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1 phospholamban activity and secondarily, the sarcoplasmic reticulum Ca2+ ATPase.
2 art, changes in alpha-myosin heavy chain and sarcoplasmic reticulum Ca2+ ATPase.
3 trial natriuretic factor, phospholamban, and sarcoplasmic reticulum Ca2+-ATPase.
4 en generated, based on the structures of the sarcoplasmic reticulum Ca2+-ATPase.
5 le resemblance to the E2 structure of rabbit sarcoplasmic reticulum Ca2+-ATPase.
7 Sarcolipin is a novel regulator of cardiac sarcoplasmic reticulum Ca2+ ATPase 2a (SERCA2a) and is e
10 Phospholamban is a critical regulator of the sarcoplasmic reticulum Ca2+-ATPase activity and myocardi
11 etch response proteins, myocyte hypertrophy, sarcoplasmic reticulum Ca2+-ATPase activity and uptake,
12 amban phosphorylation was reduced (P=0.015), sarcoplasmic reticulum Ca2+-ATPase activity was impaired
13 horylation of phospholamban (PLB), decreased sarcoplasmic reticulum Ca2+-ATPase activity, and a decre
14 biotin switch method, including the cardiac sarcoplasmic reticulum Ca2+-ATPase, alpha-ketoglutarate
15 clopiazonic acid (20 microM; an inhibitor of sarcoplasmic reticulum Ca2+-ATPase) also activated the n
16 hospho-p38 or phospho-jnk), a 30% decline in sarcoplasmic reticulum Ca2+-ATPase, an 80% reduction in
17 lay a direct role in cation transport by the sarcoplasmic reticulum Ca2+-ATPase and the Na+, K+-ATPas
18 hannel density and the relative abundance of sarcoplasmic reticulum Ca2+ ATPase density were reduced
19 suggest that continual uptake of Ca2+ by the sarcoplasmic reticulum Ca2+-ATPase into a ryanodine-sens
23 significant change in the content for either sarcoplasmic reticulum Ca2+ ATPase or calsequestrin, in
25 y have evolved in response to paucity of the sarcoplasmic reticulum Ca2+-ATPase/phospholamban complex
27 ms; P=0.001) and was associated with a lower sarcoplasmic reticulum Ca2+ ATPase pump to phospholamban
29 alpha-myosin heavy chain (alphaMHC) and the sarcoplasmic reticulum Ca2+-ATPase (SERCA) genes was rep
35 force-frequency relationship, and decreased sarcoplasmic reticulum Ca2+ ATPase (SERCA2a) activity.
36 m the left ventricular wall demonstrate that sarcoplasmic reticulum Ca2+ ATPase (SERCA2a) expression
38 controls intracellular Ca(2+) handling, the sarcoplasmic reticulum Ca2+ ATPase (SERCA2a), induces fu
39 een linked to Ca2+ cycling proteins, such as sarcoplasmic reticulum Ca2+ ATPase (SERCA2a), located in
41 ), phospholamban phosphorylation (P < 0.04), sarcoplasmic reticulum Ca2+-ATPase (SERCA2a) affinity fo
45 how information on altered expression of the sarcoplasmic reticulum Ca2+-ATPase, when interpreted thr
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