Published in Biochemistry on November 09, 2004
Revealing the bifurcation in the unfolding pathways of GFP by using single-molecule experiments and simulations. Proc Natl Acad Sci U S A (2007) 1.74
Random single amino acid deletion sampling unveils structural tolerance and the benefits of helical registry shift on GFP folding and structure. Structure (2014) 1.50
Structural basis for the fast maturation of Arthropoda green fluorescent protein. EMBO Rep (2006) 1.29
The rough energy landscape of superfolder GFP is linked to the chromophore. J Mol Biol (2007) 1.23
Fluorescent proteins as biomarkers and biosensors: throwing color lights on molecular and cellular processes. Curr Protein Pept Sci (2008) 1.22
Evolution of a fluorinated green fluorescent protein. Proc Natl Acad Sci U S A (2007) 1.21
The dual-basin landscape in GFP folding. Proc Natl Acad Sci U S A (2008) 1.16
Complementation and reconstitution of fluorescence from circularly permuted and truncated green fluorescent protein. Biochemistry (2009) 1.16
Hsp40 chaperones promote degradation of the HERG potassium channel. J Biol Chem (2009) 1.09
Assembling an intermediate filament network by dynamic cotranslation. J Cell Biol (2006) 1.08
Two electrical potential-dependent steps are required for transport by the Escherichia coli Tat machinery. J Cell Biol (2007) 1.08
Fluorescent-protein stabilization and high-resolution imaging of cleared, intact mouse brains. PLoS One (2015) 1.05
Chromophore packing leads to hysteresis in GFP. J Mol Biol (2009) 1.02
Mechanism of a genetically encoded dark-to-bright reporter for caspase activity. J Biol Chem (2011) 0.96
Structural basis of fluorescence fluctuation dynamics of green fluorescent proteins in acidic environments. J Phys Chem B (2006) 0.94
Kinetic analysis of ribosome-bound fluorescent proteins reveals an early, stable, cotranslational folding intermediate. J Biol Chem (2011) 0.93
Denaturant-dependent folding of GFP. Proc Natl Acad Sci U S A (2012) 0.92
Beta-barrel scaffold of fluorescent proteins: folding, stability and role in chromophore formation. Int Rev Cell Mol Biol (2013) 0.89
Hysteresis as a Marker for Complex, Overlapping Landscapes in Proteins. J Phys Chem Lett (2012) 0.88
Membrane-assisted online renaturation for automated microfluidic lectin blotting. J Am Chem Soc (2011) 0.87
The extremely slow-exchanging core and acid-denatured state of green fluorescent protein. HFSP J (2008) 0.86
Distinct effects of guanidine thiocyanate on the structure of superfolder GFP. PLoS One (2012) 0.85
A rewired green fluorescent protein: folding and function in a nonsequential, noncircular GFP permutant. Biochemistry (2010) 0.85
A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases. Nat Struct Mol Biol (2012) 0.83
Acid-denatured Green Fluorescent Protein (GFP) as model substrate to study the chaperone activity of protein disulfide isomerase. Int J Mol Sci (2011) 0.82
Fluorescence complementation via EF-hand interactions. J Biotechnol (2009) 0.82
A desolvation model for trifluoroethanol-induced aggregation of enhanced green fluorescent protein. Biophys J (2012) 0.82
Folding study of Venus reveals a strong ion dependence of its yellow fluorescence under mildly acidic conditions. J Biol Chem (2009) 0.82
Refolding of a membrane protein in a microfluidics reactor. Eur Biophys J (2007) 0.81
Use of RNAlater in fluorescence-activated cell sorting (FACS) reduces the fluorescence from GFP but not from DsRed. BMC Res Notes (2010) 0.80
Transmission electron microscopy characterization of fluorescently labelled amyloid β 1-40 and α-synuclein aggregates. BMC Biotechnol (2011) 0.80
Green-lighting green fluorescent protein: faster and more efficient folding by eliminating a cis-trans peptide isomerization event. Protein Sci (2014) 0.78
Multi-state proteins: approach allowing experimental determination of the formation order of structure elements in the green fluorescent protein. PLoS One (2012) 0.77
Structural basis of fluorescence quenching in caspase activatable-GFP. Protein Sci (2013) 0.77
Exploring the folding pathway of green fluorescent protein through disulfide engineering. Protein Sci (2015) 0.77
Optically induced thermal gradients for protein characterization in nanolitre-scale samples in microfluidic devices. Sci Rep (2013) 0.76
Systematic Quality Control Analysis of LINCS Data. CPT Pharmacometrics Syst Pharmacol (2016) 0.75
Toward Computationally Designed Self-Reporting Biosensors Using Leave-One-Out Green Fluorescent Protein. Biochemistry (2015) 0.75
A fusion tag to fold on: the S-layer protein SgsE confers improved folding kinetics to translationally fused enhanced green fluorescent protein. J Microbiol Biotechnol (2012) 0.75
Ultrafast folding of alpha3D: a de novo designed three-helix bundle protein. Proc Natl Acad Sci U S A (2003) 1.57
Early events in protein folding explored by rapid mixing methods. Chem Rev (2006) 1.50
Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing. Proc Natl Acad Sci U S A (2002) 1.22
Unification of the folding mechanisms of non-two-state and two-state proteins. J Mol Biol (2004) 1.16
Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments. J Am Chem Soc (2006) 1.09
Rapid mixing methods for exploring the kinetics of protein folding. Methods (2004) 1.00
Multiple parallel-pathway folding of proline-free Staphylococcal nuclease. J Mol Biol (2003) 0.98
The allosteric transition of GroEL induced by metal fluoride-ADP complexes. J Mol Biol (2003) 0.98
Fast compaction of alpha-lactalbumin during folding studied by stopped-flow X-ray scattering. J Mol Biol (2002) 0.97
Characterization of archaeal group II chaperonin-ADP-metal fluoride complexes: implications that group II chaperonins operate as a "two-stroke engine". J Biol Chem (2005) 0.96
Flexible recognition of the tRNA G18 methylation target site by TrmH methyltransferase through first binding and induced fit processes. J Biol Chem (2010) 0.96
Role of the helical protrusion in the conformational change and molecular chaperone activity of the archaeal group II chaperonin. J Biol Chem (2004) 0.93
Effects of the difference in the unfolded-state ensemble on the folding of Escherichia coli dihydrofolate reductase. J Mol Biol (2003) 0.91
Oligomeric Hsp33 with enhanced chaperone activity: gel filtration, cross-linking, and small angle x-ray scattering (SAXS) analysis. J Biol Chem (2004) 0.91
Sequential action of ATP-dependent subunit conformational change and interaction between helical protrusions in the closure of the built-in lid of group II chaperonins. J Biol Chem (2008) 0.91
The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein. J Mol Biol (2006) 0.90
Mutational analysis of protein solubility enhancement using short peptide tags. Biopolymers (2007) 0.89
Testing the relationship between foldability and the early folding events of dihydrofolate reductase from Escherichia coli. J Mol Biol (2003) 0.87
Ultrarapid mixing experiments shed new light on the characteristics of the initial conformational ensemble during the folding of ribonuclease A. Proc Natl Acad Sci U S A (2004) 0.87
Surprisingly high correlation between early and late stages in non-two-state protein folding. J Mol Biol (2006) 0.86
The catalytic domain of topological knot tRNA methyltransferase (TrmH) discriminates between substrate tRNA and nonsubstrate tRNA via an induced-fit process. J Biol Chem (2013) 0.86
Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy. J Mol Biol (2003) 0.85
Fluorescence resonance energy transfer between points on actin and the C-terminal region of tropomyosin in skeletal muscle thin filaments. J Biochem (2004) 0.85
Solvent environments significantly affect the enzymatic function of Escherichia coli dihydrofolate reductase: comparison of wild-type protein and active-site mutant D27E. Biochim Biophys Acta (2013) 0.85
Asymmetry of the GroEL-GroES complex under physiological conditions as revealed by small-angle x-ray scattering. Biophys J (2007) 0.84
Denaturation and reassembly of chaperonin GroEL studied by solution X-ray scattering. Protein Sci (2003) 0.84
Reversible and fast association equilibria of a molecular chaperone, gp57A, of bacteriophage T4. Biophys J (2003) 0.84
The molten globule of β(2)-microglobulin accumulated at pH 4 and its role in protein folding. J Mol Biol (2012) 0.84
Native-state heterogeneity of β(2)-microglobulin as revealed by kinetic folding and real-time NMR experiments. J Mol Biol (2012) 0.82
ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking. PLoS One (2013) 0.82
Different folding pathways taken by highly homologous proteins, goat alpha-lactalbumin and canine milk lysozyme. J Mol Biol (2010) 0.82
Dissecting a bimolecular process of MgATP²- binding to the chaperonin GroEL. J Mol Biol (2011) 0.81
Folding mechanism of reduced Cytochrome c: equilibrium and kinetic properties in the presence of carbon monoxide. J Mol Biol (2008) 0.81
Nucleotide-induced conformational changes of tetradecameric GroEL mapped by H/D exchange monitored by FT-ICR mass spectrometry. Sci Rep (2013) 0.81
Characterization of kinetic folding intermediates of recombinant canine milk lysozyme by stopped-flow circular dichroism. Biochemistry (2005) 0.81
Helical and expanded conformation of equine beta-lactoglobulin in the cold-denatured state. J Mol Biol (2005) 0.80
Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone. FEBS Lett (2012) 0.79
Probing force-induced unfolding intermediates of a single staphylococcal nuclease molecule and the effect of ligand binding. Biochem Biophys Res Commun (2008) 0.79
Molecular mechanisms of the cytotoxicity of human α-lactalbumin made lethal to tumor cells (HAMLET) and other protein-oleic acid complexes. J Biol Chem (2013) 0.79
Localized nature of the transition-state structure in goat alpha-lactalbumin folding. J Mol Biol (2004) 0.79
Equilibrium and kinetics of the folding and unfolding of canine milk lysozyme. Biochemistry (2007) 0.79
Evolutional design of a hyperactive cysteine- and methionine-free mutant of Escherichia coli dihydrofolate reductase. J Biol Chem (2006) 0.79
Non-native alpha-helix formation is not necessary for folding of lipocalin: comparison of burst-phase folding between tear lipocalin and beta-lactoglobulin. Proteins (2009) 0.78
Unfolding pathways of goat alpha-lactalbumin as revealed in multiple alignment of molecular dynamics trajectories. J Mol Biol (2007) 0.78
Atomically detailed description of the unfolding of alpha-lactalbumin by the combined use of experiments and simulations. J Mol Biol (2005) 0.78
Nonuniform chain collapse during early stages of staphylococcal nuclease folding detected by fluorescence resonance energy transfer and ultrarapid mixing methods. Protein Sci (2013) 0.78
NMR characterization of the interaction of GroEL with amyloid β as a model ligand. FEBS Lett (2013) 0.78
Adaptation of a hyperthermophilic group II chaperonin to relatively moderate temperatures. Protein Eng Des Sel (2010) 0.77
Sequential four-state folding/unfolding of goat α-lactalbumin and its N-terminal variants. Proteins (2012) 0.76
The H/D-exchange kinetics of the Escherichia coli co-chaperonin GroES studied by 2D NMR and DMSO-quenched exchange methods. J Mol Biol (2013) 0.76
Site-directed spin labeling-electron spin resonance mapping of the residues of cyanobacterial clock protein KaiA that are affected by KaiA-KaiC interaction. Genes Cells (2014) 0.76
Phi value analysis of an allosteric transition of GroEL based on a single-pathway model. J Mol Biol (2004) 0.76
The use of spin desalting columns in DMSO-quenched H/D-exchange NMR experiments. Protein Sci (2013) 0.75
Solubilization and folding of a fully active recombinant Gaussia luciferase with native disulfide bonds by using a SEP-Tag. Biochim Biophys Acta (2011) 0.75
Salt bridges in prion proteins are necessary for high-affinity binding to the monoclonal antibody T2. Biophys Chem (2011) 0.75
Structural insights into the stability perturbations induced by N-terminal variation in human and goat α-lactalbumin. Protein Eng Des Sel (2012) 0.75