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Volumn 8, Issue 12, 2013, Pages

Ubiquitin-specific peptidase 5, a target molecule of vialinin A, is a key molecule of TNF-α production in RBL-2H3 cells

Author keywords

[No Author keywords available]

Indexed keywords

BETA N ACETYLHEXOSAMINIDASE; DEUBIQUITINASE; INTERLEUKIN 4; MESSENGER RNA; SMALL INTERFERING RNA; TUMOR NECROSIS FACTOR ALPHA; UBIQUITIN SPECIFIC PEPTIDASE 13; UBIQUITIN SPECIFIC PEPTIDASE 4; UBIQUITIN SPECIFIC PEPTIDASE 5; UNCLASSIFIED DRUG;

EID: 84891896564     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0080931     Document Type: Article
Times cited : (20)

References (26)
  • 1
    • 0027925168 scopus 로고
    • New concepts about the mast cell
    • Galli SJ (1993) New concepts about the mast cell. N. Engl. J. Med. 328: 257-265.
    • (1993) N. Engl. J. Med. , vol.328 , pp. 257-265
    • Galli, S.J.1
  • 2
    • 0033604596 scopus 로고    scopus 로고
    • The epidemic of allergy and asthma
    • Holgate ST (1999) The epidemic of allergy and asthma. Nature 402: B2-B4.
    • (1999) Nature , vol.402
    • Holgate, S.T.1
  • 4
    • 0141991213 scopus 로고    scopus 로고
    • Human serum IgE-mediated mast cell degranulation shows poor correlation to allergen-specific IgE content
    • Marchand F, Mecheri S, Guilloux L, Iannascoli B, Weyer A, et al. (2003) Human serum IgE-mediated mast cell degranulation shows poor correlation to allergen-specific IgE content. Allergy 58: 1037-1043.
    • (2003) Allergy , vol.58 , pp. 1037-1043
    • Marchand, F.1    Mecheri, S.2    Guilloux, L.3    Iannascoli, B.4    Weyer, A.5
  • 5
    • 0034025339 scopus 로고    scopus 로고
    • Dependence of mast cell IgE-mediated cytokine production on nuclear factor-κB activity
    • Marquardt DL, Walker LL (2000) Dependence of mast cell IgE-mediated cytokine production on nuclear factor-κB activity. J. Allergy Clin. Immunol 105: 500-505.
    • (2000) J. Allergy Clin. Immunol , vol.105 , pp. 500-505
    • Marquardt, D.L.1    Walker, L.L.2
  • 6
    • 0033558357 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase activation through Fce receptor I and stem cell factor receptor id differentially regulated by phosphatidylinositol 3-kinase and calcineurin inmouse bone marrow-derived mast cells
    • Ishizuka T, Chayama K, Takeda K, Hamelmann E, Terada N, et al. (1999)Mitogen-activated protein kinase activation through Fce receptor I and stem cell factor receptor id differentially regulated by phosphatidylinositol 3-kinase and calcineurin inmouse bone marrow-derived mast cells. J. Immunol. 162: 2087-2094.
    • (1999) J. Immunol. , vol.162 , pp. 2087-2094
    • Ishizuka, T.1    Chayama, K.2    Takeda, K.3    Hamelmann, E.4    Terada, N.5
  • 8
    • 33745186215 scopus 로고    scopus 로고
    • Chlamydia trachomatis-derived deubiquitinating enzymes in mammalian cells during infection
    • Misaghi S, Balsara ZR, Catic A, Spooner E, Ploegh HL, et al. (2006) Chlamydia trachomatis-derived deubiquitinating enzymes in mammalian cells during infection. Mol. Microbiol. 61: 142-150.
    • (2006) Mol. Microbiol. , vol.61 , pp. 142-150
    • Misaghi, S.1    Balsara, Z.R.2    Catic, A.3    Spooner, E.4    Ploegh, H.L.5
  • 9
    • 23744434659 scopus 로고    scopus 로고
    • A deubiquitinating enzyme encoded by HSV-1 belongs to a family of cysteine proteases that is conserved across the family Herpesviridae
    • Kattenhorn LM, Korbel GA, Kessler BM, Spooner E, Ploegh HL (2005) A deubiquitinating enzyme encoded by HSV-1 belongs to a family of cysteine proteases that is conserved across the family Herpesviridae. Mol. Cell. 19: 547-557.
    • (2005) Mol. Cell. , vol.19 , pp. 547-557
    • Kattenhorn, L.M.1    Korbel, G.A.2    Kessler, B.M.3    Spooner, E.4    Ploegh, H.L.5
  • 10
    • 33846574355 scopus 로고    scopus 로고
    • Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems
    • Angot A, Vergunst A, Genin S, Peeters N (2007) Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems. PLoS Pathog. 3: e3.
    • (2007) PLoS Pathog. , vol.3
    • Angot, A.1    Vergunst, A.2    Genin, S.3    Peeters, N.4
  • 11
    • 29344475754 scopus 로고    scopus 로고
    • Vialinin A, a novel 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenger from an edible mushroom in China
    • Xie C, Koshino H, Esumi Y, Takahashi S, Yoshikawa K, et al. (2005) Vialinin A, a novel 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenger from an edible mushroom in China. Biosci. Biotechnol. Biochem. 69: 2326-2332.
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 2326-2332
    • Xie, C.1    Koshino, H.2    Esumi, Y.3    Takahashi, S.4    Yoshikawa, K.5
  • 12
    • 44349186775 scopus 로고    scopus 로고
    • Vialinin A, a novel potent inhibitor of TNF-α production from RBL-2H3 cells
    • Onose J, Xie C, Ye YQ, Sugaya K, Takahashi S, et al. (2008) Vialinin A, a novel potent inhibitor of TNF-α production from RBL-2H3 cells. Biol. Pharm. Bull. 31: 831-833.
    • (2008) Biol. Pharm. Bull. , vol.31 , pp. 831-833
    • Onose, J.1    Xie, C.2    Ye, Y.Q.3    Sugaya, K.4    Takahashi, S.5
  • 13
    • 84870870047 scopus 로고    scopus 로고
    • Inhibitory effects of vialinin A and its analog on tumor necrosis factor-α release and production from RBL-2H3 cells
    • Onose J, Yoshioka Y, Ye YQ, Sugaya K, Yajima A, et al. (2012) Inhibitory effects of vialinin A and its analog on tumor necrosis factor-α release and production from RBL-2H3 cells. Cell. Immunol. 279: 140-144.
    • (2012) Cell. Immunol. , vol.279 , pp. 140-144
    • Onose, J.1    Yoshioka, Y.2    Ye, Y.Q.3    Sugaya, K.4    Yajima, A.5
  • 14
    • 4444335573 scopus 로고    scopus 로고
    • Antiallergic activity of stilbenes from Korean rhubarb (Rheum undulatum L.): Structure requirements for inhibition of antigen-induced degranulation and their effects on the release of TNF-α and IL-4 in RBL-2H3 cells
    • Matsuda H, Tewtrakul S, Morikawa T, Yoshikawa M (2004) Antiallergic activity of stilbenes from Korean rhubarb (Rheum undulatum L.): structure requirements for inhibition of antigen-induced degranulation and their effects on the release of TNF-α and IL-4 in RBL-2H3 cells. Bioorg. Med. Chem. 12: 4871-4876.
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 4871-4876
    • Matsuda, H.1    Tewtrakul, S.2    Morikawa, T.3    Yoshikawa, M.4
  • 16
    • 0019460298 scopus 로고
    • IgE-induced histamine release from rat basophilic leukemia cell line: Isolation of releasing and non-releasing clones
    • Barusumian EL, Iserskey C, Petrino MG, Siraganian RP (1981) IgE-induced histamine release from rat basophilic leukemia cell line: isolation of releasing and non-releasing clones. Eur. J. Immunol. 11: 317-323
    • (1981) Eur. J. Immunol. , vol.11 , pp. 317-323
    • Barusumian, E.L.1    Iserskey, C.2    Petrino, M.G.3    Siraganian, R.P.4
  • 17
    • 0037197914 scopus 로고    scopus 로고
    • RNA interference by expression of short-interfering RNAs and hairpin RNAs in mammalian cells
    • Yu JY, DeRuiter SL, Turner DL (2002) RNA interference by expression of short-interfering RNAs and hairpin RNAs in mammalian cells. Proc. Natl. Acad. Sci. U. S. A. 99: 6047-6052.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 6047-6052
    • Yu, J.Y.1    DeRuiter, S.L.2    Turner, D.L.3
  • 18
    • 55949089929 scopus 로고    scopus 로고
    • Lipofectamine RNAiMAX: An efficient siRNA transfection reagent in human embryonic stem cells
    • Zhao M, Yang H, Jiang X, Zhou W, Zhu B (2008) Lipofectamine RNAiMAX: an efficient siRNA transfection reagent in human embryonic stem cells/Mol. Biotechnol. 40: 19-26.
    • (2008) Mol. Biotechnol. , vol.40 , pp. 19-26
    • Zhao, M.1    Yang, H.2    Jiang, X.3    Zhou, W.4    Zhu, B.5
  • 19
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa ME, Bennett EJ, Gygi SP, Harper JW (2009) Defining the human deubiquitinating enzyme interaction landscape. Cell 138: 389-403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 20
    • 79961002252 scopus 로고    scopus 로고
    • USP13 enzyme regulates Siah2 ligase stability and activity via non catalytic ubiquitin- binding domains
    • Scortegagna M, Subtil T, Qi J, Kim H, Zhao W, et al. (2011) USP13 enzyme regulates Siah2 ligase stability and activity via non catalytic ubiquitin- binding domains. J. Biol. Chem. 286: 27333-27341.
    • (2011) J. Biol. Chem. , vol.286 , pp. 27333-27341
    • Scortegagna, M.1    Subtil, T.2    Qi, J.3    Kim, H.4    Zhao, W.5
  • 22
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signalling in the NF-κB pathway
    • Chen ZJ (2005) Ubiquitin signalling in the NF-κB pathway. Nat. Cell Biol. 7: 758-765.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 758-765
    • Chen, Z.J.1
  • 23
    • 33646066025 scopus 로고    scopus 로고
    • The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin
    • Reyes-Turcu FE, Horton JR, Mullally JE, Heroux A, Cheng X, et al. (2006) The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin. Cell 124: 1197-1208.
    • (2006) Cell , vol.124 , pp. 1197-1208
    • Reyes-Turcu, F.E.1    Horton, J.R.2    Mullally, J.E.3    Heroux, A.4    Cheng, X.5
  • 24
    • 50349102579 scopus 로고    scopus 로고
    • Recognition of polyubiquitin isoforms by the multiple ubiquitin binding modules of isopeptidase T
    • Reyes-Turcu FE, Shanks JR, Komander D, Wilkinson KD (2008) Recognition of polyubiquitin isoforms by the multiple ubiquitin binding modules of isopeptidase T. J. Biol. Chem. 283: 19581-19592.
    • (2008) J. Biol. Chem. , vol.283 , pp. 19581-19592
    • Reyes-Turcu, F.E.1    Shanks, J.R.2    Komander, D.3    Wilkinson, K.D.4
  • 25
    • 0030746105 scopus 로고    scopus 로고
    • In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome
    • Amerik AY, Swaminathan S, Krantz BA, Wilkinson KD, Hochstrasser M (1997) In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome. EMBO J. 16: 4826-4838.
    • (1997) EMBO J. , vol.16 , pp. 4826-4838
    • Amerik, A.Y.1    Swaminathan, S.2    Krantz, B.A.3    Wilkinson, K.D.4    Hochstrasser, M.5
  • 26
    • 64149087218 scopus 로고    scopus 로고
    • Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53
    • Dayal S, Sparks A, Jacob J, Allende-Vega N, Lane DP, et al. (2009) Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53. J. Biol. Chem. 284: 5030-5041.
    • (2009) J. Biol. Chem. , vol.284 , pp. 5030-5041
    • Dayal, S.1    Sparks, A.2    Jacob, J.3    Allende-Vega, N.4    Lane, D.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.