메뉴 건너뛰기




Volumn 18, Issue 7, 2013, Pages 8083-8094

Luteolin inhibits inflammatory responses via p38/MK2/TTP-mediated mRNA stability

Author keywords

Anti inflammatory; Bone marrow macrophages; Luteolin; MRNA stability

Indexed keywords

ANTIINFLAMMATORY AGENT; HERBACEOUS AGENT; INTERLEUKIN 6; LUTEOLIN; MAP-KINASE-ACTIVATED KINASE 2; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE P38; NONSTEROID ANTIINFLAMMATORY AGENT; PROTEIN SERINE THREONINE KINASE; SIGNAL PEPTIDE; TRISTETRAPROLIN; TUMOR NECROSIS FACTOR ALPHA; MAP KINASE ACTIVATED KINASE 2;

EID: 84880763686     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules18078083     Document Type: Article
Times cited : (41)

References (41)
  • 2
    • 9744242794 scopus 로고    scopus 로고
    • Dietary flavonoids and cancer risk: Evidence from human population studies
    • Neuhouser, M.L. Dietary flavonoids and cancer risk: Evidence from human population studies. Nutr. Cancer 2004, 50, 1-7.
    • (2004) Nutr. Cancer , vol.50 , pp. 1-7
    • Neuhouser, M.L.1
  • 3
    • 33750567782 scopus 로고    scopus 로고
    • Immunomodulating effects of flavonoids on acute and chronic inflammatory responses caused by tumor necrosis factor alpha
    • Kumazawa, Y.; Kawaguchi, K.; Takimoto, H. Immunomodulating effects of flavonoids on acute and chronic inflammatory responses caused by tumor necrosis factor alpha. Curr. Pharm. Des. 2006, 12, 4271-4279.
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 4271-4279
    • Kumazawa, Y.1    Kawaguchi, K.2    Takimoto, H.3
  • 4
    • 33646759971 scopus 로고    scopus 로고
    • Luteolin and chrysin differentially inhibit cyclooxygenase-2 expression and scavenge reactive oxygen species but similarly inhibit prostaglandin-E2 formation in RAW 264.7 cells
    • Harris, G.K.; Qian, Y.; Leonard, S.S.; Sbarra, D.C; Shi, X. Luteolin and chrysin differentially inhibit cyclooxygenase-2 expression and scavenge reactive oxygen species but similarly inhibit prostaglandin-E2 formation in RAW 264.7 cells. J. Nutr. 2006, 136, 1517-1521.
    • (2006) J. Nutr. , vol.136 , pp. 1517-1521
    • Harris, G.K.1    Qian, Y.2    Leonard, S.S.3    Sbarra, D.C.4    Shi, X.5
  • 5
    • 79956093234 scopus 로고    scopus 로고
    • Luteolin and chicoric acid synergistically inhibited inflammatory responses via inactivation of PI3K-Akt pathway and impairment of NF-kappaB translocation in LPS stimulated RAW 264.7 cells
    • Park, C.M.; Jin, K.S; Lee, Y.W.; Song, Y.S. Luteolin and chicoric acid synergistically inhibited inflammatory responses via inactivation of PI3K-Akt pathway and impairment of NF-kappaB translocation in LPS stimulated RAW 264.7 cells. Eur. J. Pharmacol. 2011, 660, 454-459.
    • (2011) Eur. J. Pharmacol. , vol.660 , pp. 454-459
    • Park, C.M.1    Jin, K.S.2    Lee, Y.W.3    Song, Y.S.4
  • 6
    • 84859104481 scopus 로고    scopus 로고
    • Luteolin inhibited hydrogen peroxide-induced vascular smooth muscle cells proliferation and migration by suppressing the Src and Akt signalling pathways
    • Lang, Y.; Chen, D; Li, D.Y.; Zhu, M.Y.; Xu, T.D.; Zhang, T.; Qian, W.H.; Luo, Y.Y. Luteolin inhibited hydrogen peroxide-induced vascular smooth muscle cells proliferation and migration by suppressing the Src and Akt signalling pathways. J. Pharm. Pharmacol. 2012, 64, 597-603.
    • (2012) J. Pharm. Pharmacol. , vol.64 , pp. 597-603
    • Lang, Y.1    Chen, D.2    Li, D.Y.3    Zhu, M.Y.4    Xu, T.D.5    Zhang, T.6    Qian, W.H.7    Luo, Y.Y.8
  • 7
    • 84874442882 scopus 로고    scopus 로고
    • Luteolin inhibits angiotensin II-induced human umbilical vein endothelial cell proliferation and migration through downregulation of Src and Akt phosphorylation
    • Zhu, M.Y.; Chen, D.; Li, D.Y.; Ding, H.; Zhang, T.; Xu, T.D.; Zhang, Y.B. Luteolin inhibits angiotensin II-induced human umbilical vein endothelial cell proliferation and migration through downregulation of Src and Akt phosphorylation. Circ. J. 2013, 77, 772-779.
    • (2013) Circ. J. , vol.77 , pp. 772-779
    • Zhu, M.Y.1    Chen, D.2    Li, D.Y.3    Ding, H.4    Zhang, T.5    Xu, T.D.6    Zhang, Y.B.7
  • 8
    • 0037180771 scopus 로고    scopus 로고
    • Inflammation in atherosclerosis
    • Libby, P. Inflammation in atherosclerosis. Nature 2002, 420, 868-874.
    • (2002) Nature , vol.420 , pp. 868-874
    • Libby, P.1
  • 9
    • 52049104519 scopus 로고    scopus 로고
    • Pro-inflammatory cytokines in atherosclerosis
    • Szekanecz, Z. Pro-inflammatory cytokines in atherosclerosis. Isr. Med. Assoc. J. 2008, 10, 529-530.
    • (2008) Isr. Med. Assoc. J. , vol.10 , pp. 529-530
    • Szekanecz, Z.1
  • 10
    • 52049116741 scopus 로고    scopus 로고
    • Serum cytokine tumor necrosis factor-alpha and interleukin-6 associated with the severity of coronary artery disease: Indicators of an active inflammatory burden?
    • Gotsman, I.; Stabholz, A.; Planer, D.; Pugatsch, T.; Lapidus, L.; Novikov, Y.; Masrawa, S.; Soskolne, A.; Lotan, C. Serum cytokine tumor necrosis factor-alpha and interleukin-6 associated with the severity of coronary artery disease: indicators of an active inflammatory burden? Isr. Med. Assoc. J. 2008, 10, 494-498.
    • (2008) Isr. Med. Assoc. J. , vol.10 , pp. 494-498
    • Gotsman, I.1    Stabholz, A.2    Planer, D.3    Pugatsch, T.4    Lapidus, L.5    Novikov, Y.6    Masrawa, S.7    Soskolne, A.8    Lotan, C.9
  • 11
    • 84860320152 scopus 로고    scopus 로고
    • The regulation of mRNA stability in mammalian cells: 2.0
    • Wu, X.; Brewer, G. The regulation of mRNA stability in mammalian cells: 2.0. Gene 2012, 500, 10-21.
    • (2012) Gene , vol.500 , pp. 10-21
    • Wu, X.1    Brewer, G.2
  • 12
    • 2442647813 scopus 로고    scopus 로고
    • Distinct domains of AU-rich elements exert different functions in mRNA destabilization and stabilization by p38 mitogen-activated protein kinase or HuR
    • Winzen, R.; Gowrishankar, G.; Bollig F.; Redich, N.; Resch, K.; Holtmann, H. Distinct domains of AU-rich elements exert different functions in mRNA destabilization and stabilization by p38 mitogen-activated protein kinase or HuR. Mol. Cell. Biol. 2004, 24, 4835-4847.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4835-4847
    • Winzen, R.1    Gowrishankar, G.2    Bollig, F.3    Redich, N.4    Resch, K.5    Holtmann, H.6
  • 13
    • 0028788194 scopus 로고
    • AU-rich elements: Characterization and importance in mRNA degradation
    • Chen, C.Y.; Shyu, A.B. AU-rich elements: Characterization and importance in mRNA degradation. Trends Biochem. Sci. 1995, 20, 465-470.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 465-470
    • Chen, C.Y.1    Shyu, A.B.2
  • 14
    • 0023058975 scopus 로고
    • A conserved AU sequence from the 3' untranslated region of GM-CSF mRNA mediates selective mRNA degradation
    • Shaw, G.; Kamen, R. A conserved AU sequence from the 3' untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell 1986, 46, 659-667.
    • (1986) Cell , vol.46 , pp. 659-667
    • Shaw, G.1    Kamen, R.2
  • 16
    • 8544255551 scopus 로고    scopus 로고
    • The tandem CCCH zinc finger protein tristetraprolin and its relevance to cytokine mRNA turnover and arthritis
    • Carrick, D.M.; Lai, W.S.; Blackshear, P.J. The tandem CCCH zinc finger protein tristetraprolin and its relevance to cytokine mRNA turnover and arthritis. Arthritis Res. Ther. 2004, 6, 248-264.
    • (2004) Arthritis Res. Ther. , vol.6 , pp. 248-264
    • Carrick, D.M.1    Lai, W.S.2    Blackshear, P.J.3
  • 17
    • 0032601590 scopus 로고    scopus 로고
    • The search for trans-acting factors controlling messenger RNA decay
    • Wilson, G.M.; Brewer, G. The search for trans-acting factors controlling messenger RNA decay. Prog. Nucleic. Acid Res. Mol. Biol. 1999, 62, 257-291.
    • (1999) Prog. Nucleic. Acid Res. Mol. Biol. , vol.62 , pp. 257-291
    • Wilson, G.M.1    Brewer, G.2
  • 18
    • 3142546235 scopus 로고    scopus 로고
    • The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation
    • Dean, J.L.; Sully G.; Clark A.R.; Saklatvala J. The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation. Cell Signal 2004, 16, 1113-1121.
    • (2004) Cell Signal , vol.16 , pp. 1113-1121
    • Dean, J.L.1    Sully, G.2    Clark, A.R.3    Saklatvala, J.4
  • 20
    • 84859753189 scopus 로고    scopus 로고
    • MK2 posttranscriptionally regulates TNF-alpha-induced expression of ICAM-1 and IL-8 via tristetraprolin in human pulmonary microvascular endothelial cells
    • Shi, J.X.; Su X.; Xu, J.; Zhang, W.Y.; Shi, Y. MK2 posttranscriptionally regulates TNF-alpha-induced expression of ICAM-1 and IL-8 via tristetraprolin in human pulmonary microvascular endothelial cells. Am. J. Physiol. Lung Cell Mol. Physiol. 2012, 302, 793-799.
    • (2012) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.302 , pp. 793-799
    • Shi, J.X.1    Su, X.2    Xu, J.3    Zhang, W.Y.4    Shi, Y.5
  • 21
    • 0033049125 scopus 로고    scopus 로고
    • Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabili-zation of tumor necrosis factor alpha mRNA
    • Lai, W.S.; Carballo, E.; Strum, J.R.; Kennington, E.A.; Phillips, R.S.; Blackshear, P.J. Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabili-zation of tumor necrosis factor alpha mRNA. Mol. Cell Biol. 1999, 19, 4311-4323.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 4311-4323
    • Lai, W.S.1    Carballo, E.2    Strum, J.R.3    Kennington, E.A.4    Phillips, R.S.5    Blackshear, P.J.6
  • 23
    • 0034816062 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor alpha mRNA stability
    • Mahtani, K. R.; Brook, M.; Dean, J.L.; Sully, G.; Saklatvala, J.; Clark, A.R. Mitogen-activated protein kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor alpha mRNA stability. Mol. Cell. Biol. 2001, 21, 6461-6469.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6461-6469
    • Mahtani, K.R.1    Brook, M.2    Dean, J.L.3    Sully, G.4    Saklatvala, J.5    Clark, A.R.6
  • 25
    • 33644767306 scopus 로고    scopus 로고
    • Posttranslational regulation of tristetraprolin subcellular localization and protein stability by p38 mitogen-activated protein kinase and extracellular signal-regulated kinase pathways
    • Brook, M.; Tchen, C.R.; Santalucia, T.; McIlrath, J.; Arthur, J.S.; Saklatvala, J.; Clark, A.R. Posttranslational regulation of tristetraprolin subcellular localization and protein stability by p38 mitogen-activated protein kinase and extracellular signal-regulated kinase pathways. Mol. Cell Biol. 2006, 26, 2408-2418.
    • (2006) Mol. Cell Biol. , vol.26 , pp. 2408-2418
    • Brook, M.1    Tchen, C.R.2    Santalucia, T.3    McIlrath, J.4    Arthur, J.S.5    Saklatvala, J.6    Clark, A.R.7
  • 26
    • 33644753147 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase-activated protein kinase 2 regulates tumor necrosis factor mRNA stability and translation mainly by altering tristetraprolin expression, stability, and binding to adenine/uridine-rich element
    • Hitti, E.; Brook, M.; Deppenmeier, S.; Gruber, A.D.; Radzioch, D.; Clark, A.R.; Blackshear, P.J.; Kotlyarov, A.; Gaestel, M. Mitogen-activated protein kinase-activated protein kinase 2 regulates tumor necrosis factor mRNA stability and translation mainly by altering tristetraprolin expression, stability, and binding to adenine/uridine-rich element. Mol. Cell Biol. 2006, 26, 2399-2407.
    • (2006) Mol. Cell Biol. , vol.26 , pp. 2399-2407
    • Hitti, E.1    Brook, M.2    Deppenmeier, S.3    Gruber, A.D.4    Radzioch, D.5    Clark, A.R.6    Blackshear, P.J.7    Kotlyarov, A.8    Gaestel, M.9
  • 27
    • 80051499526 scopus 로고    scopus 로고
    • Tristetraprolin regulates interleukin-6 expression through p38 MAPK-dependent affinity changes with mRNA 3' untranslated region
    • Zhao, W.; Liu, M.; D'Silva, N.J.; Kirkwood, K.L. Tristetraprolin regulates interleukin-6 expression through p38 MAPK-dependent affinity changes with mRNA 3' untranslated region. J. Interferon Cytokine Res. 2011, 31, 629-637.
    • (2011) J. Interferon Cytokine Res. , vol.31 , pp. 629-637
    • Zhao, W.1    Liu, M.2    D'Silva, N.J.3    Kirkwood, K.L.4
  • 28
    • 33947495156 scopus 로고    scopus 로고
    • Tristetraprolin (TTP)-14-3-3 complex formation protects TTP from dephosphorylation by protein phosphatase 2a and stabilizes tumor necrosis factor-alpha mRNA
    • Sun, L.; Stoecklin, G.; Van Way, S.; Hinkovska-Galcheva, V.; Guo, R.F.; Anderson, P.; Shanley, T.P. Tristetraprolin (TTP)-14-3-3 complex formation protects TTP from dephosphorylation by protein phosphatase 2a and stabilizes tumor necrosis factor-alpha mRNA. J. Biol. Chem. 2007, 282, 3766-3777.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3766-3777
    • Sun, L.1    Stoecklin, G.2    Van Way, S.3    Hinkovska-Galcheva, V.4    Guo, R.F.5    Anderson, P.6    Shanley, T.P.7
  • 29
    • 78049434471 scopus 로고    scopus 로고
    • MAPKAP kinases MK2 and MK3 in inflammation: Complex regulation of TNF biosynthesis via expression and phosphorylation of tristetraprolin
    • Ronkina, N.; Menon, M.B.; Schwermann, J.; Tiedje, C.; Hitti, E.; Kotlyarov, A.; Gaestel, M. MAPKAP kinases MK2 and MK3 in inflammation: Complex regulation of TNF biosynthesis via expression and phosphorylation of tristetraprolin. Biochem. Pharmacol. 2010, 80, 1915-1920.
    • (2010) Biochem. Pharmacol. , vol.80 , pp. 1915-1920
    • Ronkina, N.1    Menon, M.B.2    Schwermann, J.3    Tiedje, C.4    Hitti, E.5    Kotlyarov, A.6    Gaestel, M.7
  • 30
    • 80055117166 scopus 로고    scopus 로고
    • Regulation of monocyte subset proinflammatory responses within the lung microvasculature by the p38 MAPK/MK2 pathway
    • O'Dea, K.P.; Dokpesi, J.O.; Tatham, K.C.; Wilson, M.R.; Takata, M. Regulation of monocyte subset proinflammatory responses within the lung microvasculature by the p38 MAPK/MK2 pathway. Am. J. Physiol. Lung Cell Mol. Physiol. 2011, 301, 812-821.
    • (2011) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.301 , pp. 812-821
    • O'Dea, K.P.1    Dokpesi, J.O.2    Tatham, K.C.3    Wilson, M.R.4    Takata, M.5
  • 31
    • 79958037012 scopus 로고    scopus 로고
    • Luteolin inhibits microglial inflammation and improves neuron survival against inflammation
    • Zhu, L.H.; Bi, W.; Qi, R.B.; Wang, H.D.; Lu, D.X. Luteolin inhibits microglial inflammation and improves neuron survival against inflammation. Int. J. Neurosci. 2011, 121, 329-336.
    • (2011) Int. J. Neurosci. , vol.121 , pp. 329-336
    • Zhu, L.H.1    Bi, W.2    Qi, R.B.3    Wang, H.D.4    Lu, D.X.5
  • 32
    • 62749163781 scopus 로고    scopus 로고
    • Suppression of the TRIF-dependent signaling pathway of Toll-like receptors by luteolin
    • Lee, J.K.; Kim, S.Y.; Kim, Y.S; Lee, W.H.; Hwang, D.H.; Lee, J.Y. Suppression of the TRIF-dependent signaling pathway of Toll-like receptors by luteolin. Biochem. Pharmacol. 2009, 77, 1391-1400.
    • (2009) Biochem. Pharmacol. , vol.77 , pp. 1391-1400
    • Lee, J.K.1    Kim, S.Y.2    Kim, Y.S.3    Lee, W.H.4    Hwang, D.H.5    Lee, J.Y.6
  • 33
    • 84865092054 scopus 로고    scopus 로고
    • The acai flavonoid velutin is a potent anti-inflammatory agent: Blockade of LPS-mediated TNF-alpha and IL-6 production through inhibiting NF-kappaB activation and MAPK pathway
    • Xie, C.; Kang, J.; Li, Z.; Schauss, A.G.; Badger, T.M.; Nagarajan, S.; Wu, T.; Wu, X. The acai flavonoid velutin is a potent anti-inflammatory agent: blockade of LPS-mediated TNF-alpha and IL-6 production through inhibiting NF-kappaB activation and MAPK pathway. J. Nutr. Biochem. 2012, 23, 1184-1191.
    • (2012) J. Nutr. Biochem. , vol.23 , pp. 1184-1191
    • Xie, C.1    Kang, J.2    Li, Z.3    Schauss, A.G.4    Badger, T.M.5    Nagarajan, S.6    Wu, T.7    Wu, X.8
  • 34
    • 40949102111 scopus 로고    scopus 로고
    • Post-transcriptional control of cytokine production
    • Anderson, P. Post-transcriptional control of cytokine production. Nat. Immunol. 2008, 9, 353-359.
    • (2008) Nat. Immunol. , vol.9 , pp. 353-359
    • Anderson, P.1
  • 36
    • 79960123457 scopus 로고    scopus 로고
    • Tristetraprolin mediates anti-inflammatory effects of nicotine in lipopolysaccharide-stimulated macrophages
    • Joe, Y.; Kim, H.J.; Kim, S.; Chung, J.; Ko, M.S.; Lee, W.H.; Chang, K.C.; Park, J.W.; Chung, H.T. Tristetraprolin mediates anti-inflammatory effects of nicotine in lipopolysaccharide-stimulated macrophages. J. Biol. Chem. 2011, 286, 24735-24742.
    • (2011) J. Biol. Chem. , vol.286 , pp. 24735-24742
    • Joe, Y.1    Kim, H.J.2    Kim, S.3    Chung, J.4    Ko, M.S.5    Lee, W.H.6    Chang, K.C.7    Park, J.W.8    Chung, H.T.9
  • 37
    • 79954601097 scopus 로고    scopus 로고
    • Tristetraprolin-dependent post-transcriptional regulation of inflammatory cytokine mRNA expression by apolipoprotein A-I: Role of ATP-binding membrane cassette transporter A1 and signal transducer and activator of transcription 3
    • Yin, K.; Deng, X.; Mo, Z.C.; Zhao, G.J.; Jiang, J.; Cui, L.B.; Tan, C.Z.; Wen, G.B.; Fu, Y.; Tang, C.K. Tristetraprolin-dependent post-transcriptional regulation of inflammatory cytokine mRNA expression by apolipoprotein A-I: role of ATP-binding membrane cassette transporter A1 and signal transducer and activator of transcription 3. J. Biol. Chem. 2011, 286, 13834-13845.
    • (2011) J. Biol. Chem. , vol.286 , pp. 13834-13845
    • Yin, K.1    Deng, X.2    Mo, Z.C.3    Zhao, G.J.4    Jiang, J.5    Cui, L.B.6    Tan, C.Z.7    Wen, G.B.8    Fu, Y.9    Tang, C.K.10
  • 38
    • 33845807361 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase (MAPK)-activated protein kinases MK2 and MK3 cooperate in stimulation of tumor necrosis factor biosynthesis and stabilization of p38 MAPK
    • Ronkina, N.; Kotlyarov, A.; Dittrich-Breiholz, O.; Kracht, M.; Hitti, E.; Milarski, K.; Askew, R.; Marusic, S.; Lin, L.L. Gaestel, M.; et al. The mitogen-activated protein kinase (MAPK)-activated protein kinases MK2 and MK3 cooperate in stimulation of tumor necrosis factor biosynthesis and stabilization of p38 MAPK. Mol. Cell. Biol. 2007, 27, 170-181.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 170-181
    • Ronkina, N.1    Kotlyarov, A.2    Dittrich-Breiholz, O.3    Kracht, M.4    Hitti, E.5    Milarski, K.6    Askew, R.7    Marusic, S.8    Lin, L.L.9    Gaestel, M.10
  • 39
    • 78751504841 scopus 로고    scopus 로고
    • Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment
    • Clement, S.L.; Scheckel, C.; Stoecklin, G.; Lykke-Andersen, J. Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment. Mol. Cell Biol. 2011, 31, 256-266.
    • (2011) Mol. Cell Biol. , vol.31 , pp. 256-266
    • Clement, S.L.1    Scheckel, C.2    Stoecklin, G.3    Lykke-Andersen, J.4
  • 40
    • 45249098952 scopus 로고    scopus 로고
    • Control of mRNA decay by phosphorylation of tristetraprolin
    • Sandler, H.; Stoecklin, G. Control of mRNA decay by phosphorylation of tristetraprolin. Biochem. Soc. Trans. 2008, 36, 491-496.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 491-496
    • Sandler, H.1    Stoecklin, G.2
  • 41
    • 44949231424 scopus 로고    scopus 로고
    • Analyzing real-time PCR data by the comparative C(T) method
    • Schmittgen, T.D.; Livak, K.J. Analyzing real-time PCR data by the comparative C(T) method. Nat. Protoc. 2008, 3, 1101-1108.
    • (2008) Nat. Protoc. , vol.3 , pp. 1101-1108
    • Schmittgen, T.D.1    Livak, K.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.