Ca(2+)-induced folding and aggregation of skeletal muscle sarcoplasmic reticulum calsequestrin. The involvement of the trifluoperazine-binding site.
about
Role of Junctin protein interactions in cellular dynamics of calsequestrin polymer upon calcium perturbationGlycosylation of Skeletal Calsequestrin: IMPLICATIONS FOR ITS FUNCTIONCalsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channelsNatively unfolded proteins: a point where biology waits for physicsRegulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation.Retrograde regulation of STIM1-Orai1 interaction and store-operated Ca2+ entry by calsequestrin.Deconstructing calsequestrin. Complex buffering in the calcium store of skeletal muscle.Organellar calcium buffers.Luminal calcium regulates calcium release in triads isolated from frog and rabbit skeletal muscle.Protons induce calsequestrin conformational changes.Head-to-tail oligomerization of calsequestrin: a novel mechanism for heterogeneous distribution of endoplasmic reticulum luminal proteins.
P2860
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P2860
Ca(2+)-induced folding and aggregation of skeletal muscle sarcoplasmic reticulum calsequestrin. The involvement of the trifluoperazine-binding site.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Ca(2+)-induced folding and agg ...... trifluoperazine-binding site.
@en
type
label
Ca(2+)-induced folding and agg ...... trifluoperazine-binding site.
@en
prefLabel
Ca(2+)-induced folding and agg ...... trifluoperazine-binding site.
@en
P2093
P1476
Ca(2+)-induced folding and agg ...... e trifluoperazine-binding site
@en
P2093
P304
24635-24641
P407
P577
1993-11-01T00:00:00Z