Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form - Wikidata - wikimedia - TriplyDB

Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form

Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form

http://www.wikidata.org/entity/Q34144755

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Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity Bridging between NMA and Elastic Network Models: Preserving All-Atom Accuracy in Coarse-Grained Models Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle Chaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteins Dynamics, flexibility, and allostery in molecular chaperonins GroEL actively stimulates folding of the endogenous substrate protein PepQ Crystal structure of the human mitochondrial chaperonin symmetrical football complex.Structural insight into the cooperation of chloroplast chaperonin subunits.Accurate optimization of amino acid form factors for computing small-angle X-ray scattering intensity of atomistic protein structures.The human mitochondrial Hsp60 in the APO conformation forms a stable tetradecameric complex.The chaperone toolbox at the single-molecule level: From clamping to confining.A Helping Hand to Overcome Solubility Challenges in Chemical Protein Synthesis.Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction.Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein.Functional divergence of chloroplast Cpn60α subunits during Arabidopsis embryo development.HSP60 possesses a GTPase activity and mediates protein folding with HSP10.Disassembly/reassembly strategy for the production of highly pure GroEL, a tetradecameric supramolecular machine, suitable for quantitative NMR, EPR and mutational studies.Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein.Chaperonin of Group I: Oligomeric Spectrum and Biochemical and Biological Implications.Chloroplast Chaperonin: An Intricate Protein Folding Machine for Photosynthesis.A Glimpse Into the Structure and Function of Atypical Type I Chaperonins.The GroEL chaperonin: a protein machine with pistons driven by ATP binding and hydrolysis.Quaternary structures of GroEL and naïve-Hsp60 chaperonins in solution: a combined SAXS-MD study

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Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form

http://www.wikidata.org/entity/Q34144755

description

2014 nî lūn-bûn

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2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի օգոստոսին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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Formation and structures of Gr ...... rotein-folding functional form

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PNAS.1412922111

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Proceedings of the National Academy of Sciences of the United States of America

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Formation and structures of Gr ...... rotein-folding functional form

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George H Lorimer

http://www.w3.org/2001/XMLSchema#string

Nicole A LaRonde

http://www.w3.org/2001/XMLSchema#string

Xue Fei

http://www.w3.org/2001/XMLSchema#string

P2860

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 A resolution

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

Inference of macromolecular assemblies from crystalline state

The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer

Chaperonin-mediated protein folding.

Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle.

Catalysis of protein folding by symmetric chaperone complexes.

Allosteric regulation of chaperonins.

GroEL-mediated protein folding: making the impossible, possible.

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12775-12780

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scholarly article

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10.1073/PNAS.1412922111

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35

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111

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2014-08-18T00:00:00Z

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25136110

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protein folding

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4156775

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