Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin.
about
Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG In vivoNeuropathy- and myopathy-associated mutations in human small heat shock proteins: Characteristics and evolutionary history of the mutation sitesMultiple molecular architectures of the eye lens chaperone B-crystallin elucidated by a triple hybrid approachCrystal structure of a small heat-shock proteinPhe71 is essential for chaperone-like function in alpha A-crystallinA novel mechanism for small heat shock proteins to function as molecular chaperones.The expanding family of Arabidopsis thaliana small heat stress proteins and a new family of proteins containing alpha-crystallin domains (Acd proteins)Methionine sulfoxidation of the chloroplast small heat shock protein and conformational changes in the oligomer.Chaperone function of mutant versions of alpha A- and alpha B-crystallin prepared to pinpoint chaperone binding sites.Deamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin.Anti-chaperone betaA3/A1(102-117) peptide interacting sites in human alphaB-crystallinA small heat shock protein enables Escherichia coli to grow at a lethal temperature of 50°C conceivably by maintaining cell envelope integrity.Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation.Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.Characterization of alpha-crystallin-plasma membrane bindingRegulation and mechanism of action of the small heat shock protein from the hyperthermophilic archaeon Pyrococcus furiosus.Structural and functional roles of deamidation of N146 and/or truncation of NH2- or COOH-termini in human αB-crystallin.The Gln32Lys polymorphism in HSP22 of Zhikong scallop Chlamys farreri is associated with heat tolerance.Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humansRecognition between flexible protein molecules: induced and assisted folding.Small heat-shock proteins regulate membrane lipid polymorphism.The function of the beta3 interactive domain in the small heat shock protein and molecular chaperone, human alphaB crystallinDissecting the functional role of the N-terminal domain of the human small heat shock protein HSPB6.ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin.Analysis of the alphaB-crystallin domain responsible for inhibiting tubulin aggregationA novel alphaB-crystallin mutation associated with autosomal dominant congenital lamellar cataract.Spectral contribution of the individual tryptophan of alphaB-crystallin: a study by site-directed mutagenesisNovel roles for α-crystallins in retinal function and disease.Alpha-crystallin-derived peptides as therapeutic chaperones.Effect of N-terminal region of nuclear Drosophila melanogaster small heat shock protein DmHsp27 on function and quaternary structure.Small heat shock protein IbpB acts as a robust chaperone in living cells by hierarchically activating its multi-type substrate-binding residues.Conformational and functional differences between recombinant human lens alphaA- and alphaB-crystallin.Molecular characterization of a small heat shock/alpha-crystallin protein in encysted Artemia embryos.Mini-alphaB-crystallin: a functional element of alphaB-crystallin with chaperone-like activityA novel mutation in CRYAB associated with autosomal dominant congenital nuclear cataract in a Chinese familyCOOH-terminal truncations and site-directed mutations enhance thermostability and chaperone-like activity of porcine alphaB-crystallin.Truncation of alphaB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells.Effect of mutations of murine lens alphaB crystallin on transfected neural cell viability and cellular translocation in response to stress.Differences in properties between human alphaA- and alphaB-crystallin proteins expressed in Escherichia coli cells in response to cold and extreme pH.Insights into the domains required for dimerization and assembly of human alphaB crystallin.
P2860
Q24521559-4AD18D2C-0F58-4C38-AFCB-C1540EA6B4EAQ27022895-3D017087-37A8-4161-984F-85FE1C5694BCQ27675996-8636D329-65E0-4EDA-BE3D-B970FDC6B9BBQ27765131-C7850156-7527-4BD2-812B-7C7AB29E7530Q28579431-7685A9B1-1EB4-473D-90EC-8B006D27F752Q30625248-F232B687-7302-4848-9864-9C2FE416D811Q30662404-8A521689-C832-429B-AA93-741BBF703B41Q30826956-F2D269A2-003A-4829-A47A-51E96359DB5AQ31897258-AADED1BE-78B1-4823-997E-7E823524E009Q33205334-706CFFD8-D1C4-4337-9849-701B1066BB44Q33327497-8838265C-9D3F-4F05-8DD0-BE6CB954B0BEQ33570139-E80AC828-C126-4D96-880A-04D60058D983Q33935094-711A03B2-0D71-49A3-88E6-45320209E7B1Q33969470-2555F961-CE40-4E04-9142-152D31EFCFE0Q33989106-ACED13A2-7DB4-4CE8-885A-C53943370F1DQ33996779-45B08871-2A02-4176-A3E0-44A5C983971DQ34041520-97F63764-BC1E-44BC-9C14-F80948C5BC3CQ34097680-CBBD1735-0244-4CF0-97E1-F9ED03427348Q34113048-0938F569-A143-4022-A30B-A1F01D6EF9BDQ34141716-F392171D-C58C-49E8-BCD2-404B29389E04Q34159787-636D320B-5CBE-4970-8197-4A4FF18BE629Q34703688-AB68E6EA-BDA6-4AEF-B2E1-478159C9059CQ35231840-7253BB60-3CCE-43C3-BA2F-4384E8D1CFD2Q35782226-F2DEFCAD-A303-4844-A8AD-0E2516216248Q35942239-7FADD1F9-5947-4AB7-8EBE-BAB187018F57Q36145661-38451649-3DC2-4296-BAB8-7F790F5812BDQ36281400-3EB464E2-52AA-4FAA-B3DD-F402F7A6F8E4Q36319594-F8010B01-3D76-4E95-91A1-D9FC644D9574Q36355484-3FA6D0B2-C662-4B46-80EE-AC112B259E71Q36375609-93A03E12-543B-404B-982D-E101E88888A0Q36796832-D7347B93-AFB7-48A9-87DE-BF72F67BFC44Q36847889-8F8CFFBC-9523-43F8-B342-C822B5A83A5FQ36871688-28191EF0-325C-49E1-85A3-58575CA80538Q37042024-5EB920BA-0233-475C-848E-200F01BA73D6Q37258687-58BD09A9-EBBE-413D-9C64-D4B9436D167FQ37278346-94891B0C-B1F3-40C5-ADA4-51FF98D9855CQ39783049-A6B71AD9-97F0-49CC-8D29-568501ACEF2AQ40994033-74D11EDC-BF45-4DBE-9247-9A5CCFA5FF27Q41830926-97561C14-B4FA-4D66-8A5C-A5FDEBB8E436Q41831099-3A844555-844B-4FF4-AB18-BD5C4E467E9E
P2860
Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin.
@en
Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin.
@nl
type
label
Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin.
@en
Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin.
@nl
prefLabel
Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin.
@en
Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin.
@nl
P2093
P2860
P356
P1476
Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin.
@en
P2093
P2860
P304
28558-28566
P356
10.1074/JBC.271.45.28558
P407
P577
1996-11-01T00:00:00Z