메뉴 건너뛰기




Volumn 1788, Issue 5, 2009, Pages 983-992

Proline 146 is critical to the structure, function and targeting of sod2, the Na+/H+ exchanger of Schizosaccharomyces pombe

Author keywords

Cation binding; Na+ H+ exchanger; Proline; salt tolerance; Site specific mutagenesis; sod2

Indexed keywords

AMINO ACID; ASPARTIC ACID; LYSINE; MUTANT PROTEIN; PROLINE; PROLINE 146; SERINE; SODIUM ION; SODIUM PROTON EXCHANGE PROTEIN; SODIUM PROTON EXCHANGE PROTEIN SOD2; THREONINE; THREONINE 142; UNCLASSIFIED DRUG;

EID: 65049091742     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.01.001     Document Type: Article
Times cited : (13)

References (37)
  • 2
    • 0034920855 scopus 로고    scopus 로고
    • Role of sodium-hydrogen exchange in cardiac hypertrophy and heart failure: a novel and promising therapeutic target
    • Karmazyn M. Role of sodium-hydrogen exchange in cardiac hypertrophy and heart failure: a novel and promising therapeutic target. Basic Res. Cardiol. 96 (2001) 325-328
    • (2001) Basic Res. Cardiol. , vol.96 , pp. 325-328
    • Karmazyn, M.1
  • 3
    • 0037426418 scopus 로고    scopus 로고
    • Sodium-hydrogen exchange inhibition during ventricular fibrillation: beneficial effects on ischemic contracture, action potential duration, reperfusion arrhythmias, myocardial function, and resuscitability
    • Ayoub I.M., Kolarova J., Yi Z., Trevedi A., Deshmukh H., Lubell D.L., Franz M.R., Maldonado F.A., and Gazmuri R.J. Sodium-hydrogen exchange inhibition during ventricular fibrillation: beneficial effects on ischemic contracture, action potential duration, reperfusion arrhythmias, myocardial function, and resuscitability. Circulation 107 (2003) 1804-1809
    • (2003) Circulation , vol.107 , pp. 1804-1809
    • Ayoub, I.M.1    Kolarova, J.2    Yi, Z.3    Trevedi, A.4    Deshmukh, H.5    Lubell, D.L.6    Franz, M.R.7    Maldonado, F.A.8    Gazmuri, R.J.9
  • 4
    • 0036587141 scopus 로고    scopus 로고
    • Sodium/hydrogen-exchanger inhibition during cardioplegic arrest and cardiopulmonary bypass: an experimental study
    • Cox Jr. C.S., Sauer H., Allen S.J., Buja L.M., and Laine G.A. Sodium/hydrogen-exchanger inhibition during cardioplegic arrest and cardiopulmonary bypass: an experimental study. J. Thorac. Cardiovasc. Surg. 123 (2002) 959-966
    • (2002) J. Thorac. Cardiovasc. Surg. , vol.123 , pp. 959-966
    • Cox Jr., C.S.1    Sauer, H.2    Allen, S.J.3    Buja, L.M.4    Laine, G.A.5
  • 8
    • 33846870761 scopus 로고    scopus 로고
    • Structural and functional analysis of the Na(+)/H(+) exchanger
    • Slepkov E.R., Rainey J.K., Sykes B.D., and Fliegel L. Structural and functional analysis of the Na(+)/H(+) exchanger. Biochem. J. 401 (2007) 623-633
    • (2007) Biochem. J. , vol.401 , pp. 623-633
    • Slepkov, E.R.1    Rainey, J.K.2    Sykes, B.D.3    Fliegel, L.4
  • 16
    • 24044442299 scopus 로고    scopus 로고
    • Mammalian NHE2 Na(+)/H+ exchanger mediates efflux of potassium upon heterologous expression in yeast
    • Flegelova H., and Sychrova H. Mammalian NHE2 Na(+)/H+ exchanger mediates efflux of potassium upon heterologous expression in yeast. FEBS Lett. 579 (2005) 4733-4738
    • (2005) FEBS Lett. , vol.579 , pp. 4733-4738
    • Flegelova, H.1    Sychrova, H.2
  • 17
    • 0030890355 scopus 로고    scopus 로고
    • Identification and localization of the sod2 gene product in fission yeast
    • Dibrov P., Smith J.J., Young P., and Fliegel L. Identification and localization of the sod2 gene product in fission yeast. FEBS Lett. 405 (1997) 119-124
    • (1997) FEBS Lett. , vol.405 , pp. 119-124
    • Dibrov, P.1    Smith, J.J.2    Young, P.3    Fliegel, L.4
  • 22
    • 0002369324 scopus 로고
    • Intrinsic membrane protein structure: principles and predicition
    • Yeagle P. (Ed), CRC Press, Boca Raton 1127p
    • Reithmeier R.A., and Deber C.M. Intrinsic membrane protein structure: principles and predicition. In: Yeagle P. (Ed). The Structure of Biological Membranes (1992), CRC Press, Boca Raton 337-393 1127p
    • (1992) The Structure of Biological Membranes , pp. 337-393
    • Reithmeier, R.A.1    Deber, C.M.2
  • 24
  • 25
    • 14244251697 scopus 로고    scopus 로고
    • + exchanger of Schizosaccharomyces pombe
    • + exchanger of Schizosaccharomyces pombe. Mol. Cell. Biochem. 268 (2005) 83-92
    • (2005) Mol. Cell. Biochem. , vol.268 , pp. 83-92
    • Fliegel, L.1
  • 26
    • 0024278714 scopus 로고
    • Helix geometry in proteins
    • Barlow D.J., and Thornton J.M. Helix geometry in proteins. J. Mol. Biol. 201 (1988) 601-619
    • (1988) J. Mol. Biol. , vol.201 , pp. 601-619
    • Barlow, D.J.1    Thornton, J.M.2
  • 28
    • 34548496285 scopus 로고    scopus 로고
    • Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signal
    • Pagant S., Kung L., Dorrington M., Lee M.C., and Miller E.A. Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signal. Mol. Biol. Cell. 18 (2007) 3398-3413
    • (2007) Mol. Biol. Cell. , vol.18 , pp. 3398-3413
    • Pagant, S.1    Kung, L.2    Dorrington, M.3    Lee, M.C.4    Miller, E.A.5
  • 30
    • 0028568176 scopus 로고
    • TopPredII: an improved software for membrane protein structure predictions
    • Claros M., and von Heijne G. TopPredII: an improved software for membrane protein structure predictions. Comput. Applic. Biosci. 10 (1994) 685-686
    • (1994) Comput. Applic. Biosci. , vol.10 , pp. 685-686
    • Claros, M.1    von Heijne, G.2
  • 32
    • 0024234855 scopus 로고
    • CLUSTAL: a package for performing multiple sequence alignment on a microcomputer
    • Higgins D.G., and Sharp P.M. CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene 73 (1988) 237-244
    • (1988) Gene , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 36
    • 0029020688 scopus 로고
    • +-antiporter gene closely related to the salt-tolerance of yeast Zygosacchromyces rouxii
    • +-antiporter gene closely related to the salt-tolerance of yeast Zygosacchromyces rouxii. Yeast 11 (1995) 829-838
    • (1995) Yeast , vol.11 , pp. 829-838
    • Watanabe, Y.1    Miwa, S.2    Tamai, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.