메뉴 건너뛰기




Volumn 89, Issue 2, 2014, Pages 210-216

Adenanthin targets proteins involved in the regulation of disulphide bonds

Author keywords

Adenanthin; Cancer; Peroxiredoxin; Protein disulphide isomerase; Thioredoxin

Indexed keywords

ADENANTHIN; BINDING PROTEIN; DITERPENOID; INSULIN; PEROXIREDOXIN; PEROXIREDOXIN 1; PEROXIREDOXIN 2; PROTEIN DISULFIDE ISOMERASE; THIOREDOXIN; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG;

EID: 84899427005     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2014.02.022     Document Type: Article
Times cited : (32)

References (18)
  • 1
    • 84859866458 scopus 로고    scopus 로고
    • Adenanthin targets peroxiredoxin i and II to induce differentiation of leukemic cells
    • C.X. Liu, Q.Q. Yin, H.C. Zhou, Y.L. Wu, J.X. Pu, and L. Xia et al. Adenanthin targets peroxiredoxin I and II to induce differentiation of leukemic cells Nat Chem Biol 8 2012 486 493
    • (2012) Nat Chem Biol , vol.8 , pp. 486-493
    • Liu, C.X.1    Yin, Q.Q.2    Zhou, H.C.3    Wu, Y.L.4    Pu, J.X.5    Xia, L.6
  • 2
    • 84883439176 scopus 로고    scopus 로고
    • Preventive and therapeutic effects of adenanthin on experimental autoimmune encephalomyelitis by inhibiting NF-kappaB signaling
    • Q.Q. Yin, C.X. Liu, Y.L. Wu, S.F. Wu, Y. Wang, and X. Zhang et al. Preventive and therapeutic effects of adenanthin on experimental autoimmune encephalomyelitis by inhibiting NF-kappaB signaling J Immunol 191 2013 2115 2125
    • (2013) J Immunol , vol.191 , pp. 2115-2125
    • Yin, Q.Q.1    Liu, C.X.2    Wu, Y.L.3    Wu, S.F.4    Wang, Y.5    Zhang, X.6
  • 3
    • 84855835527 scopus 로고    scopus 로고
    • Studies toward novel peptidomimetic inhibitors of thioredoxin-thioredoxin reductase system
    • S. Klossowski, A. Muchowicz, M. Firczuk, M. Swiech, A. Redzej, and J. Golab et al. Studies toward novel peptidomimetic inhibitors of thioredoxin-thioredoxin reductase system J Med Chem 55 2012 55 67
    • (2012) J Med Chem , vol.55 , pp. 55-67
    • Klossowski, S.1    Muchowicz, A.2    Firczuk, M.3    Swiech, M.4    Redzej, A.5    Golab, J.6
  • 4
    • 24644441050 scopus 로고    scopus 로고
    • The thioredoxin reductase/thioredoxin system: Novel redox targets for cancer therapy
    • J.E. Biaglow, and R.A. Miller The thioredoxin reductase/thioredoxin system: novel redox targets for cancer therapy Cancer Biol Ther 4 2005 6 13
    • (2005) Cancer Biol Ther , vol.4 , pp. 6-13
    • Biaglow, J.E.1    Miller, R.A.2
  • 6
    • 0026715172 scopus 로고
    • Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62
    • J.R. Matthews, N. Wakasugi, J.L. Virelizier, J. Yodoi, and R.T. Hay Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62 Nucleic Acids Res 20 1992 3821 3830
    • (1992) Nucleic Acids Res , vol.20 , pp. 3821-3830
    • Matthews, J.R.1    Wakasugi, N.2    Virelizier, J.L.3    Yodoi, J.4    Hay, R.T.5
  • 7
    • 84856940017 scopus 로고    scopus 로고
    • Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides
    • S.G. Rhee, H.A. Woo, I.S. Kil, and S.H. Bae Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides J Biol Chem 287 2012 4403 4410
    • (2012) J Biol Chem , vol.287 , pp. 4403-4410
    • Rhee, S.G.1    Woo, H.A.2    Kil, I.S.3    Bae, S.H.4
  • 8
    • 0029644246 scopus 로고
    • Thioredoxin structure and mechanism: Conformational changes on oxidation of the active-site sulfhydryls to a disulfide
    • A. Holmgren Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide Structure 3 1995 239 243
    • (1995) Structure , vol.3 , pp. 239-243
    • Holmgren, A.1
  • 9
    • 12244275240 scopus 로고    scopus 로고
    • The thioredoxin-1 inhibitor 1-methylpropyl 2-imidazolyl disulfide (PX-12) decreases vascular permeability in tumor xenografts monitored by dynamic contrast enhanced magnetic resonance imaging
    • B.F. Jordan, M. Runquist, N. Raghunand, R.J. Gillies, W.R. Tate, and G. Powis et al. The thioredoxin-1 inhibitor 1-methylpropyl 2-imidazolyl disulfide (PX-12) decreases vascular permeability in tumor xenografts monitored by dynamic contrast enhanced magnetic resonance imaging Clin Cancer Res 11 2005 529 536
    • (2005) Clin Cancer Res , vol.11 , pp. 529-536
    • Jordan, B.F.1    Runquist, M.2    Raghunand, N.3    Gillies, R.J.4    Tate, W.R.5    Powis, G.6
  • 10
    • 0018728098 scopus 로고
    • Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action
    • A. Holmgren Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action J Biol Chem 254 1979 9113 9119
    • (1979) J Biol Chem , vol.254 , pp. 9113-9119
    • Holmgren, A.1
  • 12
    • 78149469953 scopus 로고    scopus 로고
    • Multiple catalytically active thioredoxin folds: A winning strategy for many functions
    • E. Pedone, D. Limauro, K. D'Ambrosio, G. De Simone, and S. Bartolucci Multiple catalytically active thioredoxin folds: a winning strategy for many functions Cell Mol Life Sci 67 2010 3797 3814
    • (2010) Cell Mol Life Sci , vol.67 , pp. 3797-3814
    • Pedone, E.1    Limauro, D.2    D'Ambrosio, K.3    De Simone, G.4    Bartolucci, S.5
  • 13
    • 84874051169 scopus 로고    scopus 로고
    • Thioredoxin and thioredoxin target proteins: From molecular mechanisms to functional significance
    • S. Lee, S.M. Kim, and R.T. Lee Thioredoxin and thioredoxin target proteins: from molecular mechanisms to functional significance Antioxid Redox Signal 18 2013 1165 1207
    • (2013) Antioxid Redox Signal , vol.18 , pp. 1165-1207
    • Lee, S.1    Kim, S.M.2    Lee, R.T.3
  • 14
    • 84874112079 scopus 로고    scopus 로고
    • The critical roles of endoplasmic reticulum chaperones and unfolded protein response in tumorigenesis and anticancer therapies
    • B. Luo, and A.S. Lee The critical roles of endoplasmic reticulum chaperones and unfolded protein response in tumorigenesis and anticancer therapies Oncogene 32 2013 805 818
    • (2013) Oncogene , vol.32 , pp. 805-818
    • Luo, B.1    Lee, A.S.2
  • 15
    • 84878240943 scopus 로고    scopus 로고
    • Targeting allosteric disulphide bonds in cancer
    • P.J. Hogg Targeting allosteric disulphide bonds in cancer Nat Rev Cancer 13 2013 425 431
    • (2013) Nat Rev Cancer , vol.13 , pp. 425-431
    • Hogg, P.J.1
  • 16
    • 84876114193 scopus 로고    scopus 로고
    • Post-translational control of protein function by disulfide bond cleavage
    • K.M. Cook, and P.J. Hogg Post-translational control of protein function by disulfide bond cleavage Antioxid Redox Signal 18 2013 1987 2015
    • (2013) Antioxid Redox Signal , vol.18 , pp. 1987-2015
    • Cook, K.M.1    Hogg, P.J.2
  • 17
    • 78649484651 scopus 로고    scopus 로고
    • Control of mature protein function by allosteric disulfide bonds
    • I. Azimi, J.W. Wong, and P.J. Hogg Control of mature protein function by allosteric disulfide bonds Antioxid Redox Signal 14 2011 113 126
    • (2011) Antioxid Redox Signal , vol.14 , pp. 113-126
    • Azimi, I.1    Wong, J.W.2    Hogg, P.J.3
  • 18
    • 84857237485 scopus 로고    scopus 로고
    • Thioredoxin-1 and protein disulfide isomerase catalyze the reduction of similar disulfides in HIV gp120
    • K. Reiser, K.O. Francois, D. Schols, T. Bergman, H. Jornvall, and J. Balzarini et al. Thioredoxin-1 and protein disulfide isomerase catalyze the reduction of similar disulfides in HIV gp120 Int J Biochem Cell Biol 44 2012 556 562
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 556-562
    • Reiser, K.1    Francois, K.O.2    Schols, D.3    Bergman, T.4    Jornvall, H.5    Balzarini, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.