Structural rearrangement of CaMKIIalpha catalytic domains encodes activation.
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Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activationIntersubunit capture of regulatory segments is a component of cooperative CaMKII activationA Mechanism for Tunable Autoinhibition in the Structure of a Human Ca2+/Calmodulin- Dependent Kinase II HoloenzymeSize, stoichiometry, and organization of soluble LC3-associated complexesFluorescence applications in molecular neurobiologyFörster resonance energy transfer microscopy and spectroscopy for localizing protein-protein interactions in living cells.A fluorescent biosensor reveals conformational changes in human immunoglobulin E Fc: implications for mechanisms of receptor binding, inhibition, and allergen recognitionThe CaMKII holoenzyme structure in activation-competent conformationsAnomalous surplus energy transfer observed with multiple FRET acceptors.CaMKII activation and dynamics are independent of the holoenzyme structure: an infinite subunit holoenzyme approximationFluorescence polarization and fluctuation analysis monitors subunit proximity, stoichiometry, and protein complex hydrodynamicsThe impact of heterogeneity and dark acceptor states on FRET: implications for using fluorescent protein donors and acceptorsAddiction research centres and the nurturing of creativity: the National Institute on Alcohol Abuse and Alcoholism.A Simple, Highly Efficient Method for Heterologous Expression in Mammalian Primary Neurons Using Cationic Lipid-mediated mRNA Transfection.Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction.Rapid global fitting of large fluorescence lifetime imaging microscopy datasets.Conformational changes underlying calcium/calmodulin-dependent protein kinase II activation.Regulation of gastrointestinal motility by Ca2+/calmodulin-stimulated protein kinase II.Covert Changes in CaMKII Holoenzyme Structure Identified for Activation and Subsequent Interactions.Homodimerization of amyloid precursor protein at the plasma membrane: a homoFRET study by time-resolved fluorescence anisotropy imagingThe delicate bistability of CaMKIIFluorescence resonance energy transfer microscopy as demonstrated by measuring the activation of the serine/threonine kinase Akt.Multiple CaMKII Binding Modes to the Actin Cytoskeleton Revealed by Single-Molecule Imaging.Structural studies on the regulation of Ca2+/calmodulin dependent protein kinase IICaught in the act: quantifying protein behaviour in living cells.Activation of the Ano1 (TMEM16A) chloride channel by calcium is not mediated by calmodulin.Spatiotemporal Regulation of Signaling in and out of Dendritic Spines: CaMKII and Ras.Homo-FRET imaging as a tool to quantify protein and lipid clustering.Analysis of CaM-kinase signaling in cells.Quantitative microscopy and imaging tools for the mechanical analysis of morphogenesis.Probing the kinome in real time with fluorescent peptides.Homo-FRET Based Biosensors and Their Application to Multiplexed Imaging of Signalling Events in Live Cells.Simultaneous FRAP, FLIM and FAIM for measurements of protein mobility and interaction in living cells.Interactions between αCaMKII and calmodulin in living cells: conformational changes arising from CaM-dependent and -independent relationships.CRABP1 protects the heart from isoproterenol-induced acute and chronic remodeling.Deciphering CaMKII Multimerization Using Fluorescence Correlation Spectroscopy and Homo-FRET Analysis.Auto-FPFA: An Automated Microscope for Characterizing Genetically Encoded Biosensors.
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P2860
Structural rearrangement of CaMKIIalpha catalytic domains encodes activation.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on April 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Structural rearrangement of CaMKIIalpha catalytic domains encodes activation.
@en
Structural rearrangement of CaMKIIalpha catalytic domains encodes activation.
@nl
type
label
Structural rearrangement of CaMKIIalpha catalytic domains encodes activation.
@en
Structural rearrangement of CaMKIIalpha catalytic domains encodes activation.
@nl
prefLabel
Structural rearrangement of CaMKIIalpha catalytic domains encodes activation.
@en
Structural rearrangement of CaMKIIalpha catalytic domains encodes activation.
@nl
P2093
P2860
P356
P1476
Structural rearrangement of CaMKIIalpha catalytic domains encodes activation
@en
P2093
Christopher Thaler
Paul S Blank
Srinagesh V Koushik
P2860
P304
P356
10.1073/PNAS.0901913106
P407
P577
2009-04-01T00:00:00Z