The crystal structure of the bacterial chaperonin GroEL at 2.8 A
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The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coliHuman TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitroNMR characterization of the interaction of GroEL with amyloid β as a model ligandNucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludisElucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes.Crystal structure at 2.6-A resolution of human macrophage migration inhibitory factorMechanism of folding chamber closure in a group II chaperoninChaperonin-mediated folding of actin and tubulinThe effect of macromolecular crowding on chaperonin-mediated protein foldingMolecular chaperones: guardians of the proteome in normal and disease statesDynamics, flexibility and ligand-induced conformational changes in biological macromolecules: a computational approachChaperone machines for protein folding, unfolding and disaggregationStructural Mechanisms of Mutant Huntingtin Aggregation Suppression by the Synthetic Chaperonin-like CCT5 Complex Explained by Cryoelectron Tomography.The dynamic conformational cycle of the group I chaperonin C-termini revealed via molecular dynamics simulationGroEL2 of Mycobacterium tuberculosis Reveals the Importance of Structural Pliability in Chaperonin Function.Conformational sampling and nucleotide-dependent transitions of the GroEL subunit probed by unbiased molecular dynamics simulationsPerturbation-based Markovian transmission model for probing allosteric dynamics of large macromolecular assembling: a study of GroEL-GroESAutotracing of Escherichia coli acetate CoA-transferase alpha-subunit structure using 3.4 A MAD and 1.9 A native dataPurification, crystallization and structure determination of native GroEL fromEscherichia colilacking bound potassium ionsCrystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding CycleStructural and Functional Conservation of Mycobacterium tuberculosis GroEL Paralogs Suggests that GroEL1 Is a ChaperoninCrystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulinChaperonins from an Antarctic archaeon are predominantly monomeric: crystal structure of an open state monomerSymmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle.ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL ChaperoninVisualizing GroEL/ES in the Act of Encapsulating a Folding ProteinDiamonds in the rough: a strong case for the inclusion of weak-intensity X-ray diffraction dataA plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active siteConformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolutionLigand-induced distortion of an active site in thymidylate synthase upon binding anticancer drug 1843U89Interplay of structure and disorder in cochaperonin mobile loopsCrystal structures of a single coiled-coil peptide in two oligomeric states reveal the basis for structural polymorphismChaperone activity and structure of monomeric polypeptide binding domains of GroELA structural model for GroEL-polypeptide recognitionA molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperoneCrystal structure of a small heat-shock proteinSignificance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10.The Saccharomyces cerevisiae TCM62 gene encodes a chaperone necessary for the assembly of the mitochondrial succinate dehydrogenase (complex II).Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle
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P2860
The crystal structure of the bacterial chaperonin GroEL at 2.8 A
description
1994 nî lūn-bûn
@nan
1994 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
The crystal structure of the bacterial chaperonin GroEL at 2.8 A
@ast
The crystal structure of the bacterial chaperonin GroEL at 2.8 A
@en
The crystal structure of the bacterial chaperonin GroEL at 2.8 A
@nl
type
label
The crystal structure of the bacterial chaperonin GroEL at 2.8 A
@ast
The crystal structure of the bacterial chaperonin GroEL at 2.8 A
@en
The crystal structure of the bacterial chaperonin GroEL at 2.8 A
@nl
prefLabel
The crystal structure of the bacterial chaperonin GroEL at 2.8 A
@ast
The crystal structure of the bacterial chaperonin GroEL at 2.8 A
@en
The crystal structure of the bacterial chaperonin GroEL at 2.8 A
@nl
P2093
P3181
P356
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P1476
The crystal structure of the bacterial chaperonin GroEL at 2.8 A
@en
P2093
P2888
P304
P3181
P356
10.1038/371578A0
P407
P577
1994-10-13T00:00:00Z
P5875
P6179
1022157325