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Volumn 9, Issue 7, 2014, Pages

Cleavage of histone 3 by cathepsin D in the involuting mammary gland

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN D; HISTONE H3; HISTONE;

EID: 84904700324     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0103230     Document Type: Article
Times cited : (27)

References (51)
  • 1
    • 0035863007 scopus 로고    scopus 로고
    • Postnatal mammary gland morphogenesis
    • Silberstein GB (2001) Postnatal mammary gland morphogenesis. Microsc Res Tech 52: 155-162.
    • (2001) Microsc Res Tech , vol.52 , pp. 155-162
    • Silberstein, G.B.1
  • 2
    • 69849084075 scopus 로고    scopus 로고
    • Key stages in mammary gland development: The cues that regulate ductal branching morphogenesis
    • Sternlicht MD (2005) Key stages in mammary gland development: The cues that regulate ductal branching morphogenesis. Breast Cancer Res 8: 201-211.
    • (2005) Breast Cancer Res , vol.8 , pp. 201-211
    • Sternlicht, M.D.1
  • 3
    • 34247551118 scopus 로고    scopus 로고
    • Key stages in mammary gland development - The alveolar switch: Coordinating the proliferative cues and cell fate decisions that drive the formation of lobuloalveoli from ductal epithelium
    • Oakes SR, Hilton HN, Ormandy CJ (2006) Key stages in mammary gland development - The alveolar switch: coordinating the proliferative cues and cell fate decisions that drive the formation of lobuloalveoli from ductal epithelium. Breast Cancer Res. 8: 207-.
    • (2006) Breast Cancer Res , vol.8 , pp. 207
    • Oakes, S.R.1    Hilton, H.N.2    Ormandy, C.J.3
  • 4
    • 34248226985 scopus 로고    scopus 로고
    • Key stages in mammary gland development. Secretory activation in the mammary gland: It's not just about milk protein synthesis
    • Anderson SM, Rudolph MC, McManaman JL, Neville MC (2007) Key stages in mammary gland development. Secretory activation in the mammary gland: it's not just about milk protein synthesis. Breast Cancer Res. 9: 204-218.
    • (2007) Breast Cancer Res , vol.9 , pp. 204-218
    • Anderson, S.M.1    Rudolph, M.C.2    McManaman, J.L.3    Neville, M.C.4
  • 6
    • 0030030021 scopus 로고    scopus 로고
    • Two distinct phases of apoptosis in mammary gland involution: Proteinase-independent and -dependent pathways
    • Lund LR, Romer J, Thomasset N, Solberg H, Pyke C, et al (1996) Two distinct phases of apoptosis in mammary gland involution: proteinase-independent and - dependent pathways. Development 122: 181-93. (Pubitemid 26038430)
    • (1996) Development , vol.122 , Issue.1 , pp. 181-193
    • Lund, L.R.1    Romer, J.2    Thomasset, N.3    Solberg, H.4    Pyke, C.5    Bissell, M.J.6    Dano, K.7    Werb, Z.8
  • 8
    • 4143098703 scopus 로고    scopus 로고
    • Functional development of the mammary gland: Use of expression rofiling and trajectory clustering to reveal changes in gene expression during pregnancy, lactation, and involution
    • DOI 10.1023/B:JOMG.0000010030.73983.57, Microarrays
    • Rudolph MC, Mc Manaman JL, Hunter L, Phang T, Neville MC (2003) Functional development of the mammary gland: use of expression profiling and trajectory clustering to reveal changes in gene expression during pregnancy, lactation, and involution. J. Mammary Gland Biol Neoplasia 8: 287-307. (Pubitemid 39137512)
    • (2003) Journal of Mammary Gland Biology and Neoplasia , vol.8 , Issue.3 , pp. 287-307
    • Rudolph, M.C.1    McManaman, J.L.2    Hunter, L.3    Phang, T.4    Neville, M.C.5
  • 9
    • 0033111847 scopus 로고    scopus 로고
    • Transcription factor activities and gene expression during mouse mammary gland involution
    • Marti A, Lazar H, Ritter P, Jaggi R (1999) Transcription factor activities and gene expression during mouse mammary gland involution. J Mammary Gland Biol Neoplasia 4: 145-152.
    • (1999) J Mammary Gland Biol Neoplasia , vol.4 , pp. 145-152
    • Marti, A.1    Lazar, H.2    Ritter, P.3    Jaggi, R.4
  • 10
    • 0033858512 scopus 로고    scopus 로고
    • Transforming growth factor b3 induces cell death during the first stage of mammary gland involution
    • Nguyen AV, Pollard JW (2000) TGF-b3 induces cell death during the first stage of mammary gland involution. Development 127: 3107-3118. (Pubitemid 30611903)
    • (2000) Development , vol.127 , Issue.14 , pp. 3107-3118
    • Nguyen, A.V.1    Pollard, J.W.2
  • 11
    • 0036720557 scopus 로고    scopus 로고
    • Deletion of Stat3 blocks mammary gland involution and extends functional competence of the secretory epithelium in the absence of lactogenic stimuli
    • DOI 10.1210/en.2002-220224
    • Humphreys RC, Bierie B, Zhao L, Raz R, Levy D, et al (2002) Deletion of Stat3 blocks mammary gland involution and extends functional competence of the secretory epithelium in the absence of lactogenic stimuli. Endocrinology 143: 3641-3650. (Pubitemid 34925741)
    • (2002) Endocrinology , vol.143 , Issue.9 , pp. 3641-3650
    • Humphreys, R.C.1    Bierie, B.2    Zhao, L.3    Regina, R.4    Levy, D.5    Hennighausen, L.6
  • 12
    • 1542354246 scopus 로고    scopus 로고
    • Involution of the mouse mammary gland is associated with an immune cascade and an acute-phase response, involving LBP, CD14 and STAT3
    • Stein T, Morris JS, Davies CR, Weber-Hall SJ, Duffy M-A, et al (2004) Involution of the mouse mammary gland is associated with an immune cascade and an acute-phase response, involving LBP, CD14 and STAT3. Breast Cancer Res. 6: R75-R91.
    • (2004) Breast Cancer Res , vol.6
    • Stein, T.1    Morris, J.S.2    Davies, C.R.3    Weber-Hall, S.J.4    Duffy, M.-A.5
  • 13
    • 67349124434 scopus 로고    scopus 로고
    • Elf5 conditional knockout mice reveal its role as a master regulator in mammary alveolar development: Failure of Stat5 activation and functional differentiation in the absence of Elf5
    • Choi YS, Chakrabarti R, Escamilla-Hernandez R, Sinha S (2009) Elf5 conditional knockout mice reveal its role as a master regulator in mammary alveolar development: failure of Stat5 activation and functional differentiation in the absence of Elf5. Dev Biol. 329: 227-41.
    • (2009) Dev Biol , vol.329 , pp. 227-241
    • Choi, Y.S.1    Chakrabarti, R.2    Escamilla-Hernandez, R.3    Sinha, S.4
  • 15
    • 18844376887 scopus 로고    scopus 로고
    • P53 mediates a default program of mammary gland involution in the absence of Stat3
    • Mathews JR, Clark AR (2005) P53 mediates a default program of mammary gland involution in the absence of Stat3. Oncogene 24: 3083-3090.
    • (2005) Oncogene , vol.24 , pp. 3083-3090
    • Mathews, J.R.1    Clark, A.R.2
  • 17
    • 0014351020 scopus 로고
    • Studies on mammary gland involution. II. Ultrastructural evidence for auto-and hetero-phagocytosis
    • Helminen HJ, Ericsson JLE (1968) Studies on mammary gland involution. II. Ultrastructural evidence for auto-and hetero-phagocytosis. Ultrastructure Res 25: 214-227.
    • (1968) Ultrastructure Res , vol.25 , pp. 214-227
    • Helminen, H.J.1    Ericsson, J.L.E.2
  • 18
    • 0027946430 scopus 로고
    • Cathepsin B, a cysteine protease implicated in metastatic progression, is also expressed during regression of the rat prostate and mammary glands
    • DOI 10.1111/j.1432-1033.1994.tb20055.x
    • Guenette RS, Mooibroek M, Wong K, Wong P, Tenniswood M (1994) Cathepsin B, a cysteine protease implicated in metastatic progression, is also expressed during regression of the rat prostate and mammary glands. Eur J. Biochem 226: 311-321. (Pubitemid 24379049)
    • (1994) European Journal of Biochemistry , vol.226 , Issue.2 , pp. 311-321
    • Guenette, R.S.1    Mooibroek, M.2    Wong, K.3    Wong, P.4    Tenniswood, M.5
  • 19
    • 0038002071 scopus 로고    scopus 로고
    • Cathepsin L plays an active role in involution of the mouse mammary gland
    • DOI 10.1002/dvdy.10313
    • Burke MA, Hutter D, Reshamwala RP, Knepper JE (2003) Cathepsin L plays an active role in involution of the mouse mammary gland. Developmental Dynamics 227: 315-322. (Pubitemid 36828752)
    • (2003) Developmental Dynamics , vol.227 , Issue.3 , pp. 315-322
    • Burke, M.A.1    Hutter, D.2    Reshamwala, R.P.3    Knepper, J.E.4
  • 21
    • 77149164774 scopus 로고    scopus 로고
    • Matrix metalloproteinases: What do they not do? New substrates and biological roles identified by murine models and proteomics
    • Rodríguez D, Morrisona CJ, Overalla CM (2010) Matrix metalloproteinases: What do they not do? New substrates and biological roles identified by murine models and proteomics. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1803: 39-54.
    • (2010) Biochimica et Biophysica Acta (BBA) - Molecular Cell Research , vol.1803 , pp. 39-54
    • Rodríguez, D.1    Morrisona, C.J.2    Overalla, C.M.3
  • 23
    • 0035911148 scopus 로고    scopus 로고
    • Stromelysin-1 regulates adipogenesis during mammary gland involution
    • DOI 10.1083/jcb.152.4.693
    • Alexander CM, Selvarajan S, Mudgett J, Werb Z (2001) Stromelysin-1 regulates adipogenesis during mammary gland involution. J. Cell Biol. 152: 693-703. (Pubitemid 34280155)
    • (2001) Journal of Cell Biology , vol.152 , Issue.4 , pp. 693-703
    • Alexander, C.M.1    Selvarajan, S.2    Mudgett, J.3    Werbc, Z.4
  • 24
    • 79551618369 scopus 로고    scopus 로고
    • Cathepsin-D, a key protease in breast cancer, is up-regulated in obese mouse and human adipose tissue, and controls adipogenesis
    • Masson O, Prébois C, Derocq D, Meulle A, Dray C (2011) Cathepsin-D, a key protease in breast cancer, is up-regulated in obese mouse and human adipose tissue, and controls adipogenesis. PLoS One 6: e16452.
    • (2011) PLoS One , vol.6
    • Masson, O.1    Prébois, C.2    Derocq, D.3    Meulle, A.4    Dray, C.5
  • 25
    • 79955758601 scopus 로고    scopus 로고
    • Adipogenic Histone mark regulation by MMP-14 in collagen-rich environments
    • Sato-Kusubata K, Jiang Y, Ueno Y, Chun T-H (2011) Adipogenic Histone mark regulation by MMP-14 in collagen-rich environments. Mol. Endocrinol. 25: 745-753.
    • (2011) Mol. Endocrinol. , vol.25 , pp. 745-753
    • Sato-Kusubata, K.1    Jiang, Y.2    Ueno, Y.3    Chun, T.-H.4
  • 27
    • 64249088369 scopus 로고    scopus 로고
    • Nitration of cathepsin D enhances its proteolytic activity during mammary gland remodeling after lactation
    • Zaragoza R, Torres L, Garcia C, Eroles P, Corrales F, et al (2009) Nitration of cathepsin D enhances its proteolytic activity during mammary gland remodeling after lactation. Biochem J 419: 279-288.
    • (2009) Biochem J , vol.419 , pp. 279-288
    • Zaragoza, R.1    Torres, L.2    Garcia, C.3    Eroles, P.4    Corrales, F.5
  • 28
    • 0031709904 scopus 로고    scopus 로고
    • Endocytosis of pro-cathepsin D into breast cancer cells is mostly independent of mannose-6-phosphate receptors
    • Laurent-Matha V, Farnoud MR, Lucas C, Garcia M, Rochefort H (1998) Endocytosis of pro-cathepsin D into breast cancer cells is mostly independent of mannose-6-phosphate receptors. J. Cell Sci. 111: 2539-49. (Pubitemid 28474957)
    • (1998) Journal of Cell Science , vol.111 , Issue.17 , pp. 2539-2549
    • Laurent-Matha, V.1    Farnoud, M.R.2    Lucas, A.3    Rougeot, C.4    Garcia, M.5    Rochefort, H.6
  • 29
    • 53249132917 scopus 로고    scopus 로고
    • Purification and characterization of cathepsin D from normal human breast tissue
    • DOI 10.1023/A:1026322707644
    • Wright LM, Levy ES, Patel NP, Alhadeff LJ (1997) Purification and characterization of Cathepsin D from normal human breast tissue. Protein Biochem 16: 171-181. (Pubitemid 27209020)
    • (1997) Journal of Protein Chemistry , vol.16 , Issue.3 , pp. 171-181
    • Wright, L.M.1    Levy, E.S.2    Patel, N.P.3    Alhadeff, J.A.4
  • 30
    • 0036532026 scopus 로고    scopus 로고
    • Histone modifications in transcriptional regulation
    • Berger SL (2002) Histone modifications in transcriptional regulation. Curr. Opin. Genet. Dev. 12: 142-148.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 142-148
    • Berger, S.L.1
  • 31
    • 5444263735 scopus 로고    scopus 로고
    • Epigenetic aspects of differentiation
    • DOI 10.1242/jcs.01390
    • Arney KL, Fisher AG (2004) Epigenetic aspects of differentiation. J. Cell Science 117: 4355-4363. (Pubitemid 39360063)
    • (2004) Journal of Cell Science , vol.117 , Issue.19 , pp. 4355-4363
    • Arney, K.L.1    Fisher, A.G.2
  • 32
    • 55449096356 scopus 로고    scopus 로고
    • Crosstalk among histone modifications
    • Suganuma T, Workman JL (2008) Crosstalk among histone modifications. Cell 135: 604-605.
    • (2008) Cell , vol.135 , pp. 604-605
    • Suganuma, T.1    Workman, J.L.2
  • 33
    • 53549094681 scopus 로고    scopus 로고
    • Cathepsin L proteolytically processes Histone H3 during mouse embryonic stem cell differentiation
    • Duncan EM, Muratore-Schroeder TL, Cook RG, Garcia BA, Shabanowitz J, et al (2008) Cathepsin L proteolytically processes Histone H3 during mouse embryonic stem cell differentiation. Cell 135: 284-294.
    • (2008) Cell , vol.135 , pp. 284-294
    • Duncan, E.M.1    Muratore-Schroeder, T.L.2    Cook, R.G.3    Garcia, B.A.4    Shabanowitz, J.5
  • 34
    • 0023655142 scopus 로고
    • Identification and isolation of soluble histones from bovine milk
    • Waga S, Tan EM, Rubin RL (1987) Identification and isolation of soluble histones from bovine milk. Biochem. J. 244: 675-682.
    • (1987) Biochem. J. , vol.244 , pp. 675-682
    • Waga, S.1    Tan, E.M.2    Rubin, R.L.3
  • 35
    • 0037177860 scopus 로고    scopus 로고
    • Nitric oxide (NO) induces nitration of protein kinase Cε (PKCε), facilitating PKCε translocation via enhanced PKCε-RACK2 interactions. A novel mechanism of no-triggered activation of PKCε
    • DOI 10.1074/jbc.M112451200
    • Balafanova Z, Bolli R, Zhang J, Zheng Y, Pass JM, et al (2002) Nitric oxide (NO) induces nitration of protein kinaseCε (PKCε), facilitating PKCε translocation via enhanced PKCε-RACK2 interactions: A novel mechanism of NO-triggered activation of PKCε.J. Biol. Chem. 277: 15021-15027. (Pubitemid 34952578)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.17 , pp. 15021-15027
    • Balafanova, Z.1    Bolli, R.2    Zhang, J.3    Zheng, Y.4    Pass, J.M.5    Bhatnagar, A.6    Tang, X.-L.7    Wang, O.8    Cardwell, E.9    Ping, P.10
  • 36
    • 1642570319 scopus 로고    scopus 로고
    • Nitric oxide, oxidants, and protein tyrosine nitration
    • Radi R (2004) Nitric oxide, oxidants, and protein tyrosine nitration. Proc. Nat. Acad. Sci. USA 101: 4003-4008.
    • (2004) Proc. Nat. Acad. Sci. USA , vol.101 , pp. 4003-4008
    • Radi, R.1
  • 37
    • 15944409156 scopus 로고    scopus 로고
    • Tyrosine nitration on p65: A novel mechanism to rapidly inactive nuclear factor-kappaB
    • DOI 10.1074/mcp.M400195-MCP200
    • Park SW, Huq MDM, Hu X, Wei L-N (2005) Tyrosine nitration on p65: A novel mechanism to rapidly inactivate nuclear factor-kappa B. Molecular & Cellular Proteomics 4: 300-309. (Pubitemid 40439773)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.3 , pp. 300-309
    • Park, S.W.1    Huq, M.D.M.2    Hu, X.3    Wei, L.-N.4
  • 38
    • 67650354415 scopus 로고    scopus 로고
    • Protein tyrosine nitration: Selectivity, physicochemical and biological consequences, denitration, and proteomics methods for the identification of tyrosine-nitrated proteins
    • Abello N, Kerstjens HAM, Postma DS, Bischoff R (2009) Protein tyrosine nitration: Selectivity, physicochemical and biological consequences, denitration, and proteomics methods for the identification of tyrosine-nitrated proteins. J. Proteome Res. 8: 3222-3238.
    • (2009) J. Proteome Res. , vol.8 , pp. 3222-3238
    • Abello, N.1    Kerstjens, H.A.M.2    Postma, D.S.3    Bischoff, R.4
  • 39
    • 77953811292 scopus 로고    scopus 로고
    • Nitration of tyrosine 74 prevents human cytochrome C to play a key role in apoptosis signaling by blocking caspase-9 activation
    • García-Heredia JM, Díaz-Moreno I, Nieto PM, Orzáez M, Kocanis S, et al (2010) Nitration of tyrosine 74 prevents human cytochrome C to play a key role in apoptosis signaling by blocking caspase-9 activation. Biochim Biophys Acta - Bioenergetics 1797: 981-993.
    • (2010) Biochim Biophys Acta - Bioenergetics , vol.1797 , pp. 981-993
    • García-Heredia, J.M.1    Díaz-Moreno, I.2    Nieto, P.M.3    Orzáez, M.4    Kocanis, S.5
  • 40
    • 0025190848 scopus 로고
    • Foot-and-mouth disease virus protease 3C induces specific proteolytic cleavage of host cell histone H3
    • Falk MM, Grigera PR, Bergmann IE, Zibert A, Multhaup G, et al (1990) Foot-and-Mouth disease virus protease 3C induces specific proteolytic cleavage of host cell Histone H3. J. Virology 64: 748-756. (Pubitemid 20032691)
    • (1990) Journal of Virology , vol.64 , Issue.2 , pp. 748-756
    • Falk, M.M.1    Grigera, P.R.2    Bergmann, I.E.3    Zibert, A.4    Multhaup, G.5    Beck, E.6
  • 42
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey VG, Faulkner R, Mirsky AE (1964) Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Nat. Acad. Sci. USA 51: 786-794.
    • (1964) Proc. Nat. Acad. Sci. USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 43
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • DOI 10.1038/47412
    • Strahl BD, Allis CD (2000)The language of covalent histone modifications. Nature 403: 41-45. (Pubitemid 30038513)
    • (2000) Nature , vol.403 , Issue.6765 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 44
    • 34547890019 scopus 로고    scopus 로고
    • Function of site-specific histone acetylation
    • Shahbazian MD, Grunstein M (2007) Function of site-specific histone acetylation. Annu. Rev. Biochem. 76: 75-100.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 75-100
    • Shahbazian, M.D.1    Grunstein, M.2
  • 45
    • 13544252784 scopus 로고    scopus 로고
    • Epithelial cells as phagocytes: Apoptotic epithelial cells are engulfed by mammary alveolar epithelial cells and repress inflammatory mediator release
    • DOI 10.1038/sj.cdd.4401517
    • Monks J, Rosner D, Jon Geske F, Lehman L, Hanson L, et al (2005) Epithelial cells as phagocytes: apoptotic epithelial cells are engulfed by mammary alveolar epithelial cells and repress inflammatory mediator release. Cell Death and Differentiation 12: 107-114. (Pubitemid 40220641)
    • (2005) Cell Death and Differentiation , vol.12 , Issue.2 , pp. 107-114
    • Monks, J.1    Rosner, D.2    Geske, F.J.3    Lehman, L.4    Hanson, L.5    Neville, M.C.6    Fadok, V.A.7
  • 46
    • 78650602365 scopus 로고    scopus 로고
    • Epithelial cell-directed efferocytosis in the post-partum mammary gland is necessary for tissue homeostasis and future lactation
    • Sandahl M, Hunter DM, Strunk KE, Earp HS, Cook RS (2010) Epithelial cell-directed efferocytosis in the post-partum mammary gland is necessary for tissue homeostasis and future lactation. BMC Developmental Biology 10: 122-128.
    • (2010) BMC Developmental Biology , vol.10 , pp. 122-128
    • Sandahl, M.1    Hunter, D.M.2    Strunk, K.E.3    Earp, H.S.4    Cook, R.S.5
  • 48
    • 0015135055 scopus 로고
    • Effects of enforced milk stasis on mammary gland epithelium, with special reference to changes in lysosomal enzymes
    • Helminen HJ, Ericsson JLE (1971) Effects of enforced milk stasis on mammary gland epithelium, with special reference to changes in lysosomal enzymes. Exp. Cell Res. 68: 411-427.
    • (1971) Exp. Cell Res. , vol.68 , pp. 411-427
    • Helminen, H.J.1    Ericsson, J.L.E.2
  • 49
    • 0036676298 scopus 로고    scopus 로고
    • Down-regulation of cathepsin-D expression by antisense gene transfer inhibits tumor growth and experimental lung metastasis of human breast cancer cells
    • Glondu M, Liaudet-Coopman E, Derocq D, Platet N, Rochefort H, et al (2002) Down-regulation of cathepsin-D expression by antisense gene transfer inhibits tumor growth and experimental lung metastasis of human breast cancer cells. Oncogene 21: 5127-5134.
    • (2002) Oncogene , vol.21 , pp. 5127-5134
    • Glondu, M.1    Liaudet-Coopman, E.2    Derocq, D.3    Platet, N.4    Rochefort, H.5
  • 50
    • 84870332620 scopus 로고    scopus 로고
    • Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment
    • Laurent-Matha V, Huesgen PF, Masson O, Derocq D, Prébois C, et al (2012) Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment. FASEB J. 26, 1-10.
    • (2012) FASEB J. , vol.26 , pp. 1-10
    • Laurent-Matha, V.1    Huesgen, P.F.2    Masson, O.3    Derocq, D.4    Prébois, C.5
  • 51
    • 77956892285 scopus 로고    scopus 로고
    • Pro-cathepsin D interacts with the extracellular domain of the chain of LRP1 and promotes LRP1-dependent fibroblast outgrowth
    • Beaujouin M, Prébois C, Derocq D, Laurent-Matha V, Masson O, et al (2010) Pro-cathepsin D interacts with the extracellular domain of the chain of LRP1 and promotes LRP1-dependent fibroblast outgrowth. J. Cell Science 123, 3336-3346.
    • (2010) J. Cell Science , vol.123 , pp. 3336-3346
    • Beaujouin, M.1    Prébois, C.2    Derocq, D.3    Laurent-Matha, V.4    Masson, O.5


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