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

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

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

http://www.wikidata.org/entity/Q27660079

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Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro Single-Particle Cryo-EM of the Ryanodine Receptor Channel in an Aqueous Environment Fusion to a homo-oligomeric scaffold allows cryo-EM analysis of a small protein Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin Dual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin Chamber Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure.The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle.The Crystal Structures of the Eukaryotic Chaperonin CCT Reveal Its Functional Partitioning De novo modeling of the F 420 -reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy The molecular architecture of the eukaryotic chaperonin TRiC/CCT Structure of AAV-DJ, a Retargeted Gene Therapy Vector: Cryo-Electron Microscopy at 4.5 Å Resolution Atomic model of the F 420 -reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector Structural insight into autoinhibition and histone H3-induced activation of DNMT3A Dynamics, flexibility, and allostery in molecular chaperonins Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis Towards a rigorous network of protein-protein interactions of the model sulfate reducer Desulfovibrio vulgaris Hildenborough Leucine zipper-EF-hand containing transmembrane protein 1 (LETM1) forms a Ca(2+)/H(+) antiporter Modeling protein structure at near atomic resolutions with Gorgon.EM-fold: de novo atomic-detail protein structure determination from medium-resolution density maps.Gorgon and pathwalking: macromolecular modeling tools for subnanometer resolution density maps.Precise beam-tilt alignment and collimation are required to minimize the phase error associated with coma in high-resolution cryo-EM Asymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiC Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.The TRiC/CCT chaperone is implicated in Alzheimer's disease based on patient GWAS and an RNAi screen in Aβ-expressing Caenorhabditis elegans.Putting structure into context: fitting of atomic models into electron microscopic and electron tomographic reconstructions.Toward a high-resolution structure of IP₃R channel.Fabs enable single particle cryoEM studies of small proteins Creating an infrastructure for high-throughput high-resolution cryogenic electron microscopy.Cryo-electron microscopy--a primer for the non-microscopist.Problems in obtaining perfect images by single-particle electron cryomicroscopy of biological structures in amorphous ice Reaching the information limit in cryo-EM of biological macromolecules: experimental aspects.Cryo-EM of macromolecular assemblies at near-atomic resolution.Analyses of subnanometer resolution cryo-EM density maps Modulation of STAT3 folding and function by TRiC/CCT chaperonin.Structural biology of TRP channels.Single-particle cryo-EM of the ryanodine receptor channel in an aqueous environment.Near-atomic resolution reconstructions using a mid-range electron microscope operated at 200 kV.Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding.Subunit order of eukaryotic TRiC/CCT chaperonin by cross-linking, mass spectrometry, and combinatorial homology modeling.

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

http://www.wikidata.org/entity/Q27660079

description

2010 nî lūn-bûn

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2010 թուականի Մարտին հրատարակուած գիտական յօդուած

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2010 թվականի մարտին հրատարակված գիտական հոդված

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2010年の論文

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2010年学术文章

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2010年學術文章

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4.0-A resolution cryo-EM struc ...... its unique subunit arrangement

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4.0-A resolution cryo-EM struc ...... its unique subunit arrangement

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4.0-A resolution cryo-EM struc ...... its unique subunit arrangement

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4.0-A resolution cryo-EM struc ...... its unique subunit arrangement

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4.0-A resolution cryo-EM struc ...... its unique subunit arrangement

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4.0-A resolution cryo-EM struc ...... its unique subunit arrangement

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4.0-A resolution cryo-EM struc ...... its unique subunit arrangement

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Proceedings of the National Academy of Sciences of the United States of America

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4.0-A resolution cryo-EM struc ...... its unique subunit arrangement

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Aindrila Mukhopadhyay

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Alyssa M Redding-Johanson

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David Woolford

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Erik J Miller

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Joanita Jakana

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Matthew L Baker

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Ramya N Kumar

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Stefanie Reissmann

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Steven J Ludtke

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Tanveer S Batth

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P2860

Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes.

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

The inter-ring arrangement of the cytosolic chaperonin CCT

Crystal structure of the CCTgamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin

De novo backbone trace of GroEL from single particle electron cryomicroscopy

Structural mechanism of SDS-induced enzyme activity of scorpion hemocyanin revealed by electron cryomicroscopy.

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

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

EMAN: semiautomated software for high-resolution single-particle reconstructions

EMAN2: an extensible image processing suite for electron microscopy

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20194787

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cryogenic electron microscopy

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