Ca2+-dependent hydrophobic-interaction chromatography. Isolation of a novel Ca2+-binding protein and protein kinase C from bovine brain.
about
Calretinin: a gene for a novel calcium-binding protein expressed principally in neuronsRelationships between IgE/IgG4 Epitopes, Structure and Function in Anisakis simplex Ani s 5, a Member of the SXP/RAL-2 Protein FamilyPolycation-dependent, Ca2+-antagonized phosphorylation of calmodulin by casein kinase-2 and a spleen tyrosine protein kinasePhosphorylation of the myosin phosphatase inhibitors, CPI-17 and PHI-1, by integrin-linked kinaseA highly sensitive method for quantification of myosin light chain phosphorylation by capillary isoelectric focusing with laser-induced fluorescence detection.Structure-function relations of smooth muscle calponin. The critical role of serine 175.Frog p26olf, a molecule with two S100-like regions in a single peptide.A casein kinase II-related activity is involved in phosphorylation of microtubule-associated protein MAP-1B during neuroblastoma cell differentiation.R2D5 antigen: a calcium-binding phosphoprotein predominantly expressed in olfactory receptor neurons.Molecular cloning of two additional members of the neural visinin-like Ca(2+)-binding protein gene family.Stimulus-response coupling: the search for intracellular calcium mediator proteins.Smooth-muscle caldesmon phosphatase is SMP-I, a type 2A protein phosphatase.Regulation of protein kinase C activity by various lipids.Purification and characterization of calponin phosphatase from smooth muscle. Effect of dephosphorylation on calponin functionPurification and internal amino acid sequence of the 80 kDa protein kinase C substrate from Swiss 3T3 fibroblasts. Homology with substrates from brain.Phosphorylation of microtubule proteins in rat brain at different developmental stages: comparison with that found in neuronal cultures.The effects of phosphorylation of smooth-muscle caldesmon.A comparison of the effects of calponin on smooth and skeletal muscle actomyosin systems in the presence and absence of caldesmon.Calponin phosphorylation in vitro and in intact muscle.The effects of caldesmon on the ATPase activities of rabbit skeletal-muscle myosin.Myosin regulatory light chain diphosphorylation slows relaxation of arterial smooth muscle.Purification of smooth-muscle myosin free of calmodulin and myosin light-chain kinase. Susceptibility to oxidationInhibitory action of polyamines on protein kinase C association to membranes.Interaction between protein kinase C and Exo1 (14-3-3 protein) and its relevance to exocytosis in permeabilized adrenal chromaffin cells.Inhibition by calponin of isometric force in demembranated vascular smooth muscle strips: the critical role of serine-175.Purification and properties of a 23 kDa Ca2(+)-binding protein from Drosophila melanogaster.Physicochemical properties of a novel Mr-21 000 Ca2+-binding protein of bovine brain.Autophosphorylation of smooth-muscle caldesmon.The involvement of protein kinase C in myosin phosphorylation and force development in rat tail arterial smooth muscle.alpha1-Adrenoceptor-mediated phosphorylation of myosin in rat-tail arterial smooth muscle.Fluorescent and photoactive probes for the study of protein kinase C.Ca2+-independent phosphorylation of myosin in rat caudal artery and chicken gizzard myofilaments.Phosphorylation of an acidic mol. wt. 80 000 cellular protein in a cell-free system and intact Swiss 3T3 cells: a specific marker of protein kinase C activity.Kinase activity associated with caldesmon is Ca2+/calmodulin-dependent kinase II.The predominant calcimedins from Trypanosoma brucei comprise a family of flagellar EF-hand calcium-binding proteins.Purification of a phosphoprotein from rat brain closely related to the 80 kDa substrate of protein kinase C identified in Swiss 3T3 fibroblasts.Characterization of the autophosphorylation of chicken gizzard caldesmon.Properties and distribution of the protein inhibitor (Mr 17,000) of protein kinase C.Properties of caldesmon isolated from chicken gizzard.Ca2+-binding proteins from bovine brain including a potent inhibitor of protein kinase C.
P2860
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P2860
Ca2+-dependent hydrophobic-interaction chromatography. Isolation of a novel Ca2+-binding protein and protein kinase C from bovine brain.
description
1984 nî lūn-bûn
@nan
1984年の論文
@ja
1984年論文
@yue
1984年論文
@zh-hant
1984年論文
@zh-hk
1984年論文
@zh-mo
1984年論文
@zh-tw
1984年论文
@wuu
1984年论文
@zh
1984年论文
@zh-cn
name
Ca2+-dependent hydrophobic-int ...... in kinase C from bovine brain.
@en
Ca2+-dependent hydrophobic-int ...... in kinase C from bovine brain.
@nl
type
label
Ca2+-dependent hydrophobic-int ...... in kinase C from bovine brain.
@en
Ca2+-dependent hydrophobic-int ...... in kinase C from bovine brain.
@nl
prefLabel
Ca2+-dependent hydrophobic-int ...... in kinase C from bovine brain.
@en
Ca2+-dependent hydrophobic-int ...... in kinase C from bovine brain.
@nl
P2093
P2860
P356
P1433
P1476
Ca2+-dependent hydrophobic-int ...... in kinase C from bovine brain.
@en
P2093
C A Carruthers
K A Valentine
M D Hollenberg
P2860
P304
P356
10.1042/BJ2240117
P407
P577
1984-11-01T00:00:00Z