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Effect of phosphorylation on interaction of human tau protein with 14-3-3zetaInvariant amino acids essential for decoding function of polypeptide release factor eRF1.Some properties of human small heat shock protein Hsp20 (HspB6)Small heat shock protein Hsp20 (HspB6) as a partner of 14-3-3gamma.Heterooligomeric complexes of human small heat shock proteinsStructure, properties, and functions of the human small heat-shock protein HSP22 (HspB8, H11, E2IG1): a critical review.The role of intrinsically disordered regions in the structure and functioning of small heat shock proteins.Cofilin weakly interacts with 14-3-3 and therefore can only indirectly participate in regulation of cell motility by small heat shock protein HspB6 (Hsp20).A posttranslational modification cascade involving p38, Tip60, and PRAK mediates oncogene-induced senescence.Facilitating cytokine-mediated cancer cell death by proteobacterial N-acylhomoserine lactonesCell surface 4-1BBL mediates sequential signaling pathways 'downstream' of TLR and is required for sustained TNF production in macrophages.The pivotal role of the beta 7 strand in the intersubunit contacts of different human small heat shock proteinsConversion of omnipotent translation termination factor eRF1 into ciliate-like UGA-only unipotent eRF1.Multiple activation mechanisms of p38alpha mitogen-activated protein kinase.Properties of the monomeric form of human 14-3-3ζ protein and its interaction with tau and HspB6.Phosphorylation of human small heat shock protein HspB8 (Hsp22) by ERK1 protein kinase.Heterooligomeric complexes formed by human small heat shock proteins HspB1 (Hsp27) and HspB6 (Hsp20).Structure and properties of K141E mutant of small heat shock protein HSP22 (HspB8, H11) that is expressed in human neuromuscular disordersThe problem of protein kinase activity of small heat shock protein Hsp22 (H11 or HspB8)Effect of mutations in the beta5-beta7 loop on the structure and properties of human small heat shock protein HSP22 (HspB8, H11)Effect of mutations mimicking phosphorylation on the structure and properties of human 14-3-3zetaPhosphomimicking mutations of human 14-3-3ζ affect its interaction with tau protein and small heat shock protein HspB6Commentary on paper: Small heat shock proteins and the cytoskeleton: an essential interplay for cell integrity? (Wettstein et al.).
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2000-01-01T00:00:00Z