Structural changes in the calcium pump accompanying the dissociation of calcium

By C. Toyoshima, H. Nomura. Nature, 2002

875 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/6ebe664d0f10c42a4eb3f5aaf13141f01264b1bc

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In Molecular Biology

Citations in the corpus

Bilayer thickness and membrane protein function: an energetic perspective. (2007, background): “These conformational changes involve the protein/bilayer interface (112), meaning that G 0 def may be different for transporters having their binding site exposed to the left and to the right solution.”
Calcium: Phospholamban: a crucial regulator of cardiac contractility (2003, background): “(Ca 2+ ) 2 , the high-energy phosphoenzyme conformation, is formed in the phosphorylation (occlusion) stage; E 2 P, the low-energy phosphoenzyme, is formed during the stage of Ca 2+ release to the lumen; and E 2 is formed after hydrolysis of the acylphosphate and release of inorganic phosphat”
What vibrations tell about proteins (2002, background): “A comparison of two Ca2+-ATPase structures (Toyoshima et al. 2000 ; Toyoshima & Nomura, 2002) shows that much of the conformational change can be explained by rigid domain movements, kinking of helices or movements of helices relative to others.”
Artemisinins target the SERCA of Plasmodium falciparum (2003, background): “Thapsigargin irreversibly inhibits Ca 2p -dependent ATPase activity of SERCA with 1:1 stoichiometr”
Biology, structure and mechanism of P-type ATPases (2004, background): “The SR Ca 2+ -ATPase has become the archetype of the P-type-ATPase family, because its atomic structure is the only one so far to have been determined experimentall”
iMODS: internal coordinates normal mode analysis server (2014, background): “In this example, in consonance with observed functional states (25) and other NMA studies (23,26), the NMA B-factors correctly identify N, A, the luminal part of M and the tip of P as highly dynamical domains.”