메뉴 건너뛰기




Volumn 10, Issue 2, 2013, Pages 147-154

IGLuc: A luciferase-based inflammasome and protease activity reporter

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; INFLAMMASOME; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; LUCIFERASE; MONOMER; PRO INTERLEUKIN 1BETA GAUSSIA LUCIFERASE FUSION PROTEIN; PROTEIN PRECURSOR; PROTEINASE; UNCLASSIFIED DRUG;

EID: 84873408537     PISSN: 15487091     EISSN: 15487105     Source Type: Journal    
DOI: 10.1038/nmeth.2327     Document Type: Article
Times cited : (64)

References (23)
  • 2
    • 79951578449 scopus 로고    scopus 로고
    • Infammasomes: Current understanding and open questions
    • Bauernfeind, F. et al. Infammasomes: current understanding and open questions. Cell. Mol. Life Sci. 68, 765-783 (2011).
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 765-783
    • Bauernfeind, F.1
  • 3
    • 62649139025 scopus 로고    scopus 로고
    • Immunological and infammatory functions of the interleukin-1 family
    • Dinarello, C.A. Immunological and infammatory functions of the interleukin-1 family. Annu. Rev. Immunol. 27, 519-550 (2009).
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 519-550
    • Dinarello, C.A.1
  • 4
    • 0035179970 scopus 로고    scopus 로고
    • Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinfammatory syndrome and Muckle-Wells syndrome
    • Hoffman, H.M., Mueller, J.L., Broide, D.H., Wanderer, A.A. & Kolodner, R.D. Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinfammatory syndrome and Muckle-Wells syndrome. Nat. Genet. 29, 301-305 (2001).
    • (2001) Nat. Genet. , vol.29 , pp. 301-305
    • Hoffman, H.M.1    Mueller, J.L.2    Broide, D.H.3    Wanderer, A.A.4    Kolodner, R.D.5
  • 5
    • 67650736238 scopus 로고    scopus 로고
    • Horror autoinfammaticus: The molecular pathophysiology of autoinfammatory disease
    • Masters, S.L., Simon, A., Aksentijevich, I. & Kastner, D.L. Horror autoinfammaticus: the molecular pathophysiology of autoinfammatory disease. Annu. Rev. Immunol. 27, 621-668 (2009).
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 621-668
    • Masters, S.L.1    Simon, A.2    Aksentijevich, I.3    Kastner, D.L.4
  • 6
    • 32944468985 scopus 로고    scopus 로고
    • Gout-associated uric acid crystals activate the NALP3 infammasome
    • Martinon, F., Petrilli, V., Mayor, A., Tardivel, A. & Tschopp, J. Gout-associated uric acid crystals activate the NALP3 infammasome. Nature 440, 237-241 (2006).
    • (2006) Nature , vol.440 , pp. 237-241
    • Martinon, F.1    Petrilli, V.2    Mayor, A.3    Tardivel, A.4    Tschopp, J.5
  • 7
    • 77951800951 scopus 로고    scopus 로고
    • NLRP3 infammasomes are required for atherogenesis and activated by cholesterol crystals
    • Duewell, P. et al. NLRP3 infammasomes are required for atherogenesis and activated by cholesterol crystals. Nature 464, 1357-1361 (2010).
    • (2010) Nature , vol.464 , pp. 1357-1361
    • Duewell, P.1
  • 8
    • 77956958947 scopus 로고    scopus 로고
    • Activation of the NLRP3 infammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes
    • Masters, S.L. et al. Activation of the NLRP3 infammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes. Nat. Immunol. 11, 897-904 (2010).
    • (2010) Nat. Immunol. , vol.11 , pp. 897-904
    • Masters, S.L.1
  • 9
    • 47849085872 scopus 로고    scopus 로고
    • The NALP3 infammasome is involved in the innate immune response to amyloid-β
    • Halle, A. et al. The NALP3 infammasome is involved in the innate immune response to amyloid-β. Nat. Immunol. 9, 857-865 (2008).
    • (2008) Nat. Immunol. , vol.9 , pp. 857-865
    • Halle, A.1
  • 10
    • 79960542894 scopus 로고    scopus 로고
    • Cutting edge: Reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 infammasome
    • Bauernfeind, F. et al. Cutting edge: reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 infammasome. J. Immunol. 187, 613-617 (2011).
    • (2011) J. Immunol. , vol.187 , pp. 613-617
    • Bauernfeind, F.1
  • 11
    • 70249138036 scopus 로고    scopus 로고
    • Cutting edge: NF-κB activating pattern recognition and cytokine receptors license NLRP3 infammasome activation by regulating NLRP3 expression
    • Bauernfeind, F.G. et al. Cutting edge: NF-κB activating pattern recognition and cytokine receptors license NLRP3 infammasome activation by regulating NLRP3 expression. J. Immunol. 183, 787-791 (2009).
    • (2009) J. Immunol. , vol.183 , pp. 787-791
    • Bauernfeind, F.G.1
  • 12
    • 70249110860 scopus 로고    scopus 로고
    • Cutting edge: TNF-α mediates sensitization to ATP and silica via the NLRP3 infammasome in the absence of microbial stimulation
    • Franchi, L., Eigenbrod, T. & Nunez, G. Cutting edge: TNF-α mediates sensitization to ATP and silica via the NLRP3 infammasome in the absence of microbial stimulation. J. Immunol. 183, 792-796 (2009).
    • (2009) J. Immunol. , vol.183 , pp. 792-796
    • Franchi, L.1    Eigenbrod, T.2    Nunez, G.3
  • 13
    • 18344385660 scopus 로고    scopus 로고
    • New mutations of CIAS1 that are responsible for Muckle-Wells syndrome and familial cold urticaria: A novel mutation underlies both syndromes
    • Dodé, C. et al. New mutations of CIAS1 that are responsible for Muckle-Wells syndrome and familial cold urticaria: a novel mutation underlies both syndromes. Am. J. Hum. Genet. 70, 1498-1506 (2002).
    • (2002) Am. J. Hum. Genet. , vol.70 , pp. 1498-1506
    • Dodé, C.1
  • 14
    • 77953305895 scopus 로고    scopus 로고
    • Listeria monocytogenes is sensed by the NLRP3 and AIM2 infammasome
    • Kim, S. et al. Listeria monocytogenes is sensed by the NLRP3 and AIM2 infammasome. Eur. J. Immunol. 40, 1545-1551 (2010).
    • (2010) Eur. J. Immunol. , vol.40 , pp. 1545-1551
    • Kim, S.1
  • 15
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE
    • Lazebnik, Y.A., Kaufmann, S.H., Desnoyers, S., Poirier, G.G. & Earnshaw, W.C. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature 371, 346-347 (1994).
    • (1994) Nature , vol.371 , pp. 346-347
    • Lazebnik, Y.A.1    Kaufmann, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5
  • 16
    • 0032891964 scopus 로고    scopus 로고
    • Purifcation and catalytic properties of human caspase family members
    • Garcia-Calvo, M. et al. Purifcation and catalytic properties of human caspase family members. Cell Death Differ. 6, 362-369 (1999).
    • (1999) Cell Death Differ. , vol.6 , pp. 362-369
    • Garcia-Calvo, M.1
  • 17
    • 53149145649 scopus 로고    scopus 로고
    • Two forms of secreted and thermostable luciferases from the marine copepod crustacean, Metridia pacifca
    • Takenaka, Y. et al. Two forms of secreted and thermostable luciferases from the marine copepod crustacean, Metridia pacifca. Gene 425, 28-35 (2008).
    • (2008) Gene , vol.425 , pp. 28-35
    • Takenaka, Y.1
  • 18
    • 63649133278 scopus 로고    scopus 로고
    • AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating infammasome with ASC
    • Hornung, V. et al. AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating infammasome with ASC. Nature 458, 514-518 (2009).
    • (2009) Nature , vol.458 , pp. 514-518
    • Hornung, V.1
  • 19
    • 0033150406 scopus 로고    scopus 로고
    • Novel mutant green fuorescent protein protease substrates reveal the activation of specifc caspases during apoptosis
    • Mahajan, N.P., Harrison-Shostak, D.C., Michaux, J. & Herman, B. Novel mutant green fuorescent protein protease substrates reveal the activation of specifc caspases during apoptosis. Chem. Biol. 6, 401-409 (1999).
    • (1999) Chem. Biol. , vol.6 , pp. 401-409
    • Mahajan, N.P.1    Harrison-Shostak, D.C.2    Michaux, J.3    Herman, B.4
  • 20
    • 48049089845 scopus 로고    scopus 로고
    • Novel genetically encoded biosensors using frefy luciferase
    • Fan, F. et al. Novel genetically encoded biosensors using frefy luciferase. ACS Chem. Biol. 3, 346-351 (2008).
    • (2008) ACS Chem. Biol. , vol.3 , pp. 346-351
    • Fan, F.1
  • 21
    • 70449378957 scopus 로고    scopus 로고
    • Caspase substrates: Easily caught in deep waters?
    • Demon, D. et al. Caspase substrates: easily caught in deep waters? Trends Biotechnol. 27, 680-688 (2009).
    • (2009) Trends Biotechnol. , vol.27 , pp. 680-688
    • Demon, D.1
  • 23
    • 64749107970 scopus 로고    scopus 로고
    • Concentration and titration of pseudotyped HIV-1-based lentiviral vectors
    • Kutner, R.H., Zhang, X.Y. & Reiser, J. Production, concentration and titration of pseudotyped HIV-1-based lentiviral vectors. Nat. Protoc. 4, 495-505 (2009).
    • (2009) Nat. Protoc. , vol.4 , pp. 495-505
    • Kutner, R.H.1    Zhang, X.Y.2    Production, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.