human articular chondrocytes produce IL-7 and respond to IL-7 with increased production of matrix metalloproteinase-13. Arthritis Res Ther 2008; 10: R23.
    • (2008) Arthritis Res Ther , vol.10 , pp. R23
    • Long, D.1    Blake, S.2    Song, X.Y.3    Lark, M.4    Loeser, R.F.5
  • 33
    • 0042090276 scopus 로고    scopus 로고
    • Fibronectin fragment activation of proline-rich tyrosine kinase PYK2 mediates integrin signals regulating collagenase-3 expression by human chondrocytes through a protein kinase C-dependent pathway
    • Loeser RF, Forsyth CB, Samarel AM, Im HJ., Fibronectin fragment activation of proline-rich tyrosine kinase PYK2 mediates integrin signals regulating collagenase-3 expression by human chondrocytes through a protein kinase C-dependent pathway. J Biol Chem 2003; 278: 24577-85.
    • (2003) J Biol Chem , vol.278 , pp. 24577-24585
    • Loeser, R.F.1    Forsyth, C.B.2    Samarel, A.M.3    Im, H.J.4
  • 34
    • 84888301385 scopus 로고    scopus 로고
    • Thiol-blocking electrophiles interfere with labeling and detection of protein sulfenic acids
    • Reisz JA, Bechtold E, King SB, Poole LB, Furdui CM., Thiol-blocking electrophiles interfere with labeling and detection of protein sulfenic acids. FEBS J 2013; 280: 6150-61.
    • (2013) FEBS J , vol.280 , pp. 6150-6161
    • Reisz, J.A.1    Bechtold, E.2    King, S.B.3    Poole, L.B.4    Furdui, C.M.5
  • 35
    • 77956198422 scopus 로고    scopus 로고
    • Use of dimedone-based chemical probes for sulfenic acid detection evaluation of conditions affecting probe incorporation into redox-sensitive proteins
    • Klomsiri C, Nelson KJ, Bechtold E, Soito L, Johnson LC, Lowther WT, et al., Use of dimedone-based chemical probes for sulfenic acid detection evaluation of conditions affecting probe incorporation into redox-sensitive proteins. Methods Enzymol 2010; 473: 77-94.
    • (2010) Methods Enzymol , vol.473 , pp. 77-94
    • Klomsiri, C.1    Nelson, K.J.2    Bechtold, E.3    Soito, L.4    Johnson, L.C.5    Lowther, W.T.6
  • 36
    • 77956210622 scopus 로고    scopus 로고
    • Use of dimedone-based chemical probes for sulfenic acid detection methods to visualize and identify labeled proteins
    • Nelson KJ, Klomsiri C, Codreanu SG, Soito L, Liebler DC, Rogers LC, et al., Use of dimedone-based chemical probes for sulfenic acid detection methods to visualize and identify labeled proteins. Methods Enzymol 2010; 473: 95-115.
    • (2010) Methods Enzymol , vol.473 , pp. 95-115
    • Nelson, K.J.1    Klomsiri, C.2    Codreanu, S.G.3    Soito, L.4    Liebler, D.C.5    Rogers, L.C.6
  • 37
    • 78649486199 scopus 로고    scopus 로고
    • Glyceraldehyde 3-phosphate dehydrogenase is unlikely to mediate hydrogen peroxide signaling: Studies with a novel anti-dimedone sulfenic acid antibody
    • Maller C, Schroder E, Eaton P., Glyceraldehyde 3-phosphate dehydrogenase is unlikely to mediate hydrogen peroxide signaling: studies with a novel anti-dimedone sulfenic acid antibody. Antioxid Redox Signal 2011; 14: 49-60.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 49-60
    • Maller, C.1    Schroder, E.2    Eaton, P.3
  • 39
    • 0028867982 scopus 로고
    • Image thresholding by minimizing the measures of fuzziness
    • Huang LK, Wang MJ., Image thresholding by minimizing the measures of fuzziness. Pattern Recognit 1995; 28: 41-51.
    • (1995) Pattern Recognit , vol.28 , pp. 41-51
    • Huang, L.K.1    Wang, M.J.2
  • 41
    • 84872041236 scopus 로고    scopus 로고
    • Fluctuation analysis of activity biosensor images for the study of information flow in signaling pathways
    • Tetin S.Y. editor. San Diego: Elsevier Academic Press
    • Vilela M, Halidi N, Besson S, Elliott H, Hahn K, Tytell J, et al., Fluctuation analysis of activity biosensor images for the study of information flow in signaling pathways. In:, Tetin SY, editor. Fluorescence fluctuation spectroscopy. San Diego: Elsevier Academic Press; 2013. p. 253-76.
    • (2013) Fluorescence Fluctuation Spectroscopy , pp. 253-276
    • Vilela, M.1    Halidi, N.2    Besson, S.3    Elliott, H.4    Hahn, K.5    Tytell, J.6
  • 42
    • 0032090603 scopus 로고    scopus 로고
    • An iterative algorithm for minimum cross entropy thresholding
    • Li CH, Tam PK., An iterative algorithm for minimum cross entropy thresholding. Pattern Recognit Lett 1998; 19: 771-6.
    • (1998) Pattern Recognit Lett , vol.19 , pp. 771-776
    • Li, C.H.1    Tam, P.K.2
  • 43
    • 58049201815 scopus 로고    scopus 로고
    • Src redox regulation: There is more than meets the eye
    • Chiarugi P., Src redox regulation: there is more than meets the eye. Mol Cells 2008; 26: 329-37.
    • (2008) Mol Cells , vol.26 , pp. 329-337
    • Chiarugi, P.1
  • 44
    • 0347481187 scopus 로고    scopus 로고
    • Increased oxidative stress with aging reduces chondrocyte survival: Correlation with intracellular glutathione levels
    • Del Carlo M Jr, Loeser RF., Increased oxidative stress with aging reduces chondrocyte survival: correlation with intracellular glutathione levels. Arthritis Rheum 2003; 48: 3419-30.
    • (2003) Arthritis Rheum , vol.48 , pp. 3419-3430
    • Del Carlo, M.1    Loeser, R.F.2
  • 45
    • 0032496326 scopus 로고    scopus 로고
    • Role of Rac1 and oxygen radicals in collagenase-1 expression induced by cell shape change
    • Kheradmand F, Werner E, Tremble P, Symons M, Werb Z., Role of Rac1 and oxygen radicals in collagenase-1 expression induced by cell shape change. Science 1998; 280: 898-902.
    • (1998) Science , vol.280 , pp. 898-902
    • Kheradmand, F.1    Werner, E.2    Tremble, P.3    Symons, M.4    Werb, Z.5
  • 46
    • 0030589104 scopus 로고    scopus 로고
    • Fibronectin fragment mediated cartilage chondrolysis. I. Suppression by anti-oxidants
    • Homandberg GA, Hui F, Wen C., Fibronectin fragment mediated cartilage chondrolysis. I. Suppression by anti-oxidants. Biochim Biophys Acta 1996; 1317: 134-42.
    • (1996) Biochim Biophys Acta , vol.1317 , pp. 134-142
    • Homandberg, G.A.1    Hui, F.2    Wen, C.3
  • 48
    • 0029020218 scopus 로고
    • Involvement of reactive oxygen species in cytokine and growth factor induction of c-fos expression in chondrocytes
    • Lo YY, Cruz TF., Involvement of reactive oxygen species in cytokine and growth factor induction of c-fos expression in chondrocytes. J Biol Chem 1995; 270: 11727-30.
    • (1995) J Biol Chem , vol.270 , pp. 11727-11730
    • Lo, Y.Y.1    Cruz, T.F.2
  • 49
    • 25644437811 scopus 로고    scopus 로고
    • Increased matrix metalloproteinase-13 production with aging by human articular chondrocytes in response to catabolic stimuli
    • Forsyth CB, Cole A, Murphy G, Bienias JL, Im HJ, Loeser RF Jr., Increased matrix metalloproteinase-13 production with aging by human articular chondrocytes in response to catabolic stimuli. J Gerontol A Biol Sci Med Sci 2005; 60: 1118-24.
    • (2005) J Gerontol A Biol Sci Med Sci , vol.60 , pp. 1118-1124
    • Forsyth, C.B.1    Cole, A.2    Murphy, G.3    Bienias, J.L.4    Im, H.J.5    Loeser, R.F.6
  • 50
    • 0032039959 scopus 로고    scopus 로고
    • Clinical applications of N-acetylcysteine
    • Kelly GS., Clinical applications of N-acetylcysteine. Altern Med Rev 1998; 3: 114-27.
    • (1998) Altern Med Rev , vol.3 , pp. 114-127
    • Kelly, G.S.1
  • 51
    • 0029034939 scopus 로고
    • C-Src enhances the spreading of src-/- fibroblasts on fibronectin by a kinase-independent mechanism
    • Kaplan KB, Swedlow JR, Morgan DO, Varmus HE., c-Src enhances the spreading of src-/- fibroblasts on fibronectin by a kinase-independent mechanism. Genes Dev 1995; 9: 1505-17.
    • (1995) Genes Dev , vol.9 , pp. 1505-1517
    • Kaplan, K.B.1    Swedlow, J.R.2    Morgan, D.O.3    Varmus, H.E.4
  • 54
    • 0028151515 scopus 로고
    • Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527
    • Kaplan KB, Bibbins KB, Swedlow JR, Arnaud M, Morgan DO, Varmus HE., Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527. EMBO J 1994; 13: 4745-56.
    • (1994) EMBO J , vol.13 , pp. 4745-4756
    • Kaplan, K.B.1    Bibbins, K.B.2    Swedlow, J.R.3    Arnaud, M.4    Morgan, D.O.5    Varmus, H.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.