메뉴 건너뛰기




Volumn 288, Issue 11, 2013, Pages 7697-7703

Soluble epoxide hydrolase dimerization is required for hydrolase activity

Author keywords

[No Author keywords available]

Indexed keywords

CARDIO-VASCULAR DISEASE; ENZYMATIC ACTIVITIES; EPOXIDE HYDROLASES; HYDROLASE ACTIVITIES; METABOLIC CONVERSION; SUBSTRATE CONVERSION; THERAPEUTIC STRATEGY; THERAPEUTIC TARGETS;

EID: 84875180857     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.429258     Document Type: Article
Times cited : (27)

References (20)
  • 1
    • 0037452577 scopus 로고    scopus 로고
    • The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity
    • Newman, J. W., Morisseau, C., Harris, T. R., and Hammock, B. D. (2003) The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity. Proc. Natl. Acad. Sci. U.S.A. 100, 1558-1563
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 1558-1563
    • Newman, J.W.1    Morisseau, C.2    Harris, T.R.3    Hammock, B.D.4
  • 3
    • 67149084404 scopus 로고    scopus 로고
    • Soluble epoxide hydrolase inhibition: Targeting multiple mechanisms of ischemic brain injury with a single agent
    • Iliff, J. J., and Alkayed, N. J. (2009) Soluble epoxide hydrolase inhibition: targeting multiple mechanisms of ischemic brain injury with a single agent. Future Neurol. 4, 179-199
    • (2009) Future Neurol. , vol.4 , pp. 179-199
    • Iliff, J.J.1    Alkayed, N.J.2
  • 7
    • 0032849109 scopus 로고    scopus 로고
    • Detoxification of environmental mutagens and carcinogens: Structure, mechanism, and evolution of liver epoxide hydrolase
    • Argiriadi, M. A., Morisseau, C., Hammock, B. D., and Christianson, D. W. (1999) Detoxification of environmental mutagens and carcinogens: structure, mechanism, and evolution of liver epoxide hydrolase. Proc. Natl. Acad. Sci. U.S.A. 96, 10637-10642
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 10637-10642
    • Argiriadi, M.A.1    Morisseau, C.2    Hammock, B.D.3    Christianson, D.W.4
  • 8
    • 2942579253 scopus 로고    scopus 로고
    • Polymorphisms in human soluble epoxide hydrolase: Effects on enzyme activity, enzyme stability, and quaternary structure
    • Srivastava, P. K., Sharma, V. K., Kalonia, D. S., and Grant, D. F. (2004) Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure. Arch. Biochem. Biophys. 427, 164-169
    • (2004) Arch. Biochem. Biophys. , vol.427 , pp. 164-169
    • Srivastava, P.K.1    Sharma, V.K.2    Kalonia, D.S.3    Grant, D.F.4
  • 9
    • 22144444583 scopus 로고    scopus 로고
    • Fluorescent substrates for soluble epoxide hydrolase and application to inhibition studies
    • Jones, P. D., Wolf, N. M., Morisseau, C., Whetstone, P., Hock, B., and Hammock, B. D. (2005) Fluorescent substrates for soluble epoxide hydrolase and application to inhibition studies. Anal. Biochem. 343, 66-75
    • (2005) Anal. Biochem. , vol.343 , pp. 66-75
    • Jones, P.D.1    Wolf, N.M.2    Morisseau, C.3    Whetstone, P.4    Hock, B.5    Hammock, B.D.6
  • 10
    • 77954219912 scopus 로고    scopus 로고
    • Split Renilla luciferase protein fragmentassisted complementation (SRL-PFAC) to characterize Hsp90-Cdc37 complex and identify critical residues in protein/protein interactions
    • Jiang, Y., Bernard, D., Yu, Y., Xie, Y., Zhang, T., Li, Y., Burnett, J. P., Fu, X., Wang, S., and Sun, D. (2010) Split Renilla luciferase protein fragmentassisted complementation (SRL-PFAC) to characterize Hsp90-Cdc37 complex and identify critical residues in protein/protein interactions. J. Biol. Chem. 285, 21023-21036
    • (2010) J. Biol. Chem. , vol.285 , pp. 21023-21036
    • Jiang, Y.1    Bernard, D.2    Yu, Y.3    Xie, Y.4    Zhang, T.5    Li, Y.6    Burnett, J.P.7    Fu, X.8    Wang, S.9    Sun, D.10
  • 11
    • 4344656346 scopus 로고    scopus 로고
    • Kinetics of regulated proteinprotein interactions revealed with firefly luciferase complementation imaging in cells and living animals
    • Luker, K. E., Smith, M. C. P., Luker, G. D., Gammon, S. T., Piwnica-Worms, H., and Piwnica-Worms, D. (2004) Kinetics of regulated proteinprotein interactions revealed with firefly luciferase complementation imaging in cells and living animals. Proc. Natl. Acad. Sci. U.S.A. 101, 12288-12293
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12288-12293
    • Luker, K.E.1    Smith, M.C.P.2    Luker, G.D.3    Gammon, S.T.4    Piwnica-Worms, H.5    Piwnica-Worms, D.6
  • 14
    • 38549145416 scopus 로고    scopus 로고
    • Genetic variation in cytochrome P450 2J2 and soluble epoxide hydrolase and risk of ischemic stroke in a Chinese population
    • Zhang, L., Ding, H., Yan, J., Hui, R., Wang, W., Kissling, G. E., Zeldin, D. C., and Wang, D. W. (2008) Genetic variation in cytochrome P450 2J2 and soluble epoxide hydrolase and risk of ischemic stroke in a Chinese population. Pharmacogenet. Genomics 18, 45-51
    • (2008) Pharmacogenet. Genomics , vol.18 , pp. 45-51
    • Zhang, L.1    Ding, H.2    Yan, J.3    Hui, R.4    Wang, W.5    Kissling, G.E.6    Zeldin, D.C.7    Wang, D.W.8
  • 15
    • 78650810635 scopus 로고    scopus 로고
    • Genetic variation in soluble epoxide hydrolase (EPHX2) is associated with forearm vasodilator responses in humans
    • Lee, C. R., Pretorius, M., Schuck, R. N., Burch, L. H., Bartlett, J., Williams, S. M., Zeldin, D. C., and Brown N. J. (2011) Genetic variation in soluble epoxide hydrolase (EPHX2) is associated with forearm vasodilator responses in humans. Hypertension 57, 116-122
    • (2011) Hypertension , vol.57 , pp. 116-122
    • Lee, C.R.1    Pretorius, M.2    Schuck, R.N.3    Burch, L.H.4    Bartlett, J.5    Williams, S.M.6    Zeldin, D.C.7    Brown, N.J.8
  • 16
    • 0036708467 scopus 로고    scopus 로고
    • Relationship between ion pair geometries and electrostatic strengths in proteins
    • Kumar, S., and Nussinov, R. (2002) Relationship between ion pair geometries and electrostatic strengths in proteins. Biophys. J. 83, 1595-1612
    • (2002) Biophys. J. , vol.83 , pp. 1595-1612
    • Kumar, S.1    Nussinov, R.2
  • 17
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu, C. D., Chinenov, Y., and Kerppola, T. K. (2002) Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9, 789-798
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 18
    • 77955836287 scopus 로고    scopus 로고
    • A coiled-coil enabled split-luciferase three-hybrid system: Applied toward profiling inhibitors of protein kinases
    • Jester, B. W., Cox, K. J., Gaj, A., Shomin, C. D., Porter, J. R., and Ghosh, I. (2010) A coiled-coil enabled split-luciferase three-hybrid system: applied toward profiling inhibitors of protein kinases. J. Am. Chem. Soc. 132, 11727-11735
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 11727-11735
    • Jester, B.W.1    Cox, K.J.2    Gaj, A.3    Shomin, C.D.4    Porter, J.R.5    Ghosh, I.6
  • 19
    • 70450224038 scopus 로고    scopus 로고
    • ESBRI: A web server for evaluating salt bridges in proteins
    • Costantini, S., Colonna, G., and Facchiano, A. M. (2008) ESBRI: a web server for evaluating salt bridges in proteins. Bioinformation 3, 137-138
    • (2008) Bioinformation , vol.3 , pp. 137-138
    • Costantini, S.1    Colonna, G.2    Facchiano, A.M.3
  • 20
    • 70349636047 scopus 로고    scopus 로고
    • Soluble epoxide hydrolase as a therapeutic target for cardiovascular diseases
    • Imig, J. D., and Hammock, B. D. (2009) Soluble epoxide hydrolase as a therapeutic target for cardiovascular diseases. Nat. Rev. Drug Discov. 8, 794-805
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 794-805
    • Imig, J.D.1    Hammock, B.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.