About: HSPB5 engages multiple states of a destabilized client to enhance chaperone activity in a stress-dependent manner

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About: HSPB5 engages multiple states of a destabilized client to enhance chaperone activity in a stress-dependent manner Goto Sponge NotDistinct Permalink

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scientific article published on 19 December 2018

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в грудні 2018 (uk) article scientifique publié en 2018 (fr) artículu científicu espublizáu n'avientu de 2018 (ast) scientific article published on 19 December 2018 (en)
publication date	wds:Q90644576-B1B765B0-0794-422E-A8CE-C6BA210A4CAE
publication date	2018-12-19 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q90644576-72A1DE29-FCA4-47D0-86D5-B5BB488538B3
language of work or name	English
cites work	wds:Q90644576-02B96A63-A56B-42D5-85E6-F77543AFB0BE wds:Q90644576-0789071E-B9D6-4F8B-8828-DC5F9E52CB29 wds:Q90644576-125418D7-34D5-4171-9FA3-D54895FB19C1 wds:Q90644576-15E013FE-252F-490E-ABE3-234505BE83DD wds:Q90644576-1696E37E-BB3C-4D06-8E8C-66C439A770C9 wds:Q90644576-1B3F7DAC-C2A1-4B7E-B214-3A17CD43ECCA wds:Q90644576-1E6D5E5D-2D34-481A-9D04-70496D4C2EA8 wds:Q90644576-238CC33E-AB68-4CB4-A4F7-A23CF4D7E51A wds:Q90644576-2459D572-C230-4D28-B1E6-1A088260B3A9 wds:Q90644576-296523EF-4783-49BD-865C-BD7FB544B05D wds:Q90644576-29A3FB10-6303-4782-B073-A132357097BC wds:Q90644576-2A1A5101-6437-446D-971B-FAA01C5E491A wds:Q90644576-303A4214-2F50-4344-B7DB-8C25E5A62497 wds:Q90644576-396B3FAB-949A-4956-8782-BA79097FEBBC wds:Q90644576-3F9F19A9-133D-4780-8B5E-E22D2FB2375D wds:Q90644576-405A22E7-A657-428D-BEEF-3B22A6D8E169 wds:Q90644576-4C5C46A4-5E4B-4F4A-A5E1-12617DEDC666 wds:Q90644576-50E4A09E-9A75-429D-937B-3C8B4A509220 wds:Q90644576-5251FADD-4E05-4799-AD63-554A81025BD7 wds:Q90644576-587DD492-1F60-4B20-AD8D-799F8154CCD9 wds:Q90644576-5F7E68F1-40E5-4702-9C92-C6431F78E80A wds:Q90644576-747FA268-19E2-4FE3-A09E-B1F3A44AE6DE wds:Q90644576-859FF6BC-8735-4CE7-8D1F-9FFA77DACBEA wds:Q90644576-910A8124-302E-45E7-B5C6-6D31E736E316 wds:Q90644576-94554512-6A67-4065-8C24-DD933BDF756E wds:Q90644576-99BE882A-E6E7-4038-8697-FC4B58BE0971 wds:Q90644576-BF17B30C-3C59-4DE5-B3A1-3E40686BCE55 wds:Q90644576-C116E035-3ED5-437F-A309-881EE87BDA77 wds:Q90644576-D02B2358-8426-4731-BD87-239BBD0241C0 wds:Q90644576-DF2693E6-32D2-4A2B-9A7F-1DC2C5047A8C wds:Q90644576-ECAA0317-13A5-409F-AE5E-C2D852D8D493 wds:Q90644576-F512D813-6B0D-4FBF-A398-FA80294D2FA8 wds:Q90644576-FE0BF658-7EA5-4D32-A976-D7FCE57B14F4 wds:Q90644576-FE75FEEB-2098-442B-9180-F0AEF4EA8F6E
cites work	The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure The N-terminal arm of small heat shock proteins is important for both chaperone activity and substrate specificity Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motif A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy Crystal structure and assembly of a eukaryotic small heat shock protein Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomers Alpha-crystallin can function as a molecular chaperone Ser-59 is the major phosphorylation site in alphaB-crystallin accumulated in the brains of patients with Alexander's disease Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin Small heat shock proteins: a new classification scheme in mammals The IXI/V motif in the C-terminal extension of alpha-crystallins: alternative interactions and oligomeric assemblies Cytosolic beta-amyloid deposition and supranuclear cataracts in lenses from people with Alzheimer's disease The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine alpha-lactalbumin Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone Small heat shock proteins Hsp27 or alphaB-crystallin and the protein components of neurofibrillary tangles: tau and neurofilaments. Expression, purification, and molecular chaperone activity of plant recombinant small heat shock proteins Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in alphaB-crystallin A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state Mechanism of suppression of dithiothreitol-induced aggregation of bovine alpha-lactalbumin by alpha-crystallin αB-crystallin improves murine cardiac function and attenuates apoptosis in human endothelial cells exposed to ischemia-reperfusion Phosphorylation-induced change of the oligomerization state of alpha B-crystallin Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry αB-crystallin polydispersity is a consequence of unbiased quaternary dynamics. A Mechanism of Subunit Recruitment in Human Small Heat Shock Protein Oligomers Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis Small heat shock proteins and protein-misfolding diseases The Chaperone Activity of the Developmental Small Heat Shock Protein Sip1 Is Regulated by pH-Dependent Conformational Changes Compactness of the kinetic molten globule of bovine alpha-lactalbumin: a dynamic light scattering study pH-dependent structural modulation is conserved in the human small heat shock protein HSBP1. Small Heat Shock Proteins and Distal Hereditary Neuropathies The Chaperone Activity and Substrate Spectrum of Human Small Heat Shock Proteins. Transcriptional regulation of small HSP-HSF1 and beyond.
author name string	wds:Q90644576-65A56F59-3A89-4BED-8191-55D9061FB2E2
author name string	Scott P Delbecq
rdfs:label	HSPB5 engages multiple states of a destabilized client to enhance chaperone activity in a stress-dependent manner (en) HSPB5 engages multiple states of a destabilized client to enhance chaperone activity in a stress-dependent manner (nl)
skos:prefLabel	HSPB5 engages multiple states of a destabilized client to enhance chaperone activity in a stress-dependent manner (en) HSPB5 engages multiple states of a destabilized client to enhance chaperone activity in a stress-dependent manner (nl)
name	HSPB5 engages multiple states of a destabilized client to enhance chaperone activity in a stress-dependent manner (en) HSPB5 engages multiple states of a destabilized client to enhance chaperone activity in a stress-dependent manner (nl)
author	wds:Q90644576-4B49B0EF-1CE5-4111-B742-2A85C4CE2123
author	Rachel E. Klevit
title	wds:Q90644576-6DA5C825-1708-4527-929C-F7BCDB4268B2
title	HSPB5 engages multiple states of a destabilized client to enhance chaperone activity in a stress-dependent manner (en)
page(s)	wds:Q90644576-10EA3BA1-EFE1-4E7F-BB3E-C2CD5B4A23F0
page(s)	3261-3270
instance of	wds:Q90644576-CC912CBE-76FD-4864-84DE-06D398B5E4C9
instance of	scholarly article
PubMed ID	wds:Q90644576-F5D30E25-208C-4BF3-9E5D-9FB36734BC4A
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30567736
PubMed ID	30567736
published in	wds:Q90644576-754CA7B4-C093-4690-9BBF-C568F520C54D
published in	Journal of Biological Chemistry
issue	wds:Q90644576-3A98A618-701E-428A-87C2-BB9480A05756

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