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Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

http://www.wikidata.org/entity/Q27683688

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Facilitating unambiguous NMR assignments and enabling higher probe density through selective labeling of all methyl containing amino acids Structural basis for the antifolding activity of a molecular chaperone The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosome Substrate-binding domain conformational dynamics mediate Hsp70 allostery Information processing in the CNS: a supramolecular chemistry?Capturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular Modeling Efficient production of (2)H, (13)C, (15)N-enriched industrial enzyme Rhizopus chinensis lipase with native disulfide bonds.15N and 13C- SOFAST-HMQC editing enhances 3D-NOESY sensitivity in highly deuterated, selectively [1H,13C]-labeled proteins.F 1 F 2-selective NMR spectroscopy.Rotational restriction of nascent peptides as an essential element of co-translational protein folding: possible molecular players and structural consequences.Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme.Multitasking SecB chaperones in bacteria Dimeric Structure of the Bacterial Extracellular Foldase PrsA.The Trigger Factor Chaperone Encapsulates and Stabilizes Partial Folds of Substrate Proteins.Assignment of methyl NMR resonances of a 52 kDa protein with residue-specific 4D correlation maps.Mapping the conformation of a client protein through the Hsp70 functional cycle.HdeB chaperone activity is coupled to its intrinsic dynamic properties.Conformational dynamics of bacterial trigger factor in apo and ribosome-bound states.ClpB N-terminal domain plays a regulatory role in protein disaggregation E. coli metabolic protein aldehyde-alcohol dehydrogenase-E binds to the ribosome: a unique moonlighting action revealed The Activity of Escherichia coli Chaperone SurA Is Regulated by Conformational Changes Involving a Parvulin Domain.Visualizing chaperone-assisted protein folding.Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor Recognition and targeting mechanisms by chaperones in flagellum assembly and operation The Rrp4-exosome complex recruits and channels substrate RNA by a unique mechanism.The chaperone toolbox at the single-molecule level: From clamping to confining.Backbone and methyl resonance assignments of the 42 kDa human Hsc70 nucleotide binding domain in the ADP state.A Semiautomated Assignment Protocol for Methyl Group Side Chains in Large Proteins.Global Analysis of the Impact of Deleting Trigger Factor on the Transcriptome Profile of Escherichia coli.Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles.Structural and molecular comparison of bacterial and eukaryotic trigger factors Trigger factor chaperone acts as a mechanical foldase.Structured States of Disordered Proteins from Genomic Sequences Forces Driving Chaperone Action Exploiting E. coli auxotrophs for leucine, valine, and threonine specific methyl labeling of large proteins for NMR applications.Non-chaperone proteins can inhibit aggregation and cytotoxicity of Alzheimer amyloid β peptide.Preprotein mature domains contain translocase targeting signals that are essential for secretion.Ligand-driven conformational changes of MurD visualized by paramagnetic NMR.The dynamic dimer structure of the chaperone Trigger Factor.Outer membrane protein folding from an energy landscape perspective.

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P2860

Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

http://www.wikidata.org/entity/Q27683688

description

2014 nî lūn-bûn

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2014 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2014 թվականի մայիսին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

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Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

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Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

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Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

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Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

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Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

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prefLabel

Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

@ast

Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

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Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

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Structural basis for protein antiaggregation activity of the trigger factor chaperone

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Charalampos G Kalodimos

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Paolo Rossi

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Tomohide Saio

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Xiao Guan

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P2860

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Chaperone machines for protein folding, unfolding and disaggregation

Crystal structure of a defective folding protein

Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMR

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

Structural basis for cAMP-mediated allosteric control of the catabolite activator protein.

Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone

Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

Structural Instability Tuning as a Regulatory Mechanism in Protein-Protein Interactions

Version 1.2 of the Crystallography and NMR system

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Anastassios Economou

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24812405

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molecular chaperones

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4070327

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