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Volumn 5, Issue 246, 2012, Pages

Physiology: TWEAK and cIAP1 regulate myoblast fusion through the noncanonical NF-κB signaling pathway

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR INHIBITOR OF APOPTOSIS 1 PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROTEIN; PROTEIN P100; PROTEIN P52; TNF LIKE WEAK INDUCER OF APOPTOSIS PROTEIN; TRANSCRIPTION FACTOR RELB; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 3; UNCLASSIFIED DRUG; BROXURIDINE; INHIBITOR OF APOPTOSIS PROTEIN; SMALL INTERFERING RNA; TNFSF12 PROTEIN, MOUSE; TUMOR NECROSIS FACTOR;

EID: 84867805394     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2003086     Document Type: Article
Times cited : (67)

References (73)
  • 1
    • 84856141914 scopus 로고    scopus 로고
    • Myoblast fusion: Lessons from flies and mice
    • S. M. Abmayr, G. K. Pavlath, Myoblast fusion: Lessons from flies and mice. Development 139, 641-656 (2012).
    • (2012) Development , vol.139 , pp. 641-656
    • Abmayr, S.M.1    Pavlath, G.K.2
  • 3
    • 33644853217 scopus 로고    scopus 로고
    • Distinct BIR domains of cIAP1 mediate binding to and ubiquitination of tumor necrosis factor receptor-associated factor 2 and second mitochondrial activator of caspases
    • T. Samuel, K. Welsh, T. Lober, S. H. Togo, J. M. Zapata, J. C. Reed, Distinct BIR domains of cIAP1 mediate binding to and ubiquitination of tumor necrosis factor receptor-associated factor 2 and second mitochondrial activator of caspases. J. Biol. Chem. 281, 1080-1090 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 1080-1090
    • Samuel, T.1    Welsh, K.2    Lober, T.3    Togo, S.H.4    Zapata, J.M.5    Reed, J.C.6
  • 5
    • 0034607655 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli
    • Y. Yang, S. Fang, J. P. Jensen, A. M. Weissman, J. D. Ashwell, Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science 288, 874-877 (2000).
    • (2000) Science , vol.288 , pp. 874-877
    • Yang, Y.1    Fang, S.2    Jensen, J.P.3    Weissman, A.M.4    Ashwell, J.D.5
  • 6
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • C. Du, M. Fang, Y. Li, L. Li, X. Wang, Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102, 33-42 (2000).
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 16
    • 84858627919 scopus 로고    scopus 로고
    • Cellular inhibitors of apoptosis are global regulators of NF-κB and MAPK activation by members of the TNF family of receptors
    • E. Varfolomeev, T. Goncharov, H. Maecker, K. Zobel, L. G. Kömüves, K. Deshayes, D. Vucic, Cellular inhibitors of apoptosis are global regulators of NF-κB and MAPK activation by members of the TNF family of receptors. Sci. Signal. 5, ra22 (2012).
    • (2012) Sci. Signal. , vol.5
    • Varfolomeev, E.1    Goncharov, T.2    Maecker, H.3    Zobel, K.4    Kömüves, L.G.5    Deshayes, K.6    Vucic, D.7
  • 18
    • 0037059745 scopus 로고    scopus 로고
    • RelB cellular regulation and transcriptional activity are regulated by p100
    • N. J. Solan, H. Miyoshi, E. M. Carmona, G. D. Bren, C. V. Paya, RelB cellular regulation and transcriptional activity are regulated by p100. J. Biol. Chem. 277, 1405-1418 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 1405-1418
    • Solan, N.J.1    Miyoshi, H.2    Carmona, E.M.3    Bren, G.D.4    Paya, C.V.5
  • 20
    • 0032588186 scopus 로고    scopus 로고
    • NF-κB controls cell growth and differentiation through transcriptional regulation of cyclin D1
    • D. C. Guttridge, C. Albanese, J. Y. Reuther, R. G. Pestell, A. S. Baldwin Jr., NF-κB controls cell growth and differentiation through transcriptional regulation of cyclin D1. Mol. Cell. Biol. 19, 5785-5799 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5785-5799
    • Guttridge, D.C.1    Albanese, C.2    Reuther, J.Y.3    Pestell, R.G.4    Baldwin Jr., A.S.5
  • 21
    • 0037083867 scopus 로고    scopus 로고
    • TNFα inhibits skeletal myogenesis through a PW1-dependent pathway by recruitment of caspase pathways
    • D. Coletti, E. Yang, G. Marazzi, D. Sassoon, TNFα inhibits skeletal myogenesis through a PW1-dependent pathway by recruitment of caspase pathways. EMBO J. 21, 631-642 (2002).
    • (2002) EMBO J. , vol.21 , pp. 631-642
    • Coletti, D.1    Yang, E.2    Marazzi, G.3    Sassoon, D.4
  • 22
    • 2942555110 scopus 로고    scopus 로고
    • IL-1β impairs insulin-like growth factor i-induced differentiation and downstream activation signals of the insulin-like growth factor i receptor in myoblasts
    • S. R. Broussard, R. H. McCusker, J. E. Novakofski, K. Strle, W. H. Shen, R. W. Johnson, R. Dantzer, K. W. Kelley, IL-1β impairs insulin-like growth factor I-induced differentiation and downstream activation signals of the insulin-like growth factor I receptor in myoblasts. J. Immunol. 172, 7713-7720 (2004).
    • (2004) J. Immunol. , vol.172 , pp. 7713-7720
    • Broussard, S.R.1    McCusker, R.H.2    Novakofski, J.E.3    Strle, K.4    Shen, W.H.5    Johnson, R.W.6    Dantzer, R.7    Kelley, K.W.8
  • 23
    • 0035868407 scopus 로고    scopus 로고
    • Differential effects of Ras signaling through NFκB on skeletal myogenesis
    • N. Mitin, A. J. Kudla, S. F. Konieczny, E. J. Taparowsky, Differential effects of Ras signaling through NFκB on skeletal myogenesis. Oncogene 20, 1276-1286 (2001).
    • (2001) Oncogene , vol.20 , pp. 1276-1286
    • Mitin, N.1    Kudla, A.J.2    Konieczny, S.F.3    Taparowsky, E.J.4
  • 24
    • 63249086636 scopus 로고    scopus 로고
    • Tumor necrosis factor-related weak inducer of apoptosis augments matrix metalloproteinase 9 (MMP-9) production in skeletal muscle through the activation of nuclear factor-κB-inducing kinase and p38 mitogen-activated protein kinase: A potential role of MMP-9 in myopathy
    • H. Li, A. Mittal, P. K. Paul, M. Kumar, D. S. Srivastava, S. C. Tyagi, A. Kumar, Tumor necrosis factor-related weak inducer of apoptosis augments matrix metalloproteinase 9 (MMP-9) production in skeletal muscle through the activation of nuclear factor-κB-inducing kinase and p38 mitogen-activated protein kinase: A potential role of MMP-9 in myopathy. J. Biol. Chem. 284, 4439-4450 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 4439-4450
    • Li, H.1    Mittal, A.2    Paul, P.K.3    Kumar, M.4    Srivastava, D.S.5    Tyagi, S.C.6    Kumar, A.7
  • 25
    • 33744542153 scopus 로고    scopus 로고
    • Tumor necrosis factor-like weak inducer of apoptosis inhibits skeletal myogenesis through sustained activation of nuclear factor-κB and degradation of MyoD protein
    • C. Dogra, H. Changotra, S. Mohan, A. Kumar, Tumor necrosis factor-like weak inducer of apoptosis inhibits skeletal myogenesis through sustained activation of nuclear factor-κB and degradation of MyoD protein. J. Biol. Chem. 281, 10327-10336 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 10327-10336
    • Dogra, C.1    Changotra, H.2    Mohan, S.3    Kumar, A.4
  • 27
    • 2342640319 scopus 로고    scopus 로고
    • Cell fusion in skeletal muscle - Central role of NFATC2 in regulating muscle cell size
    • G. K. Pavlath, V. Horsley, Cell fusion in skeletal muscle - Central role of NFATC2 in regulating muscle cell size. Cell Cycle 2, 420-423 (2003).
    • (2003) Cell Cycle , vol.2 , pp. 420-423
    • Pavlath, G.K.1    Horsley, V.2
  • 28
    • 0035827711 scopus 로고    scopus 로고
    • Nuclear factor κB-inducing kinase and IκB kinase-α signal skeletal muscle cell differentiation
    • J. Canicio, P. Ruiz-Lozano, M. Carrasco, M. Palacin, K. Chien, A. Zorzano, P. Kaliman, Nuclear factor κB-inducing kinase and IκB kinase-α signal skeletal muscle cell differentiation. J. Biol. Chem. 276, 20228-20233 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 20228-20233
    • Canicio, J.1    Ruiz-Lozano, P.2    Carrasco, M.3    Palacin, M.4    Chien, K.5    Zorzano, A.6    Kaliman, P.7
  • 29
    • 68049148471 scopus 로고    scopus 로고
    • CHFR, a potential tumor suppressor, downregulates interleukin-8 through the inhibition of NF-κB
    • L. Kashima, M. Toyota, H. Mita, H. Suzuki, M. Idogawa, K. Ogi, Y. Sasaki, T. Tokino, CHFR, a potential tumor suppressor, downregulates interleukin-8 through the inhibition of NF-κB. Oncogene 28, 2643- 2653 (2009).
    • (2009) Oncogene , vol.28 , pp. 2643-2653
    • Kashima, L.1    Toyota, M.2    Mita, H.3    Suzuki, H.4    Idogawa, M.5    Ogi, K.6    Sasaki, Y.7    Tokino, T.8
  • 32
    • 35948994157 scopus 로고    scopus 로고
    • Autocrine TNFα signaling renders human cancer cells susceptible to Smac-mimetic-induced apoptosis
    • S. L. Petersen, L. Wang, A. Yalcin-Chin, L. Li, M. Peyton, J. Minna, P. Harran, X. Wang, Autocrine TNFα signaling renders human cancer cells susceptible to Smac-mimetic-induced apoptosis. Cancer Cell 12, 445 -456 (2007).
    • (2007) Cancer Cell , vol.12 , pp. 445-456
    • Petersen, S.L.1    Wang, L.2    Yalcin-Chin, A.3    Li, L.4    Peyton, M.5    Minna, J.6    Harran, P.7    Wang, X.8
  • 34
    • 34249775509 scopus 로고    scopus 로고
    • TNF-related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle-wasting cytokine
    • C. Dogra, H. Changotra, N. Wedhas, X. Qin, J. E. Wergedal, A. Kumar, TNF-related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle-wasting cytokine. FASEB J. 21, 1857-1869 (2007).
    • (2007) FASEB J. , vol.21 , pp. 1857-1869
    • Dogra, C.1    Changotra, H.2    Wedhas, N.3    Qin, X.4    Wergedal, J.E.5    Kumar, A.6
  • 36
    • 34447519304 scopus 로고    scopus 로고
    • Fibroblast growth factor inducible 14 (Fn14) is required for the expression of myogenic regulatory factors and differentiation of myoblasts into myotubes. Evidence for TWEAK-independent functions of Fn14 during myogenesis
    • C. Dogra, S. L. Hall, N. Wedhas, T. A. Linkhart, A. Kumar, Fibroblast growth factor inducible 14 (Fn14) is required for the expression of myogenic regulatory factors and differentiation of myoblasts into myotubes. Evidence for TWEAK-independent functions of Fn14 during myogenesis. J. Biol. Chem. 282, 15000-15010 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 15000-15010
    • Dogra, C.1    Hall, S.L.2    Wedhas, N.3    Linkhart, T.A.4    Kumar, A.5
  • 38
    • 77952912228 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF) signaling, but not TWEAK (TNF-like weak inducer of apoptosis)-triggered cIAP1 (cellular inhibitor of apoptosis protein 1) degradation, requires cIAP1 RING dimerization and E2 binding
    • R. Feltham, M. Moulin, J. E. Vince, P. D. Mace, W. W. Wong, H. Anderton, C. L. Day, D. L. Vaux, J. Silke, Tumor necrosis factor (TNF) signaling, but not TWEAK (TNF-like weak inducer of apoptosis)-triggered cIAP1 (cellular inhibitor of apoptosis protein 1) degradation, requires cIAP1 RING dimerization and E2 binding. J. Biol. Chem. 285, 17525-17536 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 17525-17536
    • Feltham, R.1    Moulin, M.2    Vince, J.E.3    Mace, P.D.4    Wong, W.W.5    Anderton, H.6    Day, C.L.7    Vaux, D.L.8    Silke, J.9
  • 39
    • 0041355229 scopus 로고    scopus 로고
    • TWEAK mediates signal transduction and differentiation of RAW264.7 cells in the absence of Fn14/TweakR. Evidence for a second TWEAK receptor
    • T. C. Polek, M. Talpaz, B. G. Darnay, T. Spivak-Kroizman, TWEAK mediates signal transduction and differentiation of RAW264.7 cells in the absence of Fn14/TweakR. Evidence for a second TWEAK receptor. J. Biol. Chem. 278, 32317-32323 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 32317-32323
    • Polek, T.C.1    Talpaz, M.2    Darnay, B.G.3    Spivak-Kroizman, T.4
  • 40
    • 0032562574 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathway is involved in the differentiation of muscle cells
    • E. Gredinger, A. N. Gerber, Y. Tamir, S. J. Tapscott, E. Bengal, Mitogen-activated protein kinase pathway is involved in the differentiation of muscle cells. J. Biol. Chem. 273, 10436-10444 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 10436-10444
    • Gredinger, E.1    Gerber, A.N.2    Tamir, Y.3    Tapscott, S.J.4    Bengal, E.5
  • 41
    • 70349973832 scopus 로고    scopus 로고
    • MEK1 plays contrary stage-specific roles in skeletal myogenic differentiation
    • C. Jo, B. G. Jang, S. A. Jo, MEK1 plays contrary stage-specific roles in skeletal myogenic differentiation. Cell. Signal. 21, 1910-1917 (2009).
    • (2009) Cell. Signal. , vol.21 , pp. 1910-1917
    • Jo, C.1    Jang, B.G.2    Jo, S.A.3
  • 42
    • 33744543239 scopus 로고    scopus 로고
    • ERK2 is required for efficient terminal differentiation of skeletal myoblasts
    • J. Li, S. E. Johnson, ERK2 is required for efficient terminal differentiation of skeletal myoblasts. Biochem. Biophys. Res. Commun. 345, 1425-1433 (2006).
    • (2006) Biochem. Biophys. Res. Commun. , vol.345 , pp. 1425-1433
    • Li, J.1    Johnson, S.E.2
  • 43
    • 77955808417 scopus 로고    scopus 로고
    • MAP kinase phosphatase-1 deficiency impairs skeletal muscle regeneration and exacerbates muscular dystrophy
    • H. Shi, E. Boadu, F. Mercan, A. M. Le, R. J. Flach, L. Zhang, K. J. Tyner, B. B. Olwin, A. M. Bennett, MAP kinase phosphatase-1 deficiency impairs skeletal muscle regeneration and exacerbates muscular dystrophy. FASEB J. 24, 2985-2997 (2010).
    • (2010) FASEB J. , vol.24 , pp. 2985-2997
    • Shi, H.1    Boadu, E.2    Mercan, F.3    Le, A.M.4    Flach, R.J.5    Zhang, L.6    Tyner, K.J.7    Olwin, B.B.8    Bennett, A.M.9
  • 45
    • 84934434314 scopus 로고    scopus 로고
    • Molecular control of mammalian myoblast fusion
    • K. M. Jansen, G. K. Pavlath, Molecular control of mammalian myoblast fusion. Methods Mol. Biol. 475, 115-133 (2008).
    • (2008) Methods Mol. Biol. , vol.475 , pp. 115-133
    • Jansen, K.M.1    Pavlath, G.K.2
  • 49
    • 79955646090 scopus 로고    scopus 로고
    • S100B in myoblasts regulates the transition from activation to quiescence and from quiescence to activation and reduces apoptosis
    • C. Tubaro, C. Arcuri, I. Giambanco, R. Donato, S100B in myoblasts regulates the transition from activation to quiescence and from quiescence to activation and reduces apoptosis. Biochim. Biophys. Acta 1813, 1092- 1104 (2011).
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1092-1104
    • Tubaro, C.1    Arcuri, C.2    Giambanco, I.3    Donato, R.4
  • 51
    • 4344638224 scopus 로고    scopus 로고
    • Glutathione depletion impairs myogenic differentiation of murine skeletal muscle C2C12 cells through sustained NF-κB activation
    • E. Ardite, J. A. Barbera, J. Roca, J. C. Fernández-Checa, Glutathione depletion impairs myogenic differentiation of murine skeletal muscle C2C12 cells through sustained NF-κB activation. Am. J. Pathol. 165, 719-728 (2004).
    • (2004) Am. J. Pathol. , vol.165 , pp. 719-728
    • Ardite, E.1    Barbera, J.A.2    Roca, J.3    Fernández-Checa, J.C.4
  • 54
    • 80054841161 scopus 로고    scopus 로고
    • Information transduction capacity of noisy biochemical signaling networks
    • R. Cheong, A. Rhee, C. J. Wang, I. Nemenman, A. Levchenko, Information transduction capacity of noisy biochemical signaling networks. Science 334, 354-358 (2011).
    • (2011) Science , vol.334 , pp. 354-358
    • Cheong, R.1    Rhee, A.2    Wang, C.J.3    Nemenman, I.4    Levchenko, A.5
  • 58
    • 84863791825 scopus 로고    scopus 로고
    • Tumor necrosis factor-like weak inducer of apoptosis (TWEAK) mediates p38 mitogen-activated protein kinase activation and signal transduction in peripheral blood mononuclear cells from patients with lupus nephritis
    • L. Zhi-Chun, Z. Qiao-Ling, L. Zhi-Qin, L. Xiao-Zhao, Z. Xiao-Xia, T. Rong, Tumor necrosis factor-like weak inducer of apoptosis (TWEAK) mediates p38 mitogen-activated protein kinase activation and signal transduction in peripheral blood mononuclear cells from patients with lupus nephritis. Inflammation 35, 935-943 (2012).
    • (2012) Inflammation , vol.35 , pp. 935-943
    • Zhi-Chun, L.1    Qiao-Ling, Z.2    Zhi-Qin, L.3    Xiao-Zhao, L.4    Xiao-Xia, Z.5    Rong, T.6
  • 59
    • 61449148439 scopus 로고    scopus 로고
    • TNF-like weak inducer of apoptosis (TWEAK) activates proinflammatory signaling pathways and gene expression through the activation of TGF-β-activated kinase 1
    • M. Kumar, D. Y. Makonchuk, H. Li, A. Mittal, A. Kumar, TNF-like weak inducer of apoptosis (TWEAK) activates proinflammatory signaling pathways and gene expression through the activation of TGF-β-activated kinase 1. J. Immunol. 182, 2439- 2448 (2009).
    • (2009) J. Immunol. , vol.182 , pp. 2439-2448
    • Kumar, M.1    Makonchuk, D.Y.2    Li, H.3    Mittal, A.4    Kumar, A.5
  • 60
    • 77957338124 scopus 로고    scopus 로고
    • Genetic ablation of TWEAK augments regeneration and post-injury growth of skeletal muscle in mice
    • A. Mittal, S. Bhatnagar, A. Kumar, P. K. Paul, S. Kuang, A. Kumar, Genetic ablation of TWEAK augments regeneration and post-injury growth of skeletal muscle in mice. Am. J. Pathol. 177, 1732-1742 (2010).
    • (2010) Am. J. Pathol. , vol.177 , pp. 1732-1742
    • Mittal, A.1    Bhatnagar, S.2    Kumar, A.3    Paul, P.K.4    Kuang, S.5    Kumar, A.6
  • 62
    • 34250669605 scopus 로고    scopus 로고
    • TNF-α regulates myogenesis and muscle regeneration by activating p38 MAPK
    • S. E. Chen, B. Jin, Y. P. Li, TNF-α regulates myogenesis and muscle regeneration by activating p38 MAPK. Am. J. Physiol. Cell Physiol. 292, C1660-C1671 (2007).
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Chen, S.E.1    Jin, B.2    Li, Y.P.3
  • 63
    • 80053339572 scopus 로고    scopus 로고
    • TWEAK causes myotube atrophy through coordinated activation of ubiquitin-proteasome system, autophagy, and caspases
    • S. Bhatnagar, A. Mittal, S. K. Gupta, A. Kumar, TWEAK causes myotube atrophy through coordinated activation of ubiquitin-proteasome system, autophagy, and caspases. J. Cell. Physiol. 227, 1042 -1051 (2012).
    • (2012) J. Cell. Physiol. , vol.227 , pp. 1042-1051
    • Bhatnagar, S.1    Mittal, A.2    Gupta, S.K.3    Kumar, A.4
  • 64
    • 9144264424 scopus 로고    scopus 로고
    • Cloning and characterization of the rat homologues of the Inhibitor of Apoptosis protein 1, 2, and 3 genes
    • M. Holcik, C. A. Lefebvre, K. Hicks, R. G. Korneluk, Cloning and characterization of the rat homologues of the Inhibitor of Apoptosis protein 1, 2, and 3 genes. BMC Genomics 3, 5 (2002).
    • (2002) BMC Genomics , vol.3 , pp. 5
    • Holcik, M.1    Lefebvre, C.A.2    Hicks, K.3    Korneluk, R.G.4
  • 65
    • 0032955888 scopus 로고    scopus 로고
    • Resolution of (+/-)-1-aryl-2-propynylamines via acyltransfer catalyzed by Candida antarctica lipase
    • F. Messina, M. Botta, F. Corelli, M. P. Schneider, F. Fazio, Resolution of (+/-)-1-aryl-2-propynylamines via acyltransfer catalyzed by Candida antarctica lipase. J. Org. Chem. 64, 3767-3769 (1999).
    • (1999) J. Org. Chem. , vol.64 , pp. 3767-3769
    • Messina, F.1    Botta, M.2    Corelli, F.3    Schneider, M.P.4    Fazio, F.5
  • 67
    • 0001037211 scopus 로고
    • Macro rings. VII. The spectral consequences of bringing two benzene rings face to face
    • D. J. Cram, N. L. Allinger, H. Steinberg, Macro rings. VII. The spectral consequences of bringing two benzene rings face to face. J. Am. Chem. Soc. 76, 6132-6141 (1954).
    • (1954) J. Am. Chem. Soc. , vol.76 , pp. 6132-6141
    • Cram, D.J.1    Allinger, N.L.2    Steinberg, H.3
  • 69
    • 33645852269 scopus 로고    scopus 로고
    • Regio- And diastereo-controlled synthesis of bis(formylmethano)[60] fullerenes and their application to the formation of [60]fullerene pearl-necklace polyimines
    • H. Ito, Y. Ishida, K. Saigo, Regio- and diastereo-controlled synthesis of bis(formylmethano)[60]fullerenes and their application to the formation of [60]fullerene pearl-necklace polyimines. Tetrahedron Lett. 47, 3095-3098 (2006).
    • (2006) Tetrahedron Lett. , vol.47 , pp. 3095-3098
    • Ito, H.1    Ishida, Y.2    Saigo, K.3
  • 73
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise huisgen cycloaddition process: Copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes
    • V. V. Rostovtsev, L. G. Green, V. V. Fokin, K. B. Sharpless, A stepwise huisgen cycloaddition process: Copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes. Angew. Chem. Int. Ed. Engl. 41, 2596-2599 (2002).
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 2596-2599
    • Rostovtsev, V.V.1    Green, L.G.2    Fokin, V.V.3    Sharpless, K.B.4


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