Pages that link to "Q27637162"
Jump to navigation
Jump to search
The following pages link to ATP-bound states of GroEL captured by cryo-electron microscopy (Q27637162):
Displaying 50 items.
- 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)