About: GroEL under Heat-Shock

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scientific article published in Journal of Biological Chemistry

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rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в грудні 1998 (uk) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im Dezember 1998 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q58660250-E74E9D6B-09D7-473A-85EC-5CE622953332
publication date	1998-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q58660250-D2CDF94C-4074-42A4-9EC2-514697C6B492
language of work or name	English
cites work	wds:Q58660250-02D0ABBE-D8BF-414D-95D4-83A2F8DB99A5 wds:Q58660250-047DF9DB-E2EF-4805-B17E-2BF0BC4B0973 wds:Q58660250-2AAE6ED0-30A7-4AAD-9C76-AC398B306798 wds:Q58660250-2E4BA358-9160-49A8-AF4A-DF0F545B5DC4 wds:Q58660250-2F5DC735-4E9D-4F35-9620-05B8DCF43717 wds:Q58660250-33C8CC98-8DFB-4BEB-8CB4-EDFA654E7CCF wds:Q58660250-36FA0845-9F7B-4863-ACDA-39903C0A0E24 wds:Q58660250-3DC9B1AD-F241-4F69-9FC6-A1D2F9801F1D wds:Q58660250-4300FC65-9790-453A-949C-543344B70080 wds:Q58660250-487449D6-1915-4652-A900-B65445E4E7DF wds:Q58660250-4F7911E0-AE69-4EBC-8CBC-9E47C8364747 wds:Q58660250-542695DF-BC6D-4658-95D4-439434ACE17D wds:Q58660250-5470B383-B01B-488C-A931-7608B43FAEFA wds:Q58660250-5A7A71E0-C92C-48FF-BE97-ED8B81503AE2 wds:Q58660250-667A65A5-7679-436A-8871-67A01FD2614B wds:Q58660250-689BBFFB-4E98-4A1C-BE9D-D9C342B89669 wds:Q58660250-72A5D8CF-BA4F-4BD1-A482-1AC2A7197DF0 wds:Q58660250-7A8798DC-04DB-4541-8125-7423EA7FA042 wds:Q58660250-7E319B97-3A23-41DB-B68A-3646339F96B7 wds:Q58660250-7EF1EFCA-8863-4530-9394-6A0E069C7CB9 wds:Q58660250-7F398E44-DBD4-45B1-9A0D-85EB297C7773 wds:Q58660250-982733CA-50AA-45FE-9417-24761B0636E0 wds:Q58660250-99F3940A-6B29-4CD1-9CED-424218C95A0B wds:Q58660250-9E8ED349-B0CF-41B2-8AEE-AED06ADCDB20 wds:Q58660250-9F285F97-CCAB-4EC2-9A18-A0FFAECC72E8 wds:Q58660250-A4E5FA0D-64D9-450E-BA4D-8408C570D8FB wds:Q58660250-B2428386-DF1A-4E47-8249-694CF3A1660E wds:Q58660250-B2FCB22F-F547-4C35-8953-E02340E2B540 wds:Q58660250-B943939E-C11F-47FC-B063-C5D838D2D7BD wds:Q58660250-CB7A2420-7158-4DA0-AFDF-058C483C40F0 wds:Q58660250-DBE96B17-4DB8-4C39-8506-6B538CB5953D wds:Q58660250-E8755325-0CAF-4191-8565-EB0AFE229C7A wds:Q58660250-F43BE6E0-2FA9-472C-90DF-2B0A9D19CB45 wds:Q58660250-F6A5BDEE-4A70-42E3-86BD-CDA2F54799CF
cites work	The Hsp70 and Hsp60 chaperone machines 9 Escherichia coli phage T4 topoisomerase A variant to the “random approximation” of the reference-free alignment algorithm Xmipp: An Image Processing Package for Electron Microscopy The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Protein folding in the central cavity of the GroEL-GroES chaperonin complex 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 asymmetric GroEL-GroES-(ADP)7 chaperonin complex Prevention of protein denaturation under heat stress by the chaperonin Hsp60 Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Three-dimensional reconstruction of single particles embedded in ice The crystal structure of the bacterial chaperonin GroEL at 2.8 A Residues in chaperonin GroEL required for polypeptide binding and release A new resolution criterion based on spectral signal-to-noise ratios Pattern recognition and classification of images of biological macromolecules using artificial neural networks Conformational changes in the GroEL oligomer during the functional cycle. Effects of the Inter-ring Communication in GroEL Structural and Functional Asymmetry The crystal structure of the GroES co-chaperonin at 2.8 Å resolution Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. 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 Biochemical Characterization of Symmetric GroEL-GroES Complexes The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer Symmetric GroEL-GroES complexes can contain substrate simultaneously in both GroEL rings Inter-ring communication is disrupted in the GroEL mutant Arg13 --> Gly; Ala126 --> Val with known crystal structure. GroES binding regulates GroEL chaperonin activity under heat shock The ATPase activity of chaperonin GroEL is highly stimulated at elevated temperatures. Release of both native and non-native proteins from a cis-only GroEL ternary complex. An arabinose-inducible expression vector, pAR3, compatible with ColE1-derived plasmids. Confidence limits for resolution estimation in image averaging by random subsampling Conditions of forming protein complexes with GroEL can influence the mechanism of chaperonin-assisted refolding.
author name string	wds:Q58660250-1902C775-1A9E-4C56-8BA7-12CE9B0688CC wds:Q58660250-3DBA5121-DBA0-4DD4-8192-C84B3B49DC9C
author name string	J L Carrascosa A Galán
rdfs:label	GroEL under Heat-Shock (en) GroEL under Heat-Shock (nl)
skos:prefLabel	GroEL under Heat-Shock (en) GroEL under Heat-Shock (nl)
name	GroEL under Heat-Shock (en) GroEL under Heat-Shock (nl)
author	wds:Q58660250-58D28F0B-7972-4A7F-8359-DB0B22CD8720 wds:Q58660250-596D43C1-86C6-4FCE-A43E-17304D5201C1 wds:Q58660250-BBA011B3-2249-4893-A6EC-CE31D3B7BAD3
author	José María Valpuesta Oscar Llorca Arturo Muga
title	wds:Q58660250-FA8F26DA-2D64-4912-A71D-32E0C79D7CE0
title	GroEL under heat-shock. Switching from a folding to a storing function (en)
page(s)	wds:Q58660250-31FD3FE7-726B-4B54-B9D2-3DAB74E4ADAA
page(s)	32587-32594
instance of	wds:Q58660250-F745D4AC-7559-485B-8FF1-E76D2AAF4CEC

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