Small heat-shock proteins: important players in regulating cellular proteostasis.
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The role of the ribosome in the regulation of longevity and lifespan extensionInteraction of HSP20 with a viral RdRp changes its sub-cellular localization and distribution pattern in plants.Structural insights into functional amyloid inhibition in Gram -ve bacteriaDopamine signaling promotes the xenobiotic stress response and protein homeostasisCharacterization of Mutants of Human Small Heat Shock Protein HspB1 Carrying Replacements in the N-Terminal Domain and Associated with Hereditary Motor Neuron DiseasesHSP70 regulates the function of mitotic centrosomesStructural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity.Biophysical chemistry of the ageing eye lens.αB-crystallin is a sensor for assembly intermediates and for the subunit topology of desmin intermediate filaments.Proline isomerization in the C-terminal region of HSP27.αB-crystallin: Portrait of a malignant chaperone as a cancer therapeutic targetSmall heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding.Tat-HSP22 inhibits oxidative stress-induced hippocampal neuronal cell death by regulation of the mitochondrial pathwayDrosophila melanogaster Hsp22: a mitochondrial small heat shock protein influencing the aging process.Medical implications of understanding the functions of human small heat shock proteins.A novel p.T139M mutation in HSPB1 highlighting the phenotypic spectrum in a family.Walking the tightrope: proteostasis and neurodegenerative disease.Expanding role of molecular chaperones in regulating α-synuclein misfolding; implications in Parkinson's disease.Small heat shock proteins in ageing and age-related diseases.Proteostasis and Diseases of the Motor Unit.The growing world of small heat shock proteins: from structure to functions.The chloroplast-localized small heat shock protein Hsp21 associates with the thylakoid membranes in heat-stressed plants.Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils.The heat shock response in neurons and astroglia and its role in neurodegenerative diseases.Using bicistronic constructs to evaluate the chaperone activities of heat shock proteins in cells.Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of AggregationHspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.Role of salt bridges in the dimer interface of 14-3-3ζ in dimer dynamics, N-terminal α-helical order, and molecular chaperone activity.Chaperone-client interactions between Hsp21 and client proteins monitored in solution by small angle X-ray scattering and captured by crosslinking mass spectrometry.Characterization of human small heat shock protein HSPB1 α-crystallin domain localized mutants associated with hereditary motor neuron diseases.Stress-Activated Chaperones: A First Line of Defense.The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity.A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins.Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding.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 influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin.Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface.7B2 chaperone knockout in APP model mice results in reduced plaque burden.
P2860
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P2860
Small heat-shock proteins: important players in regulating cellular proteostasis.
description
2014 nî lūn-bûn
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2014年の論文
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年學術文章
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name
Small heat-shock proteins: important players in regulating cellular proteostasis.
@en
type
label
Small heat-shock proteins: important players in regulating cellular proteostasis.
@en
prefLabel
Small heat-shock proteins: important players in regulating cellular proteostasis.
@en
P2860
P1476
Small heat-shock proteins: important players in regulating cellular proteostasis.
@en
P2093
Sarah Meehan
Teresa M Treweek
P2860
P2888
P304
P356
10.1007/S00018-014-1754-5
P577
2014-10-29T00:00:00Z