Brush-border calmodulin. A major component of the isolated microvillus core.
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Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actinCa++-calmodulin-dependent phosphorylation of myosin, and its role in brush border contraction in vitroOrganization of actin, myosin, and intermediate filaments in the brush border of intestinal epithelial cellsPurification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cellsCalmodulin binds to specific sequences in the cytoplasmic domain of C-CAM and down-regulates C-CAM self-associationCharacterization of an integral membrane glycoprotein associated with the microfilaments of pig intestinal microvilli.Rotavirus infection reduces sucrase-isomaltase expression in human intestinal epithelial cells by perturbing protein targeting and organization of microvillar cytoskeleton.Calmodulin in normal and cystic fibrosis human intestine at different developmental stages.Purification of calmodulin from Chlamydomonas: calmodulin occurs in cell bodies and flagella.Regulation of microvillus structure: calcium-dependent solation and cross-linking of actin filaments in the microvilli of intestinal epithelial cells.Brush-border alpha-actinin? Comparison of two proteins of the microvillus core with alpha-actinin by two-dimensional peptide mapping.Isolation and characterization of desmosome-associated tonofilaments from rat intestinal brush borderPartial reconstruction of the microvillus core bundle: characterization of villin as a Ca++-dependent, actin-bundling/depolymerizing proteinReevaluation of brush border motility: calcium induces core filament solution and microvillar vesiculation.Nucleated polymerization of actin from the membrane-associated ends of microvillar filaments in the intestinal brush border.Characterization of the 110-kdalton actin-calmodulin-, and membrane-binding protein from microvilli of intestinal epithelial cells.Direct measurement of actin polymerization rate constants by electron microscopy of actin filaments nucleated by isolated microvillus coresReactivation of intestinal epithelial cell brush border motility: ATP-dependent contraction via a terminal web contractile ring.Regulation of reactivated contraction in teleost retinal cone models by calcium and cyclic adenosine monophosphate.The brush border cytoskeleton is not static: in vivo turnover of proteins.Comparison of Ca++-regulated events in the intestinal brush border.Microvillus 110K-calmodulin: effects of nucleotides on isolated cytoskeletons and the interaction of the purified complex with F-actin.Behavior of a fluorescent analogue of calmodulin in living 3T3 cells.Calcium-regulated cooperative binding of the microvillar 110K-calmodulin complex to F-actin: formation of decorated filaments.Reassociation of microvillar core proteins: making a microvillar core in vitro.Ca2+-ATPase of the sarcoplasmic reticulum shares a common domain with a membrane glycoprotein associated with the cytoskeleton of microvilli.Analysis of cytoskeletal proteins and Ca2+-dependent regulation of structure in intestinal brush borders from rachitic chicksFimbrin is a cytoskeletal protein that crosslinks F-actin in vitroCalcium control of the intestinal microvillus cytoskeleton: its implications for the regulation of microfilament organizations.Brush border cytoskeleton and integration of cellular functions.Calcium/calmodulin inhibition of coupled NaCl transport in membrane vesicles from rabbit ileal brush border.Calmodulin accelerates the rate of polymerization of human platelet actin and alters the structural characteristics of actin filaments.Isolation and characterization of circumferential microfilament bundles from retinal pigmented epithelial cellsIsolation and characterization of a novel 68,000-Mr Ca2+-binding protein of lymphocyte plasma membrane.Troponin is unlikely to occur in bovine and chick forebrain.Ileal microvillar protein villin is tyrosine-phosphorylated and associates with PLC-gamma1. Role of cytoskeletal rearrangement in the carbachol-induced inhibition of ileal NaCl absorption.
P2860
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P2860
Brush-border calmodulin. A major component of the isolated microvillus core.
description
1980 nî lūn-bûn
@nan
1980年の論文
@ja
1980年論文
@yue
1980年論文
@zh-hant
1980年論文
@zh-hk
1980年論文
@zh-mo
1980年論文
@zh-tw
1980年论文
@wuu
1980年论文
@zh
1980年论文
@zh-cn
name
Brush-border calmodulin. A major component of the isolated microvillus core.
@ast
Brush-border calmodulin. A major component of the isolated microvillus core.
@en
type
label
Brush-border calmodulin. A major component of the isolated microvillus core.
@ast
Brush-border calmodulin. A major component of the isolated microvillus core.
@en
prefLabel
Brush-border calmodulin. A major component of the isolated microvillus core.
@ast
Brush-border calmodulin. A major component of the isolated microvillus core.
@en
P2093
P2860
P356
P1476
Brush-border calmodulin. A major component of the isolated microvillus core.
@en
P2093
P2860
P304
P356
10.1083/JCB.85.3.916
P407
P577
1980-06-01T00:00:00Z