Indirect association of ezrin with F-actin: isoform specificity and calcium sensitivity.
about
Advanced glycation end-products induce calpain-mediated degradation of ezrinVertebrates have conserved capping protein alpha isoforms with specific expression patternsEzrin is a cyclic AMP-dependent protein kinase anchoring proteinEzrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding siteSupervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamilyAfadin: A novel actin filament-binding protein with one PDZ domain localized at cadherin-based cell-to-cell adherens junctionDominant negative effect of cytoplasmic actin isoproteins on cardiomyocyte cytoarchitecture and functionThe neurofibromatosis 2 protein product merlin selectively binds F-actin but not G-actin, and stabilizes the filaments through a lateral associationVisualization of mRNA translation in living cellsCalpain- and talin-dependent control of microvascular pericyte contractility and cellular stiffness.One of the two cytoplasmic actin isoforms in Drosophila is essential.Loss of γ-cytoplasmic actin triggers myofibroblast transition of human epithelial cells.Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets.Pericyte contractility controls endothelial cell cycle progression and sprouting: insights into angiogenic switch mechanics.Controlling tumor-derived and vascular endothelial cell growth: role of the 4Ff2 cell surface antigenHow and why does beta-actin mRNA target?Ezrin regulates focal adhesion and invadopodia dynamics by altering calpain activity to promote breast cancer cell invasion.Betacap73-ARF6 interactions modulate cell shape and motility after injury in vitro.Nonredundant roles of cytoplasmic β- and γ-actin isoforms in regulation of epithelial apical junctionsEzrin oligomers are major cytoskeletal components of placental microvilli: a proposal for their involvement in cortical morphogenesis.Calpain regulates actin remodeling during cell spreading.The physiological significance of beta -actin mRNA localization in determining cell polarity and directional motility.Neurotrophin regulation of beta-actin mRNA and protein localization within growth cones.Human NK cell lytic granules and regulation of their exocytosisEpidermal growth factor activates m-calpain (calpain II), at least in part, by extracellular signal-regulated kinase-mediated phosphorylationInhibition of calpain blocks platelet secretion, aggregation, and spreadingTargeted gene inactivation reveals a functional role of calpain-1 in platelet spreading.The calpain system and cancer.Calpain mediates epithelial cell microvillar effacement by enterohemorrhagic Escherichia coli.beta-Actin is confined to structures having high capacity of remodelling in developing and adult rat cerebellum.Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway.Inhibition of angiogenesis in vitro: a central role for beta-actin dependent cytoskeletal remodelingActin is cleaved during constitutive apoptosis.Ezrin expression in stromal cells of capillary hemangioblastoma. An immunohistochemical survey of brain tumors.Calpain regulates enterocyte brush border actin assembly and pathogenic Escherichia coli-mediated effacement.Rapid and efficient purification of actin from nonmuscle sources.The amino-terminal domains of the ezrin, radixin, and moesin (ERM) proteins bind advanced glycation end products, an interaction that may play a role in the development of diabetic complications.Cytokinesis requires localized β-actin filament production by an actin isoform specific nucleator.A single vegetative actin isovariant overexpressed under the control of multiple regulatory sequences is sufficient for normal Arabidopsis development.An essential role for beta-actin mRNA localization and translation in Ca2+-dependent growth cone guidance.
P2860
Q24293645-8BDB90E1-2346-41CE-BBF6-76ADFA36766CQ24318388-952F34D9-0C5D-4560-B231-B2A27F3CC8B8Q24532065-00B93999-FD87-4FC9-9874-2F5F3D0D5800Q24617964-6F66F49D-40AD-42AA-BA7C-2ABF7C644C01Q24678046-12DC57EE-525B-4AB6-AEEE-D0BEF612B5A9Q24678766-E75B5CC9-CD7E-477F-AAD0-882A6F24AA99Q28273036-08D65C8A-EB8A-4A41-8D84-5A75ED77614BQ28365540-A878D3CD-106A-4FA0-B845-CAF7207D3964Q30480528-C6DC9581-2408-46C8-ACE0-7CC8708F286BQ33657916-95328E61-E720-49EA-99CC-E83FAF920187Q34031008-2880ED16-040D-46BF-BA97-A544D598C22BQ34337974-35C3980C-53A1-4404-A098-6A6B4E4D361BQ34369147-6F9736EE-A4EF-4ADC-A2FF-E2017F6B46A8Q34439465-146DE24D-0B3D-4A00-9F06-EE4E519B9469Q35746649-BB3D5567-A325-455F-9508-4F4F8F250D40Q35985195-77661225-3529-449B-B725-A4FFB497EFAFQ36115398-AE737683-5E06-4E69-9373-A0684C804033Q36125069-AF1EDECB-E908-4C1A-B07E-B396AC029CCEQ36234461-D3381718-A574-4D30-8F76-09DDB2ED650AQ36236171-1E3E62DD-3DA2-4E73-9CBD-65E97D32D66CQ36255313-0ACD9CD8-6828-493D-953F-2969D0F016C8Q36290552-657808B1-EBE7-4CBB-84FE-451931D529DFQ36310756-A5149BFE-B45D-4E56-8DAA-FB643905A2A7Q36386541-8379595A-A31F-41A2-A5B8-2B4E22C76606Q36571781-0C4F4393-0151-434B-984B-B6AFF1947E53Q37307187-54A68BB9-8892-46A6-97FF-9480B301B05CQ37641872-57906ED4-3524-4A73-A4CA-AFC9A118C008Q37867486-BEDE1854-F677-4495-990F-A1F9C26DE4FFQ38979394-E4BBAC37-6984-4802-9725-ADAC546A84D9Q39758660-A92437E7-F829-4F25-B411-310BE7A3C502Q40904417-26072C16-F615-4397-9FD3-18D5878D919EQ41787624-BF12C81F-A5CD-4CD7-9FE3-0E6EB7BC4795Q41968458-C8CBB21B-787E-47BA-9EEE-92C288F76DCFQ42827339-2FE49261-5BB9-4ABF-95DD-F823D6EF84EFQ43068880-69C6094B-CCFB-4622-8628-18490C44BF6EQ43201497-63B454BC-4D33-4BB3-AFD2-7C0390B11BA3Q44432075-E3299D42-5DBB-4C3C-97D0-8E8D0786015BQ47109306-E77FD6EA-4C0F-463D-8E4B-255C6EE89403Q47608583-A157DBF6-4804-4413-805B-AF1B0130F417Q48419140-1D637D93-B0F2-40CE-A436-FF0959CCBDEE
P2860
Indirect association of ezrin with F-actin: isoform specificity and calcium sensitivity.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Indirect association of ezrin with F-actin: isoform specificity and calcium sensitivity.
@en
Indirect association of ezrin with F-actin: isoform specificity and calcium sensitivity.
@nl
type
label
Indirect association of ezrin with F-actin: isoform specificity and calcium sensitivity.
@en
Indirect association of ezrin with F-actin: isoform specificity and calcium sensitivity.
@nl
prefLabel
Indirect association of ezrin with F-actin: isoform specificity and calcium sensitivity.
@en
Indirect association of ezrin with F-actin: isoform specificity and calcium sensitivity.
@nl
P2860
P356
P1476
Indirect association of ezrin with F-actin: isoform specificity and calcium sensitivity.
@en
P2093
C B Shuster
I M Herman
P2860
P304
P356
10.1083/JCB.128.5.837
P407
P577
1995-03-01T00:00:00Z