The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer
about
Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.Dynamic Complexes in the Chaperonin-Mediated Protein Folding CycleChaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteinsProteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasisChlamydia trachomatis infection and anti-Hsp60 immunity: the two sides of the coinMinimal and optimal mechanisms for GroE-mediated protein foldingHuman Hsp60 with its mitochondrial import signal occurs in solution as heptamers and tetradecamers remarkably stable over a wide range of concentrations.Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional formMeta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells.Identification of elements that dictate the specificity of mitochondrial Hsp60 for its co-chaperonin.GroES in the asymmetric GroEL14-GroES7 complex exchanges via an associative mechanism.Heat shock protein 10 (Hsp10) in immune-related diseases: one coin, two sides.Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle.Sequential action of ATP-dependent subunit conformational change and interaction between helical protrusions in the closure of the built-in lid of group II chaperonins.Catalysis of protein folding by symmetric chaperone complexes.Evidence for a lipochaperonin: association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions.Asymmetry of the GroEL-GroES complex under physiological conditions as revealed by small-angle x-ray scattering.GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATPSubstrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange.Symmetric GroEL:GroES2 complexes are the protein-folding functional form of the chaperonin nanomachineRevisiting the GroEL-GroES reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant.GroEL-mediated protein folding.Single-molecule study on the decay process of the football-shaped GroEL-GroES complex using zero-mode waveguides.Hydrolysable ATP is a requirement for the correct interaction of molecular chaperonins cpn60 and cpn10Probing open conformation of GroEL rings by cross-linking reveals single and double open ring structures of GroEL in ADP and ATP.Single-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes.Denatured proteins facilitate the formation of the football-shaped GroEL-(GroES)2 complex.The effect of nucleotides and mitochondrial chaperonin 10 on the structure and chaperone activity of mitochondrial chaperonin 60.Physicochemical Properties of the Mammalian Molecular Chaperone HSP60.On the Role of Symmetrical and Asymmetrical Chaperonin Complexes in Assisted Protein FoldingGroEL under Heat-ShockEffects of the Inter-ring Communication in GroEL Structural and Functional Asymmetry
P2860
Q27929741-FDC05871-2A38-48B5-80CE-6B587A1B09CBQ28068764-C24058E6-B87A-4212-8C45-993914E8B8EEQ28074574-6604D95C-1D56-4BDE-9046-D42A0DD37999Q28286034-F5A1706A-C042-4E4A-BBC8-DBB6050A54CAQ33497914-F77D8647-5048-4023-9550-14F50673ABD1Q33578079-F11BC60F-9AD8-4AE9-AE3D-EF393C3E1F41Q33618484-C761B0C8-257C-4A7E-8B38-2A47345953D5Q34144755-3B443FB9-F659-4FD8-A83D-A421F018ABEEQ34505905-942852C4-047B-4B71-9EE0-24D835A395B9Q34506502-00F5D21B-6DFC-48B3-859E-FA53388C0911Q35058728-AC3D246A-F456-4895-BFBE-E19E16A8500FQ35232223-A16C0970-5D75-4848-83AA-F56E5AC2DE2CQ35676628-62C224FE-2090-4C9A-91FB-810A06143B5BQ35676893-AEFADC09-CD48-4D8B-821B-5AB107EA5136Q35987874-539AFEF3-E8D5-4506-977B-61D286FB467DQ36033850-4AE2F84C-26E1-41F2-95A8-6E77FB9CE255Q36402302-9452AF20-7DD3-4BC8-9C11-F0D8E9F92BB4Q36820063-AC5C0A57-2E35-4D76-854C-2BD401DF8A56Q37319595-AABB24EF-E19F-4767-9E54-014B491D6A0AQ37319749-761A5EF9-ACC7-47F1-A898-869112ECC36CQ40452290-322CFFCE-8CF9-487B-BBEB-D278D113B20EQ41429098-DEFFEB32-09B1-4B25-A5E5-573F094FE8A9Q41891998-A0458FC1-3CD5-4E1D-9ABB-4DA0C4F5B50DQ41968619-868C720D-F9A2-4E14-A8DA-8219DA3AE7FDQ42022214-2894AE43-071D-4FC0-99BF-043992860C95Q42118511-EBC8DB67-DAA1-4D59-A9B3-559DBF6D39DAQ43178484-9F00AD3E-FB68-478E-A7A0-BA438D5B31A1Q43650854-BBEC1AF1-EB0B-4E5B-BBF4-72399B5BC060Q50131809-DD5E65EA-1CED-41DB-90E6-CE4140D3595FQ58007392-ABD286A9-6D8A-4494-8CE3-A445978DE922Q58660250-2E4BA358-9160-49A8-AF4A-DF0F545B5DC4Q58660258-AC8AA488-D59E-4CB7-8203-13994C46E279
P2860
The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer
description
1995 nî lūn-bûn
@nan
1995 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
The protein-folding activity o ...... roEL14(GroES7)2 heterooligomer
@ast
The protein-folding activity o ...... roEL14(GroES7)2 heterooligomer
@en
type
label
The protein-folding activity o ...... roEL14(GroES7)2 heterooligomer
@ast
The protein-folding activity o ...... roEL14(GroES7)2 heterooligomer
@en
prefLabel
The protein-folding activity o ...... roEL14(GroES7)2 heterooligomer
@ast
The protein-folding activity o ...... roEL14(GroES7)2 heterooligomer
@en
P2093
P2860
P356
P1476
The protein-folding activity o ...... roEL14(GroES7)2 heterooligomer
@en
P2093
P2860
P304
12021-12025
P356
10.1073/PNAS.92.26.12021
P407
P577
1995-12-01T00:00:00Z