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Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator.
By interacting with hundreds of protein partners, 14-3-3 proteins coordinate vital cellular processes. Phosphorylation of the small heat shock protein, HSPB6, within its intrinsically disorderedExpand
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The purple Trp288Ala mutant of Synechocystis OCP persistently quenches phycobilisome fluorescence and tightly interacts with FRP.
In Cyanobacteria, the Orange Carotenoid Protein (OCP) and Fluorescence Recovery Protein (FRP) are central to the photoprotective mechanism consisting in regulated quenching of phycobilisome (PBs)Expand
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Oligomeric structure of 14‐3‐3 protein: What do we know about monomers?
14‐3‐3s predominantly form homo‐/heterodimers that are in equilibrium with corresponding monomers. Dimer/monomer equilibrium depends on the nature and phosphorylation of Ser58 of certain 14‐3‐3Expand
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Assembly of photoactive Orange Carotenoid Protein from its domains unravels a carotenoid shuttle mechanism
The Orange Carotenoid Protein (OCP) is indispensable for cyanobacterial photoprotection by quenching phycobilisome fluorescence upon photoconversion from the orange OCPO to the red OCPR form.Expand
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Effect of mutations mimicking phosphorylation on the structure and properties of human 14-3-3zeta.
Effect of mutations mimicking phosphorylation on the structure of human 14-3-3zeta protein was analyzed by different methods. Mutation S58E increased intrinsic Trp fluorescence and binding of bis-ANSExpand
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The Signaling State of Orange Carotenoid Protein.
Orange carotenoid protein (OCP) is the photoactive protein that is responsible for high light tolerance in cyanobacteria. We studied the kinetics of the OCP photocycle by monitoring changes in itsExpand
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14-3-3 Proteins and regulation of cytoskeleton
The proteins of the 14-3-3 family are universal adapters participating in multiple processes running in the cell. We describe the structure, isoform composition, and distribution of 14-3-3 proteinsExpand
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Quaternary structure of human small heat shock protein HSPB6 (Hsp20) in crowded media modeled by trimethylamine N-oxide (TMAO): Effect of protein phosphorylation.
Effect of trimethylamine N-oxide (TMAO), well-known osmolyte, widely used to imitate crowded intracellular conditions, on the quaternary structure of recombinant human small heat shock protein HspB6Expand
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Phosphorylation of more than one site is required for tight interaction of human tau protein with 14‐3‐3ζ
MINT‐7233285, MINT‐7233297, MINT‐7233310: 14‐3‐3 zeta (uniprotkb:P63104) and Tau 3 (uniprotkb:P10636‐3) bind (MI:0407) by comigration in non‐denaturing gel electrophoresis (MI:0404)
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Monomeric 14-3-3ζ Has a Chaperone-Like Activity and Is Stabilized by Phosphorylated HspB6
Members of the 14-3-3 eukaryotic protein family predominantly function as dimers. The dimeric form can be converted into monomers upon phosphorylation of Ser58 located at the subunit interface.Expand
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