Published in J Biol Chem on June 25, 2014
Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein. J Biol Chem (2015) 0.76
The dynamic conformational cycle of the group I chaperonin C-termini revealed via molecular dynamics simulation. PLoS One (2015) 0.75
Essential functions linked with structural disorder in organisms of minimal genome. Biol Direct (2016) 0.75
How do chaperonins fold protein? Biophysics (Nagoya-shi) (2015) 0.75
Chaperone-client interactions: non-specificity engenders multi-functionality. J Biol Chem (2017) 0.75
Disassembly/reassembly strategy for the production of highly pure GroEL, a tetradecameric supramolecular machine, suitable for quantitative NMR, EPR and mutational studies. Protein Expr Purif (2017) 0.75
Principles that govern the folding of protein chains. Science (1973) 23.40
Protein folding and misfolding. Nature (2003) 14.92
Molecular chaperones in protein folding and proteostasis. Nature (2011) 8.63
The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature (1997) 7.33
The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature (1994) 6.72
Biological and chemical approaches to diseases of proteostasis deficiency. Annu Rev Biochem (2009) 5.23
Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell (2005) 4.78
Residues in chaperonin GroEL required for polypeptide binding and release. Nature (1994) 4.30
Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature (1997) 3.48
Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell (2006) 3.45
Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science (1994) 2.88
GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell (1994) 2.84
GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell (1999) 2.81
Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell (1996) 2.67
Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell (1995) 2.67
Chaperonin overexpression promotes genetic variation and enzyme evolution. Nature (2009) 2.61
Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry (1995) 2.49
Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature (1996) 2.46
Dual function of protein confinement in chaperonin-assisted protein folding. Cell (2001) 2.33
Endosymbiotic bacteria: groEL buffers against deleterious mutations. Nature (2002) 2.21
Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity. J Mol Biol (1999) 1.85
GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism. Nat Struct Biol (1999) 1.81
Mechanisms of protein folding. Curr Opin Struct Biol (2001) 1.80
Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism. Proc Natl Acad Sci U S A (1996) 1.79
Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. Biochemistry (1993) 1.78
Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding. Q Rev Biophys (2009) 1.62
Intermediates: ubiquitous species on folding energy landscapes? Curr Opin Struct Biol (2007) 1.60
GroEL-mediated protein folding: making the impossible, possible. Crit Rev Biochem Mol Biol (2006) 1.51
Monitoring protein conformation along the pathway of chaperonin-assisted folding. Cell (2008) 1.45
GroEL stimulates protein folding through forced unfolding. Nat Struct Mol Biol (2008) 1.43
The origins and consequences of asymmetry in the chaperonin reaction cycle. J Mol Biol (1995) 1.42
A systematic survey of in vivo obligate chaperonin-dependent substrates. EMBO J (2010) 1.41
Conservation among HSP60 sequences in relation to structure, function, and evolution. Protein Sci (2000) 1.41
Chaperonin chamber accelerates protein folding through passive action of preventing aggregation. Proc Natl Acad Sci U S A (2008) 1.37
Cooperativity in ATP hydrolysis by GroEL is increased by GroES. FEBS Lett (1991) 1.37
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding. Cell (2010) 1.36
Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds. J Mol Biol (1995) 1.36
Expansion and compression of a protein folding intermediate by GroEL. Mol Cell (2004) 1.36
Essential role of the chaperonin folding compartment in vivo. EMBO J (2008) 1.29
Multiple chaperonins in bacteria--why so many? FEMS Microbiol Rev (2009) 1.26
Application of fluorescence resonance energy transfer to the GroEL-GroES chaperonin reaction. Methods (2001) 1.18
Visualizing GroEL/ES in the act of encapsulating a folding protein. Cell (2013) 1.16
Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings. J Mol Biol (1998) 1.13
Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution. Proc Natl Acad Sci U S A (2007) 1.12
Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL. Proc Natl Acad Sci U S A (2007) 1.11
The strongly conserved carboxyl-terminus glycine-methionine motif of the Escherichia coli GroEL chaperonin is dispensable. Mol Microbiol (1993) 1.10
Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Proc Natl Acad Sci U S A (1997) 1.10
GroEL locked in a closed conformation by an interdomain cross-link can bind ATP and polypeptide but cannot process further reaction steps. J Biol Chem (1996) 1.07
Folding of malate dehydrogenase inside the GroEL-GroES cavity. Nat Struct Biol (2001) 1.07
Triggering protein folding within the GroEL-GroES complex. J Biol Chem (2008) 1.04
Reconciling theories of chaperonin accelerated folding with experimental evidence. Cell Mol Life Sci (2009) 1.02
Setting the chaperonin timer: a two-stroke, two-speed, protein machine. Proc Natl Acad Sci U S A (2008) 1.02
Hydrophilic residues 526 KNDAAD 531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity. J Biol Chem (2008) 1.01
Effect of the C-terminal truncation on the functional cycle of chaperonin GroEL: implication that the C-terminal region facilitates the transition from the folding-arrested to the folding-competent state. J Biol Chem (2008) 1.01
The effect of chaperonin buffering on protein evolution. Genome Biol Evol (2010) 1.00
A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12. J Bacteriol (1994) 1.00
Denatured proteins facilitate the formation of the football-shaped GroEL-(GroES)2 complex. Biochem J (2010) 0.98
FoldEco: a model for proteostasis in E. coli. Cell Rep (2012) 0.98
Single-molecule study on the decay process of the football-shaped GroEL-GroES complex using zero-mode waveguides. J Biol Chem (2010) 0.96
Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange. Proc Natl Acad Sci U S A (2013) 0.95
Symmetric GroEL:GroES2 complexes are the protein-folding functional form of the chaperonin nanomachine. Proc Natl Acad Sci U S A (2013) 0.93
GroEL/ES buffering and compensatory mutations promote protein evolution by stabilizing folding intermediates. J Mol Biol (2013) 0.85
Catalysis of protein folding by chaperones accelerates evolutionary dynamics in adapting cell populations. PLoS Comput Biol (2013) 0.84
Revisiting the contribution of negative charges on the chaperonin cage wall to the acceleration of protein folding. Proc Natl Acad Sci U S A (2012) 0.83
Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding. J Biol Chem (2013) 0.81