메뉴 건너뛰기




Volumn 143, Issue 2, 2008, Pages 253-259

Heparin stimulates a plasma membrane Ca2+-ATPase of Arabidopsis thaliana

Author keywords

Arabidopsis thaliana; Ca2+ ATPase; Calmodulin; Heparin; Plasma membrane

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); AGAROSE; CALMODULIN; HEPARIN; MEMBRANE PROTEIN; NUCLEOSIDE TRIPHOSPHATE; PROTEIN ACA8; UNCLASSIFIED DRUG;

EID: 39049152875     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvm218     Document Type: Article
Times cited : (8)

References (34)
  • 3
    • 0034613076 scopus 로고    scopus 로고
    • 2+-ATPase of Arabidopsis thaliana reconstituted in proteoliposomes after calmodulin-affinity purification
    • 2+-ATPase of Arabidopsis thaliana reconstituted in proteoliposomes after calmodulin-affinity purification. FEBS Lett. 482, 225-230
    • (2000) FEBS Lett , vol.482 , pp. 225-230
    • Luoni, L.1    Bonza, M.C.2    De Michelis, M.I.3
  • 4
    • 0034031809 scopus 로고    scopus 로고
    • 2+-ATPase and for the involvement of its activity in the abscisic acid-induced changes in Egeria densa leaves
    • 2+-ATPase and for the involvement of its activity in the abscisic acid-induced changes in Egeria densa leaves. Plant Biol. 2, 168-175
    • (2000) Plant Biol , vol.2 , pp. 168-175
    • Beffagna, N.1    Romani, G.2    Sforza, M.C.3
  • 7
    • 0033841214 scopus 로고    scopus 로고
    • At-ACA8 encodes a plasma membrane-localized Calcium-ATPase of Arabidopsis thaliana with a calmodulin binding domain at the N-terminus
    • Bonza, M.C., Morandini, P., Luoni, L., Geisler, M., Palmgren, M.G., and De Michelis, M.I. (2000) At-ACA8 encodes a plasma membrane-localized Calcium-ATPase of Arabidopsis thaliana with a calmodulin binding domain at the N-terminus. Plant Physiol. 123, 1495-1505
    • (2000) Plant Physiol , vol.123 , pp. 1495-1505
    • Bonza, M.C.1    Morandini, P.2    Luoni, L.3    Geisler, M.4    Palmgren, M.G.5    De Michelis, M.I.6
  • 9
    • 33644864126 scopus 로고    scopus 로고
    • 2+ pump ACA8 contains overlapping as well as physically separated autoinhibitory and calmodulin-binding domains
    • 2+ pump ACA8 contains overlapping as well as physically separated autoinhibitory and calmodulin-binding domains. J. Biol. Chem. 281, 1058-1065
    • (2006) J. Biol. Chem , vol.281 , pp. 1058-1065
    • Bækgaard, L.1    Luoni, L.2    De Michelis, M.I.3    Palmgren, M.G.4
  • 12
    • 0027139498 scopus 로고
    • Controlled proteolysis activates the plasma membrane Ca2+ pump of higher plants
    • Rasi-Caldogno, F., Carnelli, A., and De Michelis, M.I. (1993) Controlled proteolysis activates the plasma membrane Ca2+ pump of higher plants. Plant Physiol. 103, 385-390
    • (1993) Plant Physiol , vol.103 , pp. 385-390
    • Rasi-Caldogno, F.1    Carnelli, A.2    De Michelis, M.I.3
  • 14
    • 0030838196 scopus 로고    scopus 로고
    • Active calcium transporters in isolated membranes of wheat root cells
    • Olbe, M., Widell, S., and Sommarin, M. (1997) Active calcium transporters in isolated membranes of wheat root cells. J. Exp. Bot. 48, 1767-1777
    • (1997) J. Exp. Bot , vol.48 , pp. 1767-1777
    • Olbe, M.1    Widell, S.2    Sommarin, M.3
  • 15
    • 0031847388 scopus 로고    scopus 로고
    • 2+ pump is a 120 kDa polypeptide regulated by calmodulin binding to a terminal region
    • 2+ pump is a 120 kDa polypeptide regulated by calmodulin binding to a terminal region. Physiol. Plant 103, 35-44
    • (1998) Physiol. Plant , vol.103 , pp. 35-44
    • Olbe, M.1    Sommarin, M.2
  • 16
    • 0028113894 scopus 로고
    • Biogenesis: Plasma membrane calcium ATPase: 15 years of work on the purified enzyme
    • Carafoli, E. (1994) Biogenesis: plasma membrane calcium ATPase: 15 years of work on the purified enzyme. FASEB J. 8, 993-1002
    • (1994) FASEB J , vol.8 , pp. 993-1002
    • Carafoli, E.1
  • 17
    • 84941115762 scopus 로고    scopus 로고
    • Calmodulin and ion flux regulation?
    • Van Eldik, L. and Watterson, D.M, eds, pp, Brace & Company Publishers, USA Academic Press, San Diego
    • Brandt, P.C. and Vanaman, T.C. (1998) Calmodulin and ion flux regulation? in Calmodulin and Signal Transduction (Van Eldik, L. and Watterson, D.M., eds.) pp. 397-471 Brace & Company Publishers, USA Academic Press, San Diego
    • (1998) Calmodulin and Signal Transduction , pp. 397-471
    • Brandt, P.C.1    Vanaman, T.C.2
  • 18
    • 0025847743 scopus 로고
    • Glycosaminoclycans: Molecular properties, protein interactions, and role in physiological processes
    • Jackson, R.L., Busch, S.J., and Cardin, A.D. (1991) Glycosaminoclycans: molecular properties, protein interactions, and role in physiological processes. Physiol. Rev. 71, 481-539
    • (1991) Physiol. Rev , vol.71 , pp. 481-539
    • Jackson, R.L.1    Busch, S.J.2    Cardin, A.D.3
  • 19
    • 0346243796 scopus 로고    scopus 로고
    • 2+-ATPase from porcine brain synaptosome
    • 2+-ATPase from porcine brain synaptosome. Glycoconjugate J. 19, 373-378
    • (2003) Glycoconjugate J , vol.19 , pp. 373-378
    • Zhao, Y.1    Zhang, X.2
  • 20
    • 1642365552 scopus 로고    scopus 로고
    • 2+-ATPase of Arabidopsis thaliana, and characterization of a hyperactive mutant
    • 2+-ATPase of Arabidopsis thaliana, and characterization of a hyperactive mutant. Planta 218, 814-823
    • (2004) Planta , vol.218 , pp. 814-823
    • Bonza, M.C.1    Luoni, L.2    De Michelis, M.I.3
  • 21
    • 0027327277 scopus 로고
    • Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues
    • Margalit, H., Fischer, N., and Ben-Sasson, S.A. (1993) Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues. J. Biol. Chem. 268, 19228-19231
    • (1993) J. Biol. Chem , vol.268 , pp. 19228-19231
    • Margalit, H.1    Fischer, N.2    Ben-Sasson, S.A.3
  • 24
    • 0026074512 scopus 로고
    • Calcium pump of the plasma membrane
    • Carafoli, E. (1991) Calcium pump of the plasma membrane. Physiol. Rev. 71, 129-153
    • (1991) Physiol. Rev , vol.71 , pp. 129-153
    • Carafoli, E.1
  • 25
    • 0031964372 scopus 로고    scopus 로고
    • Evolution of substrate specificities in the P-type ATPases superfamily
    • Axelsen, K.B. and Palmgren, M.G. (1998) Evolution of substrate specificities in the P-type ATPases superfamily. J. Mol. Evol. 46, 84-101
    • (1998) J. Mol. Evol , vol.46 , pp. 84-101
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 31
    • 0038618955 scopus 로고    scopus 로고
    • Sulfated fucans, fresh perspectives: Structures, functions, and biological properties of sulfated fucans and an overview of enzymes active toward this class of polysaccharide
    • Berteau, O. and Mulloy, B. (2003) Sulfated fucans, fresh perspectives: structures, functions, and biological properties of sulfated fucans and an overview of enzymes active toward this class of polysaccharide. Glycobiology 13, 29R-40R
    • (2003) Glycobiology , vol.13
    • Berteau, O.1    Mulloy, B.2
  • 32
    • 0033008853 scopus 로고    scopus 로고
    • Heparinoids: Structure, biological activities and therapeutic applications
    • Gunay, N.S. and Linhardt, R.J. (1999) Heparinoids: structure, biological activities and therapeutic applications. Plant. Med. 65, 301-306
    • (1999) Plant. Med , vol.65 , pp. 301-306
    • Gunay, N.S.1    Linhardt, R.J.2
  • 33
    • 0002467899 scopus 로고    scopus 로고
    • Perception of fungal elicitors and signal transduction?
    • Aducci, P, ed, pp, Birkhauser, Basel, Switzerland
    • Cervone, F., Costorne, R., Leckie, F.D., and De Lorenzo, G. (1997) Perception of fungal elicitors and signal transduction? in Signal Transduction in Plants (Aducci, P., ed.) pp. 153-177 Birkhauser, Basel, Switzerland
    • (1997) Signal Transduction in Plants , pp. 153-177
    • Cervone, F.1    Costorne, R.2    Leckie, F.D.3    De Lorenzo, G.4
  • 34
    • 0034789069 scopus 로고    scopus 로고
    • The role of polygalacturonase-inhibiting proteins (PGIPs) in defense against pathogenic fungi
    • De Lorenzo, G., D'Ovidio, R., and Cervone, F. (2001) The role of polygalacturonase-inhibiting proteins (PGIPs) in defense against pathogenic fungi. Annu. Rev. Phytopathol. 39, 3131-335
    • (2001) Annu. Rev. Phytopathol , vol.39 , pp. 3131-3335
    • De Lorenzo, G.1    D'Ovidio, R.2    Cervone, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.