Dual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin Chamber - Wikidata - awgldk - TriplyDB

Dual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin Chamber

Dual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin Chamber

http://www.wikidata.org/entity/Q27666606

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Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro Programmed cell death protein 5 interacts with the cytosolic chaperonin containing tailless complex polypeptide 1 (CCT) to regulate β-tubulin folding Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis Therapeutic Approaches for Inhibition of Protein Aggregation in Huntington's Disease The dynamic conformational cycle of the group I chaperonin C-termini revealed via molecular dynamics simulation ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking Cryo-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 chaperonins Flexible interwoven termini determine the thermal stability of thermosomes The molecular architecture of the eukaryotic chaperonin TRiC/CCT Interaction of p53 with the CCT complex promotes protein folding and wild-type p53 activity Dynamics, flexibility, and allostery in molecular chaperonins The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT Design of Light-Controlled Protein Conformations and Functions Reprogramming an ATP-driven protein machine into a light-gated nanocage Multiscale natural moves refine macromolecules using single-particle electron microscopy projection images Asymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiC Sequential allosteric mechanism of ATP hydrolysis by the CCT/TRiC chaperone is revealed through Arrhenius analysis Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.A human CCT5 gene mutation causing distal neuropathy impairs hexadecamer assembly in an archaeal model.Structures of the Gβ-CCT and PhLP1-Gβ-CCT complexes reveal a mechanism for G-protein β-subunit folding and Gβγ dimer assembly.A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle.Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers.Characterization of group II chaperonins from an acidothermophilic archaeon Picrophilus torridus.The ribosome as a hub for protein quality control.Opportunities and challenges for molecular chaperone modulation to treat protein-conformational brain diseases The Mechanism and Function of Group II Chaperonins.High Expression of Cell Division Cycle 42 Promotes Pancreatic Cancer Growth and Predicts Poor Outcome of Pancreatic Cancer Patients.Evolution of the archaeal and mammalian information processing systems: towards an archaeal model for human disease.Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM.Chaperone-client interactions: Non-specificity engenders multifunctionality.Group II archaeal chaperonin recognition of partially folded human γD-crystallin mutants An information theoretic framework reveals a tunable allosteric network in group II chaperonins.Surface Engineering of Nanoparticles for Targeted Delivery to Hepatocellular Carcinoma.Intraring allostery controls the function and assembly of a hetero-oligomeric class II chaperonin.Using the dendritic polymer PAMAM to form gold nanoparticles in the protein cage thermosome.Time-Resolved Measurement of the ATP-Dependent Motion of the Group II Chaperonin by Diffracted Electron Tracking.Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle Molecular determinants of the ATP hydrolysis asymmetry of the CCT chaperonin complex

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Dual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin Chamber

http://www.wikidata.org/entity/Q27666606

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2011 nî lūn-bûn

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2011年の論文

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Dual Action of ATP Hydrolysis ...... he Group II Chaperonin Chamber

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J.CELL.2010.12.017

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Dual Action of ATP Hydrolysis ...... he Group II Chaperonin Chamber

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Bo Chen

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Joanita Jakana

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Junjie Zhang

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Nicholai R Douglas

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Ramya Kumar

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Stefanie Reissmann

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P2860

Mechanism of folding chamber closure in a group II chaperonin

4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement

Crystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding Cycle

Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT

UCSF Chimera--a visualization system for exploratory research and analysis

Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets.

Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies

Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms

The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin

Biological and chemical approaches to diseases of proteostasis deficiency

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