Cyclopiazonic Acid Is Complexed to a Divalent Metal Ion When Bound to the Sarcoplasmic Reticulum Ca2+-ATPase
Open Access
- 1 May 2009
- journal article
- Published by Elsevier BV
- Vol. 284 (20), 13513-13518
- https://doi.org/10.1074/jbc.c900031200
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- Calcium SignalingCell, 2007
- Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitorsProceedings of the National Academy of Sciences of the United States of America, 2007
- Modulatory and catalytic modes of ATP binding by the calcium pumpThe EMBO Journal, 2006
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D-Biological Crystallography, 2004
- Cyclopiazonic acid reduces the coupling factor of the Ca2+‐ATPase acting on Ca2+ bindingFEBS Letters, 2004
- Hydrogen bonds with π-acceptors in proteins: frequencies and role in stabilizing local 3D structures11Edited by R. HuberJournal of Molecular Biology, 2001
- Mutagenesis of Segment 487Phe-Ser-Arg-Asp-Arg-Lys492 of Sarcoplasmic Reticulum Ca2+-ATPase Produces Pumps Defective in ATP BindingPublished by Elsevier BV ,1996
- Structural organization, ion transport, and energy transduction of P-type ATPasesBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1996
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- 2,5‐Di(tert‐butyl)‐1,4‐benzohydroquinone — a novel inhibitor of liver microsomal Ca2+ sequestrationFEBS Letters, 1987