Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity.
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Proline isomerization in the C-terminal region of HSP27.A novel molecular dynamics approach to evaluate the effect of phosphorylation on multimeric protein interface: the αB-Crystallin case study.Multi-kinase inhibitors can associate with heat shock proteins through their NH2-termini by which they suppress chaperone functionSpasmolytic Mechanism of Aqueous Licorice Extract on Oxytocin-Induced Uterine Contraction through Inhibiting the Phosphorylation of Heat Shock Protein 27.Heat shock protein-27 (HSP27) regulates STAT3 and eIF4G levels in first trimester human placenta.Therapeutic Strategies for Restoring Tau Homeostasis.The C-terminal extension of Mycobacterium tuberculosis Hsp16.3 regulates its oligomerization, subunit exchange dynamics and chaperone function.Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of AggregationBAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins.pH-dependent structural modulation is conserved in the human small heat shock protein HSBP1.HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.Characterization of human small heat shock protein HSPB1 α-crystallin domain localized mutants associated with hereditary motor neuron diseases.The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity.The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins.Chaperone activity of human small heat shock protein-GST fusion proteins.The Chaperone Activity and Substrate Spectrum of Human Small Heat Shock Proteins.Mild systemic thermal therapy ameliorates renal dysfunction in a rodent model of chronic kidney disease.Increased expression of phosphorylated forms of heat-shock protein-27 and p38MAPK in macrophage-rich regions of fibro-fatty atherosclerotic lesions in the rabbit.The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin.Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau
P2860
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P2860
Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年学术文章
@wuu
2015年学术文章
@zh-cn
2015年学术文章
@zh-hans
2015年学术文章
@zh-my
2015年学术文章
@zh-sg
2015年學術文章
@yue
2015年學術文章
@zh
2015年學術文章
@zh-hant
name
Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity.
@en
type
label
Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity.
@en
prefLabel
Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity.
@en
P2093
P50
P1476
Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity.
@en
P2093
Anthea P Rote
Heidi Y Gastall
J Andrew Aquilina
Megan A Kelly
Tracey Berg
P304
P356
10.1016/J.CHEMBIOL.2015.01.001
P577
2015-02-01T00:00:00Z