Related references
Note: Only part of the references are listed.GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side
Yali Li et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2009)
Chaperonin complex with a newly folded protein encapsulated in the folding chamber
D. K. Clare et al.
NATURE (2009)
Probing protein-chaperone interactions with single-molecule fluorescence spectroscopy
Frank Hillger et al.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2008)
Monitoring protein conformation along the pathway of chaperonin-assisted folding
Shruti Sharma et al.
CELL (2008)
Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroEL
Tatsuya Nojima et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
Triggering Protein Folding within the GroEL-GroES Complex
Damian Madan et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
Concerted release of substrate domains from GroEL by ATP is demonstrated with FRET
Niv Papo et al.
JOURNAL OF MOLECULAR BIOLOGY (2008)
GroEL stimulates protein folding through forced unfolding
Zong Lin et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2008)
Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state
Eli Chapman et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2008)
Chaperonin chamber accelerates protein folding through passive action of preventing aggregation
Adrian C. Apetri et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2008)
Folding trajectories of human dihydrofolate reductase inside the GroEL-GroES chaperonin cavity and free in solution
Reto Horst et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2007)
Topologies of a substrate protein bound to the chaperonin GroEL
Nadav Elad et al.
MOLECULAR CELL (2007)
Perturbed ATPase activity and not close confinement of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL
George W. Farr et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2007)
Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner
Yakov Kipnis et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2007)
Quantitative dynamics and binding studies of the 20S proteasome by NMR
Remco Sprangers et al.
NATURE (2007)
Proton-proton Overhauser NMR spectroscopy with polypeptide chains in large structures
Reto Horst et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2006)
Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE
Matthew J. Cliff et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein
Yun-Chi Tang et al.
CELL (2006)
GroEL-GroES-mediated protein folding
Arthur L. Horwich et al.
CHEMICAL REVIEWS (2006)
GroEL1: A dedicated chaperone involved in mycolic acid biosynthesis during biofilm formation in mycobacteria
A Ojha et al.
CELL (2005)
Direct NMR observation of a substrate protein bound to the chaperonin GroEL
R Horst et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2005)
Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation
J Hinnerwisch et al.
CELL (2005)
The 13Å structure of a chaperonin GroEL-protein substrate complex by cryo-electron microscopy
S Falke et al.
JOURNAL OF MOLECULAR BIOLOGY (2005)
Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis
D Rivenzon-Segal et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2005)
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
ES Park et al.
FEBS LETTERS (2005)
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
M Taniguchi et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL
F Motojima et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2004)
Expansion and compression of a protein folding intermediate by GroEL
Z Lin et al.
MOLECULAR CELL (2004)
Sculpting the proteome with AAA+ proteases and disassembly machines
RT Sauer et al.
CELL (2004)
Role of the γ-phosphate of ATP in triggering protein folding by GroEL-GroES:: function, structure and energetics
C Chaudhry et al.
EMBO JOURNAL (2003)
Chaperonin-mediated protein folding: fate of substrate polypeptide
WA Fenton et al.
QUARTERLY REVIEWS OF BIOPHYSICS (2003)
Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy
T Inobe et al.
JOURNAL OF MOLECULAR BIOLOGY (2003)
GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle
T Miyazaki et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
ATP-bound states of GroEL captured by cryo-electron microscopy
NA Ranson et al.
CELL (2001)
Dual function of protein confinement in chaperonin-assisted protein folding
A Brinker et al.
CELL (2001)
GroEL/GroES-mediated folding of a protein too large to be encapsulated
TK Chaudhuri et al.
CELL (2001)
The disordered mobile loop of GroES folds into a defined β-hairpin upon binding GroEL
F Shewmaker et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2001)
Folding of malate dehydrogenase inside the GroEL-GroES cavity
JW Chen et al.
NATURE STRUCTURAL BIOLOGY (2001)
A thermodynamic coupling mechanism can explain the GroEL-mediated acceleration of the folding of barstar
N Bhutani et al.
JOURNAL OF MOLECULAR BIOLOGY (2000)
Multivalent binding of nonnative substrate proteins by the chaperonin GroEL
GW Farr et al.
CELL (2000)