Pages that link to "Q27637162"
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The following pages link to ATP-bound states of GroEL captured by cryo-electron microscopy (Q27637162):
Displaying 139 items.
- EMDataBank.org: unified data resource for CryoEM (Q24609088) (← links)
- Heat shock proteins: stimulators of innate and acquired immunity (Q26829100) (← links)
- Dynamics, flexibility and ligand-induced conformational changes in biological macromolecules: a computational approach (Q26851157) (← links)
- The dynamic conformational cycle of the group I chaperonin C-termini revealed via molecular dynamics simulation (Q27315643) (← links)
- Bridging between NMA and Elastic Network Models: Preserving All-Atom Accuracy in Coarse-Grained Models (Q27317289) (← links)
- Conformational sampling and nucleotide-dependent transitions of the GroEL subunit probed by unbiased molecular dynamics simulations (Q27333790) (← links)
- ATTRACT-EM: a new method for the computational assembly of large molecular machines using cryo-EM maps (Q27335189) (← links)
- Perturbation-based Markovian transmission model for probing allosteric dynamics of large macromolecular assembling: a study of GroEL-GroES (Q27335329) (← links)
- Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution (Q27640777) (← links)
- VirB11 ATPases are dynamic hexameric assemblies: new insights into bacterial type IV secretion (Q27641112) (← links)
- Role of the -phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics (Q27642245) (← links)
- Purification, crystallization and structure determination of native GroEL fromEscherichia colilacking bound potassium ions (Q27645313) (← links)
- Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure (Q27667812) (← links)
- ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin (Q27678189) (← links)
- Flexible interwoven termini determine the thermal stability of thermosomes (Q27678329) (← links)
- Accurate determination of local defocus and specimen tilt in electron microscopy (Q27861008) (← links)
- Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle (Q28068764) (← links)
- Dynamics, flexibility, and allostery in molecular chaperonins (Q28087481) (← links)
- Lectin control of protein folding and sorting in the secretory pathway (Q28576042) (← links)
- Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations (Q29039687) (← links)
- Molecular dynamics study on folding and allostery in RfaH. (Q30152917) (← links)
- Structure-function relationships of the outer membrane translocon Wza investigated by cryo-electron microscopy and mutagenesis (Q30157351) (← links)
- Coherent conformational degrees of freedom as a structural basis for allosteric communication (Q30410732) (← links)
- Gorgon and pathwalking: macromolecular modeling tools for subnanometer resolution density maps (Q30417985) (← links)
- Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL. (Q30478041) (← links)
- Dynamics of allosteric transitions in GroEL. (Q30478627) (← links)
- Fitting low-resolution cryo-EM maps of proteins using constrained geometric simulations. (Q30481292) (← links)
- Biomolecular pleiomorphism probed by spatial interpolation of coarse models. (Q30489776) (← links)
- Architecture and molecular mechanism of PAN, the archaeal proteasome regulatory ATPase (Q30490705) (← links)
- Conversion of the allosteric transition of GroEL from concerted to sequential by the single mutation Asp-155 -> Ala. (Q30493539) (← links)
- UCSF Chimera, MODELLER, and IMP: an integrated modeling system (Q30523971) (← links)
- Quaternary structure of the European spiny lobster (Palinurus elephas) 1x6-mer hemocyanin from cryoEM and amino acid sequence data (Q30753650) (← links)
- Characterization of the performance of a 200-kV field emission gun for cryo-electron microscopy of biological molecules (Q30860924) (← links)
- A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation (Q31120057) (← links)
- Automated image acquisition and processing using a new generation of 4K x 4K CCD cameras for cryo electron microscopic studies of macromolecular assemblies. (Q31156882) (← links)
- Development of phase plates for electron microscopes and their biological application (Q33318892) (← links)
- A test-bed for optimizing high-resolution single particle reconstructions (Q33340907) (← links)
- Alignment of protein structures in the presence of domain motions (Q33363471) (← links)
- FitEM2EM--tools for low resolution study of macromolecular assembly and dynamics (Q33381597) (← links)
- Allosteric transitions of supramolecular systems explored by network models: application to chaperonin GroEL. (Q33432712) (← links)
- The endoplasmic reticulum chaperone Cosmc directly promotes in vitro folding of T-synthase (Q33593911) (← links)
- Out-of-equilibrium conformational cycling of GroEL under saturating ATP concentrations (Q33778946) (← links)
- Consensus among flexible fitting approaches improves the interpretation of cryo-EM data (Q34054556) (← links)
- Probing the functional mechanism of Escherichia coli GroEL using circular permutation (Q34058603) (← links)
- The unfolding action of GroEL on a protein substrate (Q34186327) (← links)
- Determining macromolecular assembly structures by molecular docking and fitting into an electron density map (Q34188709) (← links)
- Molecular architecture of the basal transcription factor B-TFIID. (Q34301663) (← links)
- Phi value analysis of heterogeneity in pathways of allosteric transitions: Evidence for parallel pathways of ATP-induced conformational changes in a GroEL ring (Q34392034) (← links)
- Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy (Q34480953) (← links)
- Apoptosome: the seven-spoked death machine (Q34552531) (← links)
- Deriving folds of macromolecular complexes through electron cryomicroscopy and bioinformatics approaches (Q34604797) (← links)
- Coarse-grained normal mode analysis in structural biology (Q34694568) (← links)
- On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60. (Q34703664) (← links)
- Allostery and cooperativity revisited (Q34786984) (← links)
- Type I chaperonins: not all are created equal (Q34921944) (← links)
- The chaperonin folding machine (Q35018016) (← links)
- Probing the dynamic process of encapsulation in Escherichia coli GroEL. (Q35036090) (← links)
- Rapid refinement of crystallographic protein construct definition employing enhanced hydrogen/deuterium exchange MS. (Q35554097) (← links)
- Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle. (Q35676628) (← links)
- Evolutionary bidirectional expansion for the tracing of alpha helices in cryo-electron microscopy reconstructions. (Q35783224) (← links)
- Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein (Q35829026) (← links)
- Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins (Q35920574) (← links)
- Using Sculptor and Situs for simultaneous assembly of atomic components into low-resolution shapes (Q35961701) (← links)
- Spontaneous conformational changes in the E. coli GroEL subunit from all-atom molecular dynamics simulations (Q35963381) (← links)
- Allosteric transitions in the chaperonin GroEL are captured by a dominant normal mode that is most robust to sequence variations. (Q35972950) (← links)
- Protein structural transitions and their functional role (Q36017446) (← links)
- Weak intra-ring allosteric communications of the archaeal chaperonin thermosome revealed by normal mode analysis (Q36246516) (← links)
- Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis (Q36458411) (← links)
- Molecular dynamics: survey of methods for simulating the activity of proteins (Q36472758) (← links)
- Particle alignment reliability in single particle electron cryomicroscopy: a general approach (Q36602408) (← links)
- Nucleotide-induced conformational changes of tetradecameric GroEL mapped by H/D exchange monitored by FT-ICR mass spectrometry (Q36605501) (← links)
- Allosteric transitions in biological nanomachines are described by robust normal modes of elastic networks (Q36722945) (← links)
- Phase contrast electron microscopy: development of thin-film phase plates and biological applications (Q36756372) (← links)
- Ring Separation Highlights the Protein-Folding Mechanism Used by the Phage EL-Encoded Chaperonin. (Q36772307) (← links)
- Setting the chaperonin timer: a two-stroke, two-speed, protein machine (Q36967128) (← links)
- Measuring how much work the chaperone GroEL can do. (Q36990800) (← links)
- Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state (Q36993737) (← links)
- Hollow Cone Electron Imaging for Single Particle 3D Reconstruction of Proteins (Q36996531) (← links)
- Location and flexibility of the unique C-terminal tail of Aquifex aeolicus co-chaperonin protein 10 as derived by cryo-electron microscopy and biophysical techniques (Q37034202) (← links)
- Structural frameworks for considering microbial protein- and nucleic acid-dependent motor ATPases (Q37223884) (← links)
- Multiple states of a nucleotide-bound group 2 chaperonin (Q37286298) (← links)
- Conformational shift in the closed state of GroEL induced by ATP-binding triggers a transition to the open state (Q37296194) (← links)
- Bayesian analysis of individual electron microscopy images: towards structures of dynamic and heterogeneous biomolecular assemblies (Q37373538) (← links)
- GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state (Q37420630) (← links)
- The GroEL/GroES cis cavity as a passive anti-aggregation device (Q37541176) (← links)
- Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding (Q37564668) (← links)
- Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL. (Q37585485) (← links)
- Smart nanocontainers and nanoreactors (Q37774574) (← links)
- The intermediate domain defines broad nucleotide selectivity for protein folding in Chlamydophila GroEL1. (Q37858145) (← links)
- Macromolecular structure modeling from 3D EM using VolRover 2.0. (Q38018577) (← links)
- Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions. (Q38095686) (← links)
- ATP-driven molecular chaperone machines (Q38123448) (← links)
- Flexible tethering of primase and DNA Pol α in the eukaryotic primosome. (Q38612714) (← links)
- Substrate Interaction Networks of the Escherichia coli Chaperones: Trigger Factor, DnaK and GroEL. (Q38654107) (← links)
- The human mitochondrial Hsp60 in the APO conformation forms a stable tetradecameric complex. (Q38736673) (← links)
- Bayesian Modeling of Biomolecular Assemblies with Cryo-EM Maps (Q38851274) (← links)
- Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes (Q39790938) (← links)
- ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle (Q39892865) (← links)
- Reconstruction algorithm for single-particle diffraction imaging experiments (Q39942991) (← links)
- Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes (Q40597273) (← links)
- Molecular dynamics of biological macromolecules: a brief history and perspective (Q40603907) (← links)
- A fast mathematical programming procedure for simultaneous fitting of assembly components into cryoEM density maps. (Q40903689) (← links)
- Features of large hinge-bending conformational transitions. Prediction of closed structure from open state (Q41142772) (← links)
- Electron Microscopy and Image Processing: Essential Tools for Structural Analysis of Macromolecules (Q41603733) (← links)
- Nhs: network-based hierarchical segmentation for cryo-electron microscopy density maps. (Q41613229) (← links)
- Real-space refinement with DireX: from global fitting to side-chain improvements. (Q41613255) (← links)
- Objective evaluation of the relative modulation transfer function of densitometers for digitisation of electron micrographs (Q41629403) (← links)
- A core-weighted fitting method for docking atomic structures into low-resolution maps: application to cryo-electron microscopy. (Q41629571) (← links)
- Caught in the act: how ATP binding triggers cooperative conformational changes in a molecular machine (Q41630515) (← links)
- Analysis of peptides and proteins in their binding to GroEL (Q41668841) (← links)
- Multiple subunit fitting into a low-resolution density map of a macromolecular complex using a gaussian mixture model. (Q41774671) (← links)
- Triggering protein folding within the GroEL-GroES complex (Q42146402) (← links)
- Predicting the order in which contacts are broken during single molecule protein stretching experiments (Q42153432) (← links)
- NOMAD-Ref: visualization, deformation and refinement of macromolecular structures based on all-atom normal mode analysis (Q42553727) (← links)
- Functional divergence of chloroplast Cpn60α subunits during Arabidopsis embryo development. (Q42650927) (← links)
- Ionic interactions at both inter-ring contact sites of GroEL are involved in transmission of the allosteric signal: a time-resolved infrared difference study (Q43052174) (← links)
- Differential effects of co-chaperonin homologs on cpn60 oligomers (Q43067991) (← links)
- Inferential optimization for simultaneous fitting of multiple components into a CryoEM map of their assembly (Q43129602) (← links)
- Salt bridges at the inter-ring interface regulate the thermostat of GroEL. (Q44058488) (← links)
- Transient kinetic analysis of ATP-induced allosteric transitions in the eukaryotic chaperonin containing TCP-1. (Q44317704) (← links)
- The allosteric transition of GroEL induced by metal fluoride-ADP complexes (Q44437566) (← links)
- Chaperonin-mediated stabilization and ATP-triggered release of semiconductor nanoparticles (Q44467321) (← links)
- Stopped-flow fluorescence analysis of the conformational changes in the GroEL apical domain: relationships between movements in the apical domain and the quaternary structure of GroEL. (Q44735766) (← links)
- Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis (Q45254396) (← links)
- No evidence for a forced-unfolding mechanism during ATP/GroES binding to substrate-bound GroEL: no observable protection of metastable Rubisco intermediate or GroEL-bound Rubisco from tritium exchange (Q45264613) (← links)
- Kinetic analysis of conformational changes of GroEL based on the fluorescence of tyrosine 506. (Q46219879) (← links)
- Electron paramagnetic resonance and fluorescence studies of the conformation of aspartate aminotransferase bound to GroEL. (Q46836250) (← links)
- GroEL stability and function. Contribution of the ionic interactions at the inter-ring contact sites (Q47848437) (← links)
- Minimum free energy pathways and free energy profiles for conformational transitions based on atomistic molecular dynamics simulations. (Q51975554) (← links)
- Annealing function of GroEL: structural and bioinformatic analysis. (Q52020198) (← links)
- A dynamic model of long-range conformational adaptations triggered by nucleotide binding in GroEL-GroES. (Q54336657) (← links)
- Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE. (Q54465588) (← links)
- Directed evolution of substrate-optimized GroEL/S chaperonins (Q56900591) (← links)
- Bayesian Weighing of Electron Cryo-Microscopy Data for Integrative Structural Modeling (Q58571238) (← links)
- A dynamic analysis of the rotation mechanism for conformational change in F(1)-ATPase (Q74471754) (← links)
- Watching and weighting--chaperone complexes in action (Q81676989) (← links)
- Signalling networks and dynamics of allosteric transitions in bacterial chaperonin GroEL: implications for iterative annealing of misfolded proteins (Q88596138) (← links)
- Chaperonin-assisted protein folding: a chronologue (Q89763905) (← links)
- Molecular Dynamics Simulation for All (Q91588369) (← links)