about
Effect of TBCD and its regulatory interactor Arl2 on tubulin and microtubule integrityHuman TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitroProteostatic control of telomerase function through TRiC-mediated folding of TCAB1An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptorsActivities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organisationModel systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicityThe concept of allosteric interaction and its consequences for the chemistry of the brainWhat distinguishes GroEL substrates from other Escherichia coli proteins?Structural 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 simulationATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangementThe crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperoninsDefining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologiesP. falciparum cpn20 is a bona fide co-chaperonin that can replace GroES in E. coliDynamic Complexes in the Chaperonin-Mediated Protein Folding CycleChaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteinsHistoplasma capsulatum heat-shock 60 orchestrates the adaptation of the fungus to temperature stressRevealing the functions of the transketolase enzyme isoforms in Rhodopseudomonas palustris using a systems biology approachCCT chaperonin complex is required for efficient delivery of anthrax toxin into the cytosol of host cellsxTract: software for characterizing conformational changes of protein complexes by quantitative cross-linking mass spectrometryThe cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domainsCoherent conformational degrees of freedom as a structural basis for allosteric communication.Stress response in tardigrades: differential gene expression of molecular chaperonesUCSF Chimera, MODELLER, and IMP: an integrated modeling system.Chaperonins facilitate KNOTTED1 cell-to-cell trafficking and stem cell function.The chaperonin CCT8 facilitates spread of tobamovirus infectionChaperonin contributes to cold hardiness of the onion maggot Delia antiqua through repression of depolymerization of actin at low temperatures.Crystallization and preliminary X-ray crystallographic analysis of the XoGroEL chaperonin from Xanthomonas oryzae pv. oryzae.An in vivo RNA interference screen identifies gene networks controlling Drosophila melanogaster blood cell homeostasisAnalysis of chaperone mRNA expression in the adult mouse brain by meta analysis of the Allen Brain Atlas.The minimal proteome in the reduced mitochondrion of the parasitic protist Giardia intestinalis.A chaperonin subunit with unique structures is essential for folding of a specific substrate.Single-molecule fluorescence polarization study of conformational change in archaeal group II chaperonin.Protein folding in the cytoplasm and the heat shock response.Functional chromatography reveals three natural products that target the same protein with distinct mechanisms of action.Caenorhabditis elegans chaperonin CCT/TRiC is required for actin and tubulin biogenesis and microvillus formation in intestinal epithelial cellsArchaeal-like chaperonins in bacteria.Inactivation of the hereditary spastic paraplegia-associated Hspd1 gene encoding the Hsp60 chaperone results in early embryonic lethality in mice.Coevolution analyses illuminate the dependencies between amino acid sites in the chaperonin system GroES-L.
P2860
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P2860
description
2007 nî lūn-bûn
@nan
2007 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Two families of chaperonin: physiology and mechanism.
@ast
Two families of chaperonin: physiology and mechanism.
@en
Two families of chaperonin: physiology and mechanism.
@nl
type
label
Two families of chaperonin: physiology and mechanism.
@ast
Two families of chaperonin: physiology and mechanism.
@en
Two families of chaperonin: physiology and mechanism.
@nl
prefLabel
Two families of chaperonin: physiology and mechanism.
@ast
Two families of chaperonin: physiology and mechanism.
@en
Two families of chaperonin: physiology and mechanism.
@nl
P2093
P1476
Two families of chaperonin: physiology and mechanism.
@en
P2093
Eli Chapman
George W Farr
Wayne A Fenton
P304
P356
10.1146/ANNUREV.CELLBIO.23.090506.123555
P577
2007-01-01T00:00:00Z