about
sameAs
Heterozygous yeast deletion collection screens reveal essential targets of Hsp90Proteostatic control of telomerase function through TRiC-mediated folding of TCAB1State of the science: an update on renal cell carcinomaMechanism of folding chamber closure in a group II chaperoninThe predicted structure of the headpiece of the Huntingtin protein and its implications on Huntingtin aggregationMisfolded proteins partition between two distinct quality control compartmentsSorting out the trash: the spatial nature of eukaryotic protein quality controlThe dynamic conformational cycle of the group I chaperonin C-termini revealed via molecular dynamics simulation4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangementCrystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding CycleDual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin ChamberCryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure.Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle.Mechanism of nucleotide sensing in group II chaperoninsThe molecular architecture of the eukaryotic chaperonin TRiC/CCTMechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets.A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesisSystems analyses reveal two chaperone networks with distinct functions in eukaryotic cells.Systematic functional prioritization of protein posttranslational modifications.Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologiesParkinson's disease genes VPS35 and EIF4G1 interact genetically and converge on α-synucleinHsp90 inhibitors exhibit resistance-free antiviral activity against respiratory syncytial virusThe structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCTxTract: software for characterizing conformational changes of protein complexes by quantitative cross-linking mass spectrometryCellular inclusion bodies of mutant huntingtin exon 1 obscure small fibrillar aggregate species.Exogenous delivery of chaperonin subunit fragment ApiCCT1 modulates mutant Huntingtin cellular phenotypesSpatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress.Super-resolution fluorescence of huntingtin reveals growth of globular species into short fibers and coexistence of distinct aggregatesDelayed emergence of subdiffraction-sized mutant huntingtin fibrils following inclusion body formation.The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis.The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions.Interplay between chaperones and protein disorder promotes the evolution of protein networks.Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexesDefining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes.Action of the chaperonin GroEL/ES on a non-native substrate observed with single-molecule FRET.Trivalent arsenic inhibits the functions of chaperonin complex.Cellular strategies of protein quality control.Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy.Tracheostomy and mechanical ventilation weaning in children affected by respiratory virus according to a weaning protocol in a pediatric intensive care unit in Argentina: an observational restrospective trialModulation of STAT3 folding and function by TRiC/CCT chaperonin.
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P50
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geneticist
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wetenschapper
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Judith Frydman
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Judith Frydman
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Judith Frydman
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Judith Frydman
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Judith Frydman
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Judith Frydman
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Judith Frydman
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Judith Frydman
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Judith Frydman
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Judith Frydman
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Judith Frydman
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Judith Frydman
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