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1 ed to probe interactions between CaM and the plasma-membrane Ca2+-ATPase.
2 haracterized sarco/endoplasmic reticulum and plasma membrane Ca2+-ATPases.
3 cence labeling for myosin 1c, myosin 7a, and plasma membrane Ca2+ ATPase 2 was studied to determine t
4 l distribution, mobility, and trafficking of plasma membrane Ca2+ATPase-2 (PMCA2), a protein enriched
5 We showed previously that deficiency of the plasma membrane Ca2+ ATPase 4 (PMCA4) in L929 cells impa
6 owever, massive up-regulation of the PMCA2bw plasma membrane Ca2+-ATPase also occurs during lactation
7 ion, we characterize CG2165, which encodes a plasma membrane Ca2+-ATPase, and show that it plays an i
9 , inhibition of the Na+/Ca2+exchanger or the plasma membrane Ca2+ ATPase had no influence on the abil
12 ease, calpain, leading to the degradation of plasma membrane Ca2+-ATPase isoform 1 and fodrin; the de
15 satory mechanisms include Ca2+ extrusion via plasma membrane Ca2+-ATPase, mitochondrial uptake, myopl
19 is study examined the potential roles of the plasma membrane Ca2+-ATPase (PMCA) at the blood-CSF and
22 trinsic tryptophan (Trp) fluorescence of the plasma membrane Ca2+-ATPase (PMCA) is significantly quen
23 (P < 0.07) but expression of TRPV6/ECaC2 and plasma membrane Ca2+-ATPase (PMCA) isoforms 1 and 4 were
26 n of calcium metabolism in the platelet, the plasma membrane Ca2+-ATPase (PMCA) was assessed for cAMP
27 ected oscillations whereas inhibition of the plasma membrane Ca2+-ATPase (PMCA) with La3+ had little
28 e the Kd for the interaction of CaM with the plasma membrane Ca2+-ATPase (PMCA), a Ca2+ pump regulate
29 binds to a domain near the C-terminus of the plasma membrane Ca2+-ATPase (PMCA), causing the release
32 nmasked in the presence of inhibitors of the plasma membrane Ca2+ ATPases (PMCAs) and mitochondrial C
33 e endoplasmic or sarcoplasmic reticulum, the plasma membrane Ca2+-ATPases (PMCAs), which extrude Ca2+
35 ular calcium had no effect), activation of a plasma membrane Ca2+-ATPase (two inhibitors, vanadate (3
37 n represents a novel biological role for the plasma membrane Ca2+-ATPases, which are generally regard
38 ner ear, robust Ca2+/H+ exchange mediated by plasma-membrane Ca2+-ATPase would rapidly acidify mechan
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