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      Characterization of anti-inflammatory effect of soybean septapeptide and its molecular mechanism

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      https://www.riss.kr/link?id=A105920664

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      다국어 초록 (Multilingual Abstract)

      Activation of nuclear factor kappa B (NFκB) leads to theinflammatory process. During this NFκB-dependent inflammationprocess, inducible nitric oxide synthase (iNOS) are expressedin the inflammatory cells. Our previous data indicated that aspecific septapeptide (GVAWWMY) from the soybean extractfermented by Bacillus licheniformis B1 inhibited iNOS mRNAexpression and NO production in cultured macrophage cells. Ourfurther experiments revealed that treatment of same septapeptideresulted in inhibition of LPS-induced NFκB activation byreversing degradation of IκBα, an inhibitory protein for NFκB.
      The molecular docking indicated that the septapeptide binds toIκB kinase β (IKKβ), and thus it can inhibit phosphorylation ofIκBα. Supporting this, the binding site for the septapeptide hasthe highest affinity (-8.7 kcal/mol) and the site was located atthe kinase domain (KD) of IKKβ, which can significantlyaffect the kinase activity of IKKβ.
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      Activation of nuclear factor kappa B (NFκB) leads to theinflammatory process. During this NFκB-dependent inflammationprocess, inducible nitric oxide synthase (iNOS) are expressedin the inflammatory cells. Our previous data indicated that aspecific s...

      Activation of nuclear factor kappa B (NFκB) leads to theinflammatory process. During this NFκB-dependent inflammationprocess, inducible nitric oxide synthase (iNOS) are expressedin the inflammatory cells. Our previous data indicated that aspecific septapeptide (GVAWWMY) from the soybean extractfermented by Bacillus licheniformis B1 inhibited iNOS mRNAexpression and NO production in cultured macrophage cells. Ourfurther experiments revealed that treatment of same septapeptideresulted in inhibition of LPS-induced NFκB activation byreversing degradation of IκBα, an inhibitory protein for NFκB.
      The molecular docking indicated that the septapeptide binds toIκB kinase β (IKKβ), and thus it can inhibit phosphorylation ofIκBα. Supporting this, the binding site for the septapeptide hasthe highest affinity (-8.7 kcal/mol) and the site was located atthe kinase domain (KD) of IKKβ, which can significantlyaffect the kinase activity of IKKβ.

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      참고문헌 (Reference)

      1 松井利郞, "청국장으로부터 Angiotensin Ⅰ전환효소 저해 Peptide의 분리" 한국미생물학회 40 (40): 355-358, 2004

      2 유형재, "청국장에 존재하는 Isoflavone의 Mass 분석" 한국미생물학회 43 (43): 54-58, 2007

      3 Eric F. Pettersen, "UCSF Chimera?A visualization system for exploratory research and analysis" Wiley 25 (25): 1605-1612, 2004

      4 Lawrence A Kelley, "The Phyre2 web portal for protein modeling, prediction and analysis" Springer Nature 10 (10): 845-858, 2015

      5 Cramer P, "Structure of the human NF-${\kappa}B$ p52 homodimer-DNA complex at 2.1 ${\AA}$ resolution" 16 : 7078-7090, 1997

      6 Christoph W. Müller, "Structure of the NF-κB p50 homodimer bound to DNA" Springer Nature 373 (373): 311-317, 1995

      7 James C. Stroud, "Structural Basis of HIV-1 Activation by NF-κB—A Higher-Order Complex of p50:RelA Bound to the HIV-1 LTR" Elsevier BV 393 (393): 98-112, 2009

      8 이우형, "Specific Oligopeptides in Fermented Soybean Extract Inhibit NF-κB-Dependent iNOS and Cytokine Induction by Toll-Like Receptor Ligands" 한국식품영양과학회 17 (17): 1239-1246, 2014

      9 Sanner MF, "Phython: a programming language for software integration and development" 17 : 57-61, 1999

      10 Adams PD, "Phenix: a comprehensive Python-based system for macromolecular structure resolution" D66 : 213-221, 2010

      1 松井利郞, "청국장으로부터 Angiotensin Ⅰ전환효소 저해 Peptide의 분리" 한국미생물학회 40 (40): 355-358, 2004

      2 유형재, "청국장에 존재하는 Isoflavone의 Mass 분석" 한국미생물학회 43 (43): 54-58, 2007

      3 Eric F. Pettersen, "UCSF Chimera?A visualization system for exploratory research and analysis" Wiley 25 (25): 1605-1612, 2004

      4 Lawrence A Kelley, "The Phyre2 web portal for protein modeling, prediction and analysis" Springer Nature 10 (10): 845-858, 2015

      5 Cramer P, "Structure of the human NF-${\kappa}B$ p52 homodimer-DNA complex at 2.1 ${\AA}$ resolution" 16 : 7078-7090, 1997

      6 Christoph W. Müller, "Structure of the NF-κB p50 homodimer bound to DNA" Springer Nature 373 (373): 311-317, 1995

      7 James C. Stroud, "Structural Basis of HIV-1 Activation by NF-κB—A Higher-Order Complex of p50:RelA Bound to the HIV-1 LTR" Elsevier BV 393 (393): 98-112, 2009

      8 이우형, "Specific Oligopeptides in Fermented Soybean Extract Inhibit NF-κB-Dependent iNOS and Cytokine Induction by Toll-Like Receptor Ligands" 한국식품영양과학회 17 (17): 1239-1246, 2014

      9 Sanner MF, "Phython: a programming language for software integration and development" 17 : 57-61, 1999

      10 Adams PD, "Phenix: a comprehensive Python-based system for macromolecular structure resolution" D66 : 213-221, 2010

      11 Erika Mathes, "NF-κB dictates the degradation pathway of IκBα" Wiley 27 (27): 1357-1367, 2008

      12 Makarov SS, "NF-kappaB in rheumatoid arthritis: a pivotal regulator of inflammation, hyperplasia, and tissue destruction" 3 : 200-206, 2001

      13 Dolcet X, "NF-${\kappa}B$ in development and progression of human cancer" 446 : 475-482, 2005

      14 Sankar Ghosh, "Missing Pieces in the NF-κB Puzzle" Elsevier BV 109 (109): S81-S96, 2002

      15 Simon T. Whiteside, "IκB proteins: structure, function and regulation" Elsevier BV 8 (8): 75-82, 1997

      16 Jae Sung Hwang*, "Inflammation-Related Signaling Pathways Implicating TGFβ are Revealed in the Expression Profiling of MCF7 Cell Treated with Fermented Soybean, Chungkookjang" Informa UK Limited 63 (63): 645-652, 2011

      17 Strana J., "Ikappa B kinase inhibitors for treating auto immune and inflammatory disorders: potential and challenges" 28 : 142-148, 2007

      18 M. N. Ndlovu, "Hyperactivated NF- B and AP-1 Transcription Factors Promote Highly Accessible Chromatin and Constitutive Transcription across the Interleukin-6 Gene Promoter in Metastatic Breast Cancer Cells" American Society for Microbiology 29 (29): 5488-5504, 2009

      19 Michael Karin, "How NF-κB is activated: the role of the IκB kinase (IKK) complex" Springer Nature 18 (18): 6867-6874, 1999

      20 Lee JJ, "Fermentation patterns of Chungkookjang and Kanjang by Bacillus licheniformis B1" 35 : 296-301, 1999

      21 P. Emsley, "Features and development of Coot" International Union of Crystallography (IUCr) 66 (66): 486-501, 2010

      22 W. Shibata, "Cutting Edge: The I B Kinase (IKK) Inhibitor, NEMO-Binding Domain Peptide, Blocks Inflammatory Injury in Murine Colitis" The American Association of Immunologists 179 (179): 2681-2685, 2007

      23 Guozhou Xu, "Crystal structure of inhibitor of κB kinase β" Springer Nature 472 (472): 325-330, 2011

      24 Garrett M. Morris, "AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility" Wiley 30 (30): 2785-2791, 2009

      25 Trott O., "AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading" 31 : 455-461, 2010

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      학술지 이력

      학술지 이력
      연월일 이력구분 이력상세 등재구분
      2023 평가예정 해외DB학술지평가 신청대상 (해외등재 학술지 평가)
      2020-01-01 평가 등재학술지 유지 (해외등재 학술지 평가) KCI등재
      2013-12-02 학술지명변경 외국어명 : The Korean Journal of Microbiology -> Korean Journal of Microbiology KCI등재
      2010-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2008-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2006-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2004-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2001-01-01 평가 등재학술지 선정 (등재후보2차) KCI등재
      1998-07-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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      학술지 인용정보

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      기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
      2016 0.21 0.21 0.21
      KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
      0.26 0.24 0.48 0.02
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