About: Biochemical Characterization of Symmetric GroEL-GroES Complexes

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scientific article published in Journal of Biological Chemistry

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1996 (uk) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im Januar 1996 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q58660280-EFAEE851-F8E0-4857-A44C-7E71530345D6
publication date	1996-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q58660280-6AB5A7E5-507E-466B-8F89-11B36E9664DF
language of work or name	English
cites work	wds:Q58660280-001BE06A-B07D-4350-97B1-0F9400B465B8 wds:Q58660280-04EE9D5D-EB53-4BAE-A839-4B4B8610F94B wds:Q58660280-0D107794-44EF-426E-B961-4FA8DAA4E1F6 wds:Q58660280-157671B6-7D99-43E7-82C8-64CA314EA2C0 wds:Q58660280-1C048846-3DF2-4F4F-8448-16A5AB776186 wds:Q58660280-27DC7584-75D1-43A9-8EC5-F7E56D013AE6 wds:Q58660280-3FB01234-20B6-4B0B-BFEE-D477B79DF7FA wds:Q58660280-5E75BC4B-0322-4FC7-B79A-DD86F9CD731E wds:Q58660280-65D03FB1-F980-40F9-A6DB-B1BC36A0292A wds:Q58660280-817C02F2-22F4-40F6-B14D-C9F69235D36D wds:Q58660280-8BD432DE-B04A-4140-9752-C6D8FF2623A5 wds:Q58660280-8FA25F02-D32B-4315-8066-1ED216560227 wds:Q58660280-A6A20BE3-4433-43AF-A714-F5D1B9ADAD1B wds:Q58660280-BF10929C-4FF3-46B7-B3B9-C0FC1F981DB7 wds:Q58660280-C7831417-3AC6-4358-B5E5-73C476CAE79A wds:Q58660280-D9ADCE52-0CC4-40EE-B1AD-FD9564ACA1FE wds:Q58660280-DF2576AB-E6CD-49C1-BE27-4E5A9701EFCD wds:Q58660280-E9B338FA-52B9-4C19-BF2A-0C57698A04DA wds:Q58660280-F16928C4-137F-4CBB-AE2F-B6682E9B7737
cites work	Proteins as molecular chaperones. Molecular chaperones in cellular protein folding Regulation of insecticidal crystal protein production in Bacillus thuringiensis Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms The crystal structure of the bacterial chaperonin GroEL at 2.8 A Residues in chaperonin GroEL required for polypeptide binding and release Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding. Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes. The formation of symmetrical GroEL-GroES complexes in the presence of ATP. Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer Symmetric complexes of GroE chaperonins as part of the functional cycle The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes A polypeptide bound by the chaperonin groEL is localized within a central cavity Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion. Transmission electron microscopy of GroEL, GroES, and the symmetrical GroEL/ES complex. Stability of the asymmetric Escherichia coli chaperonin complex. Guanidine chloride causes rapid dissociation
author name string	wds:Q58660280-AB6EF3CB-5706-4498-9E73-91C3703080C9
author name string	J L Carrascosa
rdfs:label	Biochemical Characterization of Symmetric GroEL-GroES Complexes (en) Biochemical Characterization of Symmetric GroEL-GroES Complexes (nl)
skos:prefLabel	Biochemical Characterization of Symmetric GroEL-GroES Complexes (en) Biochemical Characterization of Symmetric GroEL-GroES Complexes (nl)
name	Biochemical Characterization of Symmetric GroEL-GroES Complexes (en) Biochemical Characterization of Symmetric GroEL-GroES Complexes (nl)
author	wds:Q58660280-719D9EFF-B8AA-43DC-8694-43402D549C1C wds:Q58660280-98C0FBCF-ABD9-4E48-9D5E-ED648406CB31
author	José María Valpuesta Oscar Llorca
title	wds:Q58660280-96BA2D63-7DC9-4697-A772-6F5DA49B0D98
title	Biochemical characterization of symmetric GroEL-GroES complexes. Evidence for a role in protein folding (en)
page(s)	wds:Q58660280-C498A081-FBC1-4970-8136-60FD2DB118A8
page(s)	68-76
instance of	wds:Q58660280-C15EA998-02F2-426B-ADB5-302ADE005105
instance of	scholarly article
PubMed ID	wds:Q58660280-D86E9EB6-9929-4D61-8D58-E16FC438693F
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8550627
PubMed ID	8550627
published in	wds:Q58660280-BAC6CBE4-5182-4BB4-B516-FAE9EAA87466
published in	Journal of Biological Chemistry
issue	wds:Q58660280-1D4D50D9-9C63-4B4C-8B7B-213C85AA7933
volume	wds:Q58660280-87684662-D7E0-47D9-A2D4-176EE7E5FB10
issue	1
volume	271
DOI	wds:Q58660280-7F80A13B-B0B2-4B9A-8DF5-7B3EF55AA58A
DOI	http://dx.doi.org/10.1074/JBC.271.1.68
DOI	10.1074/JBC.271.1.68
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q58660280
is cites work of	Alternating translocation of protein substrates from both ends of ClpXP protease Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60. Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin In vitro stabilization and in vivo solubilization of foreign proteins by the beta subunit of a chaperonin from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1. GroEL under Heat-Shock Effects of the Inter-ring Communication in GroEL Structural and Functional Asymmetry GroEL-mediated protein folding Role of the amino terminal domain in GroES oligomerization Catalysis of protein folding by symmetric chaperone complexes 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. Kinetic significance of GroEL14.(GroES7)2 complexes in molecular chaperone activity. On the Role of Symmetrical and Asymmetrical Chaperonin Complexes in Assisted Protein Folding ATP-driven molecular chaperone machines Structural comparison of prokaryotic and eukaryotic chaperonins. Putting a lid on protein folding: structure and function of the co-chaperonin, GroES. GroES binding regulates GroEL chaperonin activity under heat shock Hydrolysable ATP is a requirement for the correct interaction of molecular chaperonins cpn60 and cpn10 GroES in the asymmetric GroEL14-GroES7 complex exchanges via an associative mechanism

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