The 2.7 A crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation
about
Evolution and origin of merlin, the product of the Neurofibromatosis type 2 (NF2) tumor-suppressor geneStructural basis of cargo recognition by the myosin-X MyTH4-FERM domainTarget-selective protein S-nitrosylation by sequence motif recognitionStructure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304Model membranes to shed light on the biochemical and physical properties of ezrin/radixin/moesinStructural basis for neurofibromatosis type 2. Crystal structure of the merlin FERM domainStructure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactionsUnfurling of the band 4.1, ezrin, radixin, moesin (FERM) domain of the merlin tumor suppressorThe phosphotyrosine binding-like domain of talin activates integrinsA novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targetingOrganizing the cell cortex: the role of ERM proteinsCrystal structure of the FERM domain of focal adhesion kinase.FERM domain interaction promotes FAK signaling.Characterization of a novel intracellular heparanase that has a FERM domain.Structural conservation in band 4.1, ezrin, radixin, moesin (FERM) domains as a guide to identify inhibitors of the proline-rich tyrosine kinase 2.Binding of moesin and ezrin to membranes containing phosphatidylinositol (4,5) bisphosphate: a comparative study of the affinity constants and conformational changes.Targeting Pyk2 for therapeutic interventionEmerging role for ERM proteins in cell adhesion and migration.The Pyk2 FERM domain as a target to inhibit glioma migration.Membrane recognition and targeting by lipid-binding domains.Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain.Cellular and molecular interactions of phosphoinositides and peripheral proteinsLocalization of the ezrin binding epitope for glycated proteins.PtdIns-4,5-P2 as a potential therapeutic target for pathologic angiogenesis.In Vitro and in Vivo Characterization of Molecular Interactions between Calmodulin, Ezrin/Radixin/Moesin, and L-selectin.FERM domain of moesin desorbs the basic-rich cytoplasmic domain of l-selectin from the anionic membrane surface.The expanding family of FERM proteins.Re-defining ERM function in lymphocyte activation and migration.Moesin-induced signaling in response to lipopolysaccharide in macrophages.Dissecting the actin cortex density and membrane-cortex distance in living cells by super-resolution microscopy.Mechanistic principles underlying regulation of the actin cytoskeleton by phosphoinositides.Molecular Regulation of Sprouting Angiogenesis.Single-molecule detection of phosphorylation-induced plasticity changes during ezrin activation.A phosphatidylinositol 4,5-bisphosphate redistribution-based sensing mechanism initiates a phagocytosis programing
P2860
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P2860
The 2.7 A crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation
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2001 nî lūn-bûn
@nan
2001 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2001年の論文
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2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
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name
The 2.7 A crystal structure of ...... ructural changes on activation
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The 2.7 A crystal structure of ...... ructural changes on activation
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The 2.7 A crystal structure of ...... ructural changes on activation
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The 2.7 A crystal structure of ...... ructural changes on activation
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The 2.7 A crystal structure of ...... ructural changes on activation
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The 2.7 A crystal structure of ...... ructural changes on activation
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The 2.7 A crystal structure of ...... ructural changes on activation
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The 2.7 A crystal structure of ...... ructural changes on activation
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The 2.7 A crystal structure of ...... ructural changes on activation
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P356
P1433
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The 2.7 A crystal structure of ...... ructural changes on activation
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P2093
P304
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10.1021/BI010419H
P407
P577
2001-06-19T00:00:00Z