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Volumn 349, Issue 1, 2006, Pages 96-102

A fluorescence-based assay for indoleamine 2,3-dioxygenase

Author keywords

Fluorescence assay; Inhibitors; Kynurenine; Recombinant human indoleamine 2,3 dioxygenase

Indexed keywords

AMINO ACIDS; CORROSION INHIBITORS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY;

EID: 31144434857     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2005.10.039     Document Type: Article
Times cited : (41)

References (33)
  • 1
    • 0029497024 scopus 로고
    • Chemistry and neurochemistry of the kynurenine pathway of tryptophan metabolism
    • N.P. Botting Chemistry and neurochemistry of the kynurenine pathway of tryptophan metabolism Chem. Soc. Rev. 24 1995 401 412
    • (1995) Chem. Soc. Rev. , vol.24 , pp. 401-412
    • Botting, N.P.1
  • 2
    • 0742323784 scopus 로고    scopus 로고
    • The kynurenine pathway of tryptophan degradation as a drug target
    • R. Schwarcz The kynurenine pathway of tryptophan degradation as a drug target Curr. Opin. Pharmacol. 4 2004 12 17
    • (2004) Curr. Opin. Pharmacol. , vol.4 , pp. 12-17
    • Schwarcz, R.1
  • 3
    • 0005780874 scopus 로고
    • Indoleamine 2,3-dioxygenase: Properties and functions of a superoxide utilizing enzyme
    • O. Hayaishi, O. Takikawa, and R. Yoshida Indoleamine 2,3-dioxygenase: properties and functions of a superoxide utilizing enzyme Prog. Inorg. Chem. Bioinorg. Chem. 38 1990 75 95
    • (1990) Prog. Inorg. Chem. Bioinorg. Chem. , vol.38 , pp. 75-95
    • Hayaishi, O.1    Takikawa, O.2    Yoshida, R.3
  • 4
    • 0034652442 scopus 로고    scopus 로고
    • Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway
    • Y. Dang, W.E. Dale, and O.R. Brown Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway Free Radical Biol. Med. 28 2000 615 624
    • (2000) Free Radical Biol. Med. , vol.28 , pp. 615-624
    • Dang, Y.1    Dale, W.E.2    Brown, O.R.3
  • 5
    • 0035870927 scopus 로고    scopus 로고
    • Expression of indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase in early concepti
    • S. Suzuki, S. Tone, O. Takikawa, T. Kubos, I. Kohno, and Y. Minatogawa Expression of indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase in early concepti Biochem. J. 355 2001 425 429
    • (2001) Biochem. J. , vol.355 , pp. 425-429
    • Suzuki, S.1    Tone, S.2    Takikawa, O.3    Kubos, T.4    Kohno, I.5    Minatogawa, Y.6
  • 7
    • 0035123904 scopus 로고    scopus 로고
    • Kynurenine in the CNS: From endogenous obscurity to theraputic importance
    • W.T. Stone Kynurenine in the CNS: from endogenous obscurity to theraputic importance Prog. Neurobiol. 64 2001 185 218
    • (2001) Prog. Neurobiol. , vol.64 , pp. 185-218
    • Stone, W.T.1
  • 8
    • 0036690151 scopus 로고    scopus 로고
    • Endogenous kynurenines as targets for drug discovery and development
    • W.T. Stone, and L.G. Darlington Endogenous kynurenines as targets for drug discovery and development Nat. Rev. 1 2002 609 620
    • (2002) Nat. Rev. , vol.1 , pp. 609-620
    • Stone, W.T.1    Darlington, L.G.2
  • 10
    • 0037136266 scopus 로고    scopus 로고
    • Inhibition of allogeneic T cell proliferation by indoleamine 2,3-dioxygenase expressing dendritic cells: Mediation of suppression by tryptophan metabolites
    • P. Terness, T.M. Bauer, L. Rose, C. Duffer, A. Watzlik, H. Simon, and G. Opelz Inhibition of allogeneic T cell proliferation by indoleamine 2,3-dioxygenase expressing dendritic cells: Mediation of suppression by tryptophan metabolites J. Exp. Med. 196 2002 447 457
    • (2002) J. Exp. Med. , vol.196 , pp. 447-457
    • Terness, P.1    Bauer, T.M.2    Rose, L.3    Duffer, C.4    Watzlik, A.5    Simon, H.6    Opelz, G.7
  • 11
    • 0029041430 scopus 로고
    • Involvement of two regulatory elements in interferon gamma regulated expression of human indoleamine 2,3-dioxygenase gene
    • S.Y. Chon, H.H. Hassanain, R. Pine, and S.L. Gupta Involvement of two regulatory elements in interferon gamma regulated expression of human indoleamine 2,3-dioxygenase gene J. Interf. Cytok. Res. 15 1995 517 526
    • (1995) J. Interf. Cytok. Res. , vol.15 , pp. 517-526
    • Chon, S.Y.1    Hassanain, H.H.2    Pine, R.3    Gupta, S.L.4
  • 12
    • 0025990701 scopus 로고
    • Interferon type I and II antagonism: A novel regulatory mechanism of indoleamine 2,3-dioxygenase induction in human peripheral blood monocytes and pertitoneal macrophages
    • Y. Ozaki, E.C. Borden, R.V. Smalley, and R.R. Brown Interferon type I and II antagonism: a novel regulatory mechanism of indoleamine 2,3-dioxygenase induction in human peripheral blood monocytes and pertitoneal macrophages Adv. Exp. Med. Biol. 294 1991 547 553
    • (1991) Adv. Exp. Med. Biol. , vol.294 , pp. 547-553
    • Ozaki, Y.1    Borden, E.C.2    Smalley, R.V.3    Brown, R.R.4
  • 13
    • 0025944659 scopus 로고
    • Relationship between interferon gamma, indoleamine 2,3-dioxygenase, and tryptophan catabolism
    • M.W. Taylor, and G. Feng Relationship between interferon gamma, indoleamine 2,3-dioxygenase, and tryptophan catabolism FASEB J. 5 1991 2516 2522
    • (1991) FASEB J. , vol.5 , pp. 2516-2522
    • Taylor, M.W.1    Feng, G.2
  • 15
    • 0033915899 scopus 로고    scopus 로고
    • Tissue distribution of indoleamine 2,3-dioxygenase in normal and malaria-infected tissue
    • A.M. Hansen, C. Driussi, V. Turner, O. Takikawa, and N.H. Hunt Tissue distribution of indoleamine 2,3-dioxygenase in normal and malaria-infected tissue Redox Rep. 5 2000 112 115
    • (2000) Redox Rep. , vol.5 , pp. 112-115
    • Hansen, A.M.1    Driussi, C.2    Turner, V.3    Takikawa, O.4    Hunt, N.H.5
  • 16
    • 7944224888 scopus 로고    scopus 로고
    • Increased expression of indoleamine 2,3-dioxygenase in murine malaria infection is predominantly localised to the vascular endothelium
    • A.M. Hansen, H.J. Ball, A.J. Mitchell, J. Miu, O. Takikawa, and N.H. Hunt Increased expression of indoleamine 2,3-dioxygenase in murine malaria infection is predominantly localised to the vascular endothelium Int. J. Parasitol. 34 2004 1309 1319
    • (2004) Int. J. Parasitol. , vol.34 , pp. 1309-1319
    • Hansen, A.M.1    Ball, H.J.2    Mitchell, A.J.3    Miu, J.4    Takikawa, O.5    Hunt, N.H.6
  • 17
    • 0034774242 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase in the human lens, the first enzyme in the synthesis of uv filters
    • O. Takikawa, T.K. Littlejohn, and R.J.W. Truscott Indoleamine 2,3-dioxygenase in the human lens, the first enzyme in the synthesis of uv filters Exp. Eye Res. 72 2001 271 277
    • (2001) Exp. Eye Res. , vol.72 , pp. 271-277
    • Takikawa, O.1    Littlejohn, T.K.2    Truscott, R.J.W.3
  • 18
    • 0033998033 scopus 로고    scopus 로고
    • Induction of indoleamine 2,3-dioxygenase in primary human macrophages by human immunodeficiency virus type 1 is strain dependent
    • R. Grant, H. Naif, S.J. Thuruthyil, N. Nasr, T.K. Littlejohn, O. Takikawa, and V. Kapoor Induction of indoleamine 2,3-dioxygenase in primary human macrophages by human immunodeficiency virus type 1 is strain dependent J. Virol. 74 2000 4110 4115
    • (2000) J. Virol. , vol.74 , pp. 4110-4115
    • Grant, R.1    Naif, H.2    Thuruthyil, S.J.3    Nasr, N.4    Littlejohn, T.K.5    Takikawa, O.6    Kapoor, V.7
  • 20
    • 2342507918 scopus 로고    scopus 로고
    • A beta1-42 induces production of quinolinic acid by human macrophages and microglia
    • G.J. Guillemin, G.A. Smythe, L.A. Veas, O. Takikawa, and B.J. Brew A beta1-42 induces production of quinolinic acid by human macrophages and microglia NeuroReport 14 2003 2311 2315
    • (2003) NeuroReport , vol.14 , pp. 2311-2315
    • Guillemin, G.J.1    Smythe, G.A.2    Veas, L.A.3    Takikawa, O.4    Brew, B.J.5
  • 22
    • 0345310615 scopus 로고
    • A facile synthesis of 6-chloro-d-tryptophan
    • T. Moriya, K. Hagio, and N. Yoneda A facile synthesis of 6-chloro-d-tryptophan Bull. Chem. Soc. Jpn. 48 1975 2217 2218
    • (1975) Bull. Chem. Soc. Jpn. , vol.48 , pp. 2217-2218
    • Moriya, T.1    Hagio, K.2    Yoneda, N.3
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0020157737 scopus 로고
    • Fluorescence characteristics of kynurenine and N-formylkynurenine. Their use as reporters of the environment of tryptophan 62 in hen egg-white lysozyme
    • Y. Fukunaga, Y. Katsuragi, T. Izumi, and F. Sakiyama Fluorescence characteristics of kynurenine and N-formylkynurenine. Their use as reporters of the environment of tryptophan 62 in hen egg-white lysozyme J. Biochem. 92 1982 129 141
    • (1982) J. Biochem. , vol.92 , pp. 129-141
    • Fukunaga, Y.1    Katsuragi, Y.2    Izumi, T.3    Sakiyama, F.4
  • 28
    • 0015527725 scopus 로고
    • L-Kynurenine: A fluorescent probe of serum albumins
    • J.E. Churchich l-Kynurenine: a fluorescent probe of serum albumins BioChim. BioPhys. Acta 285 1972 91 98
    • (1972) BioChim. BioPhys. Acta , vol.285 , pp. 91-98
    • Churchich, J.E.1
  • 29
    • 0016791416 scopus 로고
    • Studies on indoleamine 2,3-dioxygenase (Superoxide anions as substrate)
    • F. Hirata, and O. Hayaishi Studies on indoleamine 2,3-dioxygenase (Superoxide anions as substrate) J. Biol. Chem. 250 1975 5960 5966
    • (1975) J. Biol. Chem. , vol.250 , pp. 5960-5966
    • Hirata, F.1    Hayaishi, O.2
  • 30
    • 4243525727 scopus 로고
    • Tryptophan 2,3-dioxygenase (tryptophan pyrrolase) rabbit intestine
    • S. Yamamoto, and O. Hayaishi Tryptophan 2,3-dioxygenase (tryptophan pyrrolase) rabbit intestine Methods Enzymol. A 17 1970 434 438
    • (1970) Methods Enzymol. a , vol.17 , pp. 434-438
    • Yamamoto, S.1    Hayaishi, O.2
  • 31
    • 31144476400 scopus 로고
    • L-Tryptophan 2,3-dioxygenase (tryptophan pyrrolase) (Pseudomonas fluorescens)
    • Y. Ishimura l-Tryptophan 2,3-dioxygenase (tryptophan pyrrolase) (Pseudomonas fluorescens) Methods Enzymol. A 17 1970 429 434
    • (1970) Methods Enzymol. a , vol.17 , pp. 429-434
    • Ishimura, Y.1
  • 33
    • 0042762821 scopus 로고    scopus 로고
    • Inhibition of indoleamine 2,3-dioxygenase activity in interferon gamma stimulated astroglioma cells decreases intracellular NAD levels
    • R. Grant, and V. Kapoor Inhibition of indoleamine 2,3-dioxygenase activity in interferon gamma stimulated astroglioma cells decreases intracellular NAD levels Biochem. Pharmacol. 66 2003 1033 1036
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1033-1036
    • Grant, R.1    Kapoor, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.