ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin - Wikidata - awgldk - TriplyDB

ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin

ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin

http://www.wikidata.org/entity/Q27678189

about

Chaperone machines for protein folding, unfolding and disaggregation The dynamic conformational cycle of the group I chaperonin C-termini revealed via molecular dynamics simulation Unraveling low-resolution structural data of large biomolecules by constructing atomic models with experiment-targeted parallel cascade selection simulations.Flexible interwoven termini determine the thermal stability of thermosomes Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein CryoEM and Molecular Dynamics of the Circadian KaiB–KaiC Complex Indicates That KaiB Monomers Interact with KaiC and Block ATP Binding Clefts Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 A resolution GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle Dynamics, flexibility, and allostery in molecular chaperonins HermiteFit: fast-fitting atomic structures into a low-resolution density map using three-dimensional orthogonal Hermite functions.Refinement of atomic models in high resolution EM reconstructions using Flex-EM and local assessment.Do's and don'ts of cryo-electron microscopy: a primer on sample preparation and high quality data collection for macromolecular 3D reconstruction.Crystallization and preliminary X-ray crystallographic analysis of the XoGroEL chaperonin from Xanthomonas oryzae pv. oryzae.Human Hsp60 with its mitochondrial import signal occurs in solution as heptamers and tetradecamers remarkably stable over a wide range of concentrations.Conditional disorder in chaperone action.Role of denatured-state properties in chaperonin action probed by single-molecule spectroscopy Conformational States of macromolecular assemblies explored by integrative structure calculation.A national facility for biological cryo-electron microscopy Probing the dynamic process of encapsulation in Escherichia coli GroEL.A cool hybrid approach to the herpesvirus 'life' cycle.From high symmetry to high resolution in biological electron microscopy: a commentary on Crowther (1971) 'Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs'Cryo-EM: A Unique Tool for the Visualization of Macromolecular Complexity.Molecular Chaperones of Leishmania: Central Players in Many Stress-Related and -Unrelated Physiological Processes.Structural insight into the cooperation of chloroplast chaperonin subunits.HdeB chaperone activity is coupled to its intrinsic dynamic properties.Go hybrid: EM, crystallography, and beyond Engineering a nanopore with co-chaperonin function.Nucleotide-induced conformational changes of tetradecameric GroEL mapped by H/D exchange monitored by FT-ICR mass spectrometry Visualization of uncorrelated, tandem symmetry mismatches in the internal genome packaging apparatus of bacteriophage T7 GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP Validation of cryo-EM structure of IP₃R1 channel.Targeted conformational search with map-restrained self-guided Langevin dynamics: application to flexible fitting into electron microscopic density maps.Unravelling biological macromolecules with cryo-electron microscopy.A molecular mechanism of chaperone-client recognition.ATP-driven molecular chaperone machines.Hsp60 chaperonopathies and chaperonotherapy: targets and agents.Structure-Encoded Global Motions and Their Role in Mediating Protein-Substrate Interactions.Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM.The human mitochondrial Hsp60 in the APO conformation forms a stable tetradecameric complex.

P2860

Q27026110-1487E5C7-B002-4A75-BD51-C9F4A9CC26DE Q27315643-FAE79629-E529-4C8A-9D61-54846710187C Q27332000-487774E2-82E5-4E23-A79E-A1839CEEF2A0 Q27678329-F56E52E3-3A29-4582-9070-F3B117CBB24A Q27678536-1359CCA2-745D-4DF1-9AEC-6BA6A00A5655 Q27678761-6727F1B6-2A09-4BCD-9947-DBB2233A1EFB Q27679114-8847BD75-D37E-48F9-8CCA-4AF4CA373855 Q27683698-E3ED71C7-A1C6-4552-9986-735EA5B038E3 Q28068764-5AC72B1F-0386-425F-B104-521F85FA01D6 Q28087481-A8FCCCDE-F70B-4BFA-9789-D764BD30AE02 Q30365362-2103B05A-F69C-4A0C-A41E-279B16669495 Q30385763-EAD985C9-F75F-4916-A557-9DFB090C95D5 Q30887503-812EC302-8E58-49B7-B55C-540AEFCE80D8 Q33583352-26F93E90-389E-4117-A6F1-A6608B46E26A Q33618484-2BD435BD-CC93-430F-89EB-192535E77368 Q34302314-43452CC7-B92D-4300-AEF9-0F5057A01B3C Q34727615-7064AD33-3046-4AAF-9C61-5A6985FE4C0E Q34980210-5627FD6D-EC27-40A7-BE39-6BB9682B9BAF Q35006831-BF93B9AF-74FA-4F97-8256-07B074AEBB59 Q35036090-9B744E41-8043-4C27-BF23-3E38CD8A7184 Q35098318-303DA9BC-23BF-438B-A24E-99F50AC5CD41 Q35178810-1AECD48B-3106-4BBD-B5DE-06FA5C5FDFAF Q35638563-14262B50-15D2-484F-8550-9ACF0F90EFCE Q35808069-88B06602-BBF2-4CB5-953A-9A6A86A10124 Q35987912-5D364370-4744-4FD7-B046-CDA8071C5900 Q36305554-26126E73-1B5F-49F7-BDFE-FAC872408A70 Q36339269-2C298D73-017C-4839-98AD-2E0BFA3D00AD Q36514091-BAF586CF-E18B-4B32-BAE9-AE5D84F7262B Q36605501-74D87176-1E4A-482E-85BB-BB8E4D5E62CB Q36799252-8206994A-2916-410E-A97F-AD524B929B43 Q36820063-FA990214-A15D-4715-AF89-658B8503F592 Q36965481-9FB4285E-14C1-45D2-ACCA-AFB0BC072663 Q37202039-64034E23-14AD-4974-AA1D-C7BFEBF58215 Q37357527-2788ADA7-8ECF-4B9F-8797-1BC814A81CC4 Q37603844-041F4789-D324-4C8C-80A2-7D95AC58E302 Q38123448-39CD66C1-8700-4C07-A43D-3CB039045514 Q38167037-40C2CE4C-618A-4429-B986-7E59A06020A3 Q38542912-DA22FB66-B2E3-445C-92FA-BFD96AB4E3E9 Q38678101-F733AD6A-8F35-463E-BE6E-280C34CAE7A0 Q38736673-B7D02388-4BDE-474B-83BF-44B95ECC025A

P2860

ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin

http://www.wikidata.org/entity/Q27678189

description

2012 nî lūn-bûn

@nan

2012 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի մարտին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

ATP-Triggered Conformational C ...... hanics of the GroEL Chaperonin

@ast

ATP-Triggered Conformational C ...... hanics of the GroEL Chaperonin

@en

ATP-Triggered Conformational C ...... hanics of the GroEL Chaperonin

@nl

type

label

ATP-Triggered Conformational C ...... hanics of the GroEL Chaperonin

@ast

ATP-Triggered Conformational C ...... hanics of the GroEL Chaperonin

@en

ATP-Triggered Conformational C ...... hanics of the GroEL Chaperonin

@nl

prefLabel

ATP-Triggered Conformational C ...... hanics of the GroEL Chaperonin

@ast

ATP-Triggered Conformational C ...... hanics of the GroEL Chaperonin

@en

ATP-Triggered Conformational C ...... hanics of the GroEL Chaperonin

@nl

P1433

Q27678189-B6CB329C-4F8D-4ADE-B94A-0F4873AF95FF

P1476

Q27678189-1324FE2D-2321-4B3C-8C23-3A4536215CE9

P2093

Q27678189-12B2460F-77BF-4C36-9798-F3BFB3F8F7D6

Q27678189-26ADC98F-5579-4CCA-8B2B-834174D3C681

Q27678189-390519AC-1565-41D6-9F16-2E0B37C3AF1D

Q27678189-473E25E3-1AB8-4AB1-8E29-436C2144913D

Q27678189-6F952292-90A8-470D-8284-08E6FAAE0815

Q27678189-7B1D361C-834B-4066-9791-DE15A2846576

Q27678189-DFD76EAC-DD71-490A-93F4-5F9B6ED425EE

P2860

Q27678189-01703FA2-74A9-4684-92A7-45379A712809

Q27678189-03DE6C00-F8E9-4624-8994-E278626C326D

Q27678189-0DBC363C-39DB-4E76-BD46-AB300BFB361D

Q27678189-0EB6C8D6-AA04-43E7-AD4C-1791F64DA177

Q27678189-0ECB9891-0F0F-4EB3-A80C-B1FD47ACDB77

Q27678189-0FC84A11-124E-4E89-BC36-DFF30DBBA784

Q27678189-1D01EFD8-28A8-4B4C-8EC4-8F827DCBAF2B

Q27678189-1D96BF06-1849-4D62-98A3-CB200787E28A

Q27678189-21487794-58C0-40A4-9DB8-A6FB30856957

Q27678189-29243558-D23F-494C-B943-9BA3E18F46A7

P304

Q27678189-8F35199F-A0CD-4680-9D60-17E82DC41566

P31

Q27678189-121AB6B2-D314-4B66-87F1-83C532ECEACB

P3181

Q27678189-93667A6F-272D-4C92-8EB0-633D687F3610

P356

Q27678189-BB2019CE-B5D8-4C33-9D23-04281ECA424C

P407

Q27678189-051724CC-0026-473F-99E0-F198D1D15C49

P433

Q27678189-E45650B5-8C14-4497-A58A-A9900A08285A

P478

Q27678189-5E4719D6-FC3E-4A06-BFCB-2F808459E03B

P50

Q27678189-1F3ECE20-47E2-42F5-815B-A572F9736352

P577

Q27678189-BC24B2B3-EBA1-4B94-999F-D90672BDD0E1

P5875

Q27678189-1E0E3897-040A-4776-A5BA-673A7D9D0D1F

P698

Q27678189-2DFCF340-3BBC-4B15-9C92-E79FC9F229C3

P932

Q27678189-F2A5F1F9-1674-46B8-AA72-FA37FFD6E708

P3181

P356

J.CELL.2012.02.047

P1433

P1476

ATP-Triggered Conformational C ...... hanics of the GroEL Chaperonin

@en

P2093

Daniel K Clare

http://www.w3.org/2001/XMLSchema#string

Daven Vasishtan

http://www.w3.org/2001/XMLSchema#string

George W Farr

http://www.w3.org/2001/XMLSchema#string

Helen R Saibil

http://www.w3.org/2001/XMLSchema#string

Joel Quispe

http://www.w3.org/2001/XMLSchema#string

Maya Topf

http://www.w3.org/2001/XMLSchema#string

Scott Stagg

http://www.w3.org/2001/XMLSchema#string

P2860

A simple method for displaying the hydropathic character of a protein

ATP-bound states of GroEL captured by cryo-electron microscopy

Role of the -phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics

Crystal Structure of Group II Chaperonin in the Open State

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

Interplay of structure and disorder in cochaperonin mobile loops

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

SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields

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

P304

113-23

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

251589

http://www.w3.org/2001/XMLSchema#string

P356

10.1016/J.CELL.2012.02.047

http://www.w3.org/2001/XMLSchema#string

P407

P433

1

http://www.w3.org/2001/XMLSchema#string

P478

149

http://www.w3.org/2001/XMLSchema#string

P50

Arthur L. Horwich

P577

2012-03-30T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

221973951

http://www.w3.org/2001/XMLSchema#string

P698

22445172

http://www.w3.org/2001/XMLSchema#string

P932

3326522

http://www.w3.org/2001/XMLSchema#string