Modulating sarco(endo)plasmic reticulum Ca2+ ATPase 2 (SERCA2) activity: cell biological implications.
作者： Peter Vangheluwe , Luc Raeymaekers , Leonard Dode , Frank Wuytack
DOI: 10.1016/J.CECA.2005.06.033
关键词:
摘要: … 2+ -transport ATPases (ie plasma membrane Ca 2+ ATPase (PMCA) in the plasma membrane and secretory pathway Ca 2+ ATPase (… , the SERCA ATPase activity is maximal at a fatty …
core.ac.uk
elsevier.com
sci-hub.se 参考文章(118)
Peter VANGHELUWE, Marleen SCHUERMANS, Ernö ZÁDOR, Etienne WAELKENS, Luc RAEYMAEKERS, Frank WUYTACK, Sarcolipin and phospholamban mRNA and protein expression in cardiac and skeletal muscle of different species Biochemical Journal. ,vol. 389, pp. 151- 159 ,(2005) , 10.1042/BJ20050068
Rosa I. VINER, Deborah A. FERRINGTON, Todd D. WILLIAMS, Diana J. BIGELOW, Christian SCHÖNEICH, Protein modification during biological aging: selective tyrosine nitration of the SERCA2a isoform of the sarcoplasmic reticulum Ca2+-ATPase in skeletal muscle. Biochemical Journal. ,vol. 340, pp. 657- 669 ,(1999) , 10.1042/BJ3400657
Alex Odermatt, Stefan Becker, Vijay K. Khanna, Kazimierz Kurzydlowski, Elmi Leisner, Dirk Pette, David H. MacLennan, Sarcolipin regulates the activity of SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+-ATPase. Journal of Biological Chemistry. ,vol. 273, pp. 12360- 12369 ,(1998) , 10.1074/JBC.273.20.12360
Alex Odermatt, Kazimierz Kurzydlowski, David H. MacLennan, The vmax of the Ca2+-ATPase of cardiac sarcoplasmic reticulum (SERCA2a) is not altered by Ca2+/calmodulin-dependent phosphorylation or by interaction with phospholamban. Journal of Biological Chemistry. ,vol. 271, pp. 14206- 14213 ,(1996) , 10.1074/JBC.271.24.14206
Ursula G. Danilczyk, David B. Williams, The lectin chaperone calnexin utilizes polypeptide-based interactions to associate with many of its substrates in vivo. Journal of Biological Chemistry. ,vol. 276, pp. 25532- 25540 ,(2001) , 10.1074/JBC.M100270200
R. Foyouzi-Youssefi, S. Arnaudeau, C. Borner, W. L. Kelley, J. Tschopp, D. P. Lew, N. Demaurex, K.-H. Krause, Bcl-2 decreases the free Ca2+ concentration within the endoplasmic reticulum Proceedings of the National Academy of Sciences of the United States of America. ,vol. 97, pp. 5723- 5728 ,(2000) , 10.1073/PNAS.97.11.5723
Petra Algenstaedt, David A. Antonetti, Michael B. Yaffe, C. Ronald Kahn, Insulin receptor substrate proteins create a link between the tyrosine phosphorylation cascade and the Ca2+-ATPases in muscle and heart. Journal of Biological Chemistry. ,vol. 272, pp. 23696- 23702 ,(1997) , 10.1074/JBC.272.38.23696
Yoshito Ihara, Myrna F Cohen-Doyle, Yoshiro Saito, David B Williams, Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro. Molecular Cell. ,vol. 4, pp. 331- 341 ,(1999) , 10.1016/S1097-2765(00)80335-4
Patricia Camacho, James D Lechleiter, Calreticulin inhibits repetitive intracellular Ca2+ waves Cell. ,vol. 82, pp. 765- 771 ,(1995) , 10.1016/0092-8674(95)90473-5
Hetty N. Wong, Malcolm A. Ward, Alexander W. Bell, Eric Chevet, Satty Bains, Walter P. Blackstock, Roberto Solari, David Y. Thomas, John J. M. Bergeron, Conserved in VivoPhosphorylation of Calnexin at Casein Kinase II Sites as Well as a Protein Kinase C/Proline-directed Kinase Site Journal of Biological Chemistry. ,vol. 273, pp. 17227- 17235 ,(1998) , 10.1074/JBC.273.27.17227