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Volumn 579, Issue 14, 2005, Pages 3159-3163

Direct interaction between the reductase domain of endothelial nitric oxide synthase and the ryanodine receptor

Author keywords

Calcium channels; Nitric oxide synthase; Ryanodine receptors

Indexed keywords

ENDOTHELIAL NITRIC OXIDE SYNTHASE; OXIDOREDUCTASE; RYANODINE RECEPTOR;

EID: 20444365874     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.04.078     Document Type: Article
Times cited : (19)

References (17)
  • 1
    • 0037168483 scopus 로고    scopus 로고
    • There's NO binding like NOS binding: Protein-protein interactions in NO/cGMP signaling
    • P.I. Nedvetsky, W.C. Sessa, and H.H.H.W. Schmidt There's NO binding like NOS binding: protein-protein interactions in NO/cGMP signaling Proc. Natl. Acad. Sci. USA 99 2002 16510 16512
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16510-16512
    • Nedvetsky, P.I.1    Sessa, W.C.2    Schmidt, H.H.H.W.3
  • 2
    • 3042730959 scopus 로고    scopus 로고
    • ENOS at a glance
    • W.C. Sessa eNOS at a glance J. Cell Sci. 117 2004 2427 2429
    • (2004) J. Cell Sci. , vol.117 , pp. 2427-2429
    • Sessa, W.C.1
  • 3
    • 0029889353 scopus 로고    scopus 로고
    • Endothelial nitric-oxide synthase. Expression in Escherichia coli, spectroscopic characterization, and role of tetrahydrobiopterin in dimer formation
    • I. Rodriguez-Crespo, N.C. Gerber, and P.R. Ortiz de Montellano Endothelial nitric-oxide synthase. Expression in Escherichia coli, spectroscopic characterization, and role of tetrahydrobiopterin in dimer formation J. Biol. Chem. 271 1996 11462 11467
    • (1996) J. Biol. Chem. , vol.271 , pp. 11462-11467
    • Rodriguez-Crespo, I.1    Gerber, N.C.2    Ortiz De Montellano, P.R.3
  • 4
    • 0039702796 scopus 로고    scopus 로고
    • Mutation of the five conserved histidines in the endothelial nitric-oxide synthase hemoprotein domain. No evidence for a non-heme metal requirement for catalysis
    • I. Rodriguez-Crespo, C.R. Nishida, G.M. Knudsen, and P.R. Ortiz de Montellano Mutation of the five conserved histidines in the endothelial nitric-oxide synthase hemoprotein domain. No evidence for a non-heme metal requirement for catalysis J. Biol. Chem. 274 1999 21617 21624
    • (1999) J. Biol. Chem. , vol.274 , pp. 21617-21624
    • Rodriguez-Crespo, I.1    Nishida, C.R.2    Knudsen, G.M.3    Ortiz De Montellano, P.R.4
  • 6
    • 0036676541 scopus 로고    scopus 로고
    • Distance-dependent cellular palmitoylation of de novo-designed sequences and their translocation to plasma membrane subdomains
    • I. Navarro-Lérida, A. Álvarez-Barrientos, F. Gavilanes, and I. Rodríguez-Crespo Distance-dependent cellular palmitoylation of de novo-designed sequences and their translocation to plasma membrane subdomains J. Cell Sci. 115 2002 3119 3130
    • (2002) J. Cell Sci. , vol.115 , pp. 3119-3130
    • Navarro-Lérida, I.1    Álvarez-Barrientos, A.2    Gavilanes, F.3    Rodríguez-Crespo, I.4
  • 8
    • 0027444278 scopus 로고
    • Anti-ryanodine receptor antibody binding sites in vascular and endocardial endothelium
    • R.E. Lesh, A.R. Marks, A.V. Somlyo, S. Fleischer, and A.P. Somlyo Anti-ryanodine receptor antibody binding sites in vascular and endocardial endothelium Circ. Res. 72 1993 481 488
    • (1993) Circ. Res. , vol.72 , pp. 481-488
    • Lesh, R.E.1    Marks, A.R.2    Somlyo, A.V.3    Fleischer, S.4    Somlyo, A.P.5
  • 11
    • 0035949671 scopus 로고    scopus 로고
    • Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
    • J. Sun, C. Xin, J.P. Eu, J.S. Stamler, and G. Meissner Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO Proc. Natl. Acad. Sci. USA 98 2001 11158 11162
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11158-11162
    • Sun, J.1    Xin, C.2    Eu, J.P.3    Stamler, J.S.4    Meissner, G.5
  • 13
    • 0035844120 scopus 로고    scopus 로고
    • Classes of thiols that influence the activity of the skeletal muscle calcium release channel
    • J.H. Sun, L. Xu, J.P. Eu, J.S. Stamler, and G. Meissner Classes of thiols that influence the activity of the skeletal muscle calcium release channel J. Biol. Chem. 276 2001 15625 15630
    • (2001) J. Biol. Chem. , vol.276 , pp. 15625-15630
    • Sun, J.H.1    Xu, L.2    Eu, J.P.3    Stamler, J.S.4    Meissner, G.5
  • 14
    • 0034680790 scopus 로고    scopus 로고
    • Transmembrane redox sensor of ryanodine receptor complex
    • W. Feng, G. Liu, P.D. Allen, and I.N. Pessah Transmembrane redox sensor of ryanodine receptor complex J. Biol. Chem. 275 2000 35902 35907
    • (2000) J. Biol. Chem. , vol.275 , pp. 35902-35907
    • Feng, W.1    Liu, G.2    Allen, P.D.3    Pessah, I.N.4
  • 15
    • 0034711213 scopus 로고    scopus 로고
    • Skeletal muscle ryanodine receptor is a redox sensor with a well defined redox potential that is sensitive to channel modulators
    • R. Xia, T. Stangler, and J.J. Abramson Skeletal muscle ryanodine receptor is a redox sensor with a well defined redox potential that is sensitive to channel modulators J. Biol. Chem. 275 2000 36556 36561
    • (2000) J. Biol. Chem. , vol.275 , pp. 36556-36561
    • Xia, R.1    Stangler, T.2    Abramson, J.J.3
  • 17
    • 20444409884 scopus 로고    scopus 로고
    • Receptor-regulated dynamic S-nitrosylation of endothelial nitric oxide synthase in vascular endothelial cells
    • P.A. Erwin, A.J. Lin, D.E. Golan, and T. Michel Receptor-regulated dynamic S-nitrosylation of endothelial nitric oxide synthase in vascular endothelial cells J. Biol. Chem. 280 2005 19888 19894
    • (2005) J. Biol. Chem. , vol.280 , pp. 19888-19894
    • Erwin, P.A.1    Lin, A.J.2    Golan, D.E.3    Michel, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.