Published in J Biol Chem on April 20, 2011
Probing the functional mechanism of Escherichia coli GroEL using circular permutation. PLoS One (2011) 0.78
Suppression of amyloid fibrils using the GroEL apical domain. Sci Rep (2016) 0.77
Asparagine deamidation reduces DNA-binding affinity of the Drosophila melanogaster Scr homeodomain. FEBS Lett (2015) 0.75
NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR (1995) 93.94
MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph (1996) 39.73
Alpha-synuclein in Lewy bodies. Nature (1997) 20.83
In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat Protoc (2006) 16.56
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol (1999) 11.38
Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell (1993) 10.15
Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol (2004) 10.13
Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell (1997) 7.59
Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature (2009) 6.99
Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature (2007) 6.26
Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. J Biol Chem (1987) 4.99
Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation. Protein Sci (2006) 3.73
Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim Biophys Acta (2004) 3.69
The structural basis of protein folding and its links with human disease. Philos Trans R Soc Lond B Biol Sci (2001) 3.65
Amyloid fibril formation by an SH3 domain. Proc Natl Acad Sci U S A (1998) 3.55
Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease. J Biol Chem (1993) 3.52
Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences. Chem Rev (2006) 3.00
alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease. J Biol Chem (1999) 2.91
Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington's disease and related disorders. Neuron (2002) 2.67
Amyloid-like features of polyglutamine aggregates and their assembly kinetics. Biochemistry (2002) 2.59
A toxic monomeric conformer of the polyglutamine protein. Nat Struct Mol Biol (2007) 2.33
NMR analysis of a 900K GroEL GroES complex. Nature (2002) 2.12
Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Crit Rev Biochem Mol Biol (1991) 1.80
Amyloid oligomers: formation and toxicity of Abeta oligomers. FEBS J (2010) 1.78
Lens aging: effects of crystallins. Biochim Biophys Acta (2009) 1.75
Characterization of a functionally important mobile domain of GroES. Nature (1993) 1.74
Biophysics of Parkinson's disease: structure and aggregation of alpha-synuclein. Curr Protein Pept Sci (2009) 1.66
Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins. Int J Pept Protein Res (1987) 1.62
Deamidation of human proteins. Proc Natl Acad Sci U S A (2001) 1.53
Isoaspartate in peptides and proteins: formation, significance, and analysis. J Pharm Biomed Anal (2000) 1.45
Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins. FEBS Lett (1997) 1.37
Intrinsic disorder in proteins associated with neurodegenerative diseases. Front Biosci (Landmark Ed) (2009) 1.33
Characterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: implication for aggregation. J Mol Biol (2008) 1.33
Isoaspartate formation and neurodegeneration in Alzheimer's disease. Arch Biochem Biophys (2000) 1.27
Structural characterization of the intrinsically unfolded protein beta-synuclein, a natural negative regulator of alpha-synuclein aggregation. J Mol Biol (2007) 1.21
Simultaneous racemization and isomerization at specific aspartic acid residues in alpha B-crystallin from the aged human lens. Biochim Biophys Acta (1994) 1.20
Deamidation and isoaspartate formation in smeared tau in paired helical filaments. Unusual properties of the microtubule-binding domain of tau. J Biol Chem (1999) 1.19
Basis of microheterogeneity of myelin basic protein. J Biol Chem (1976) 1.17
Amyloid fibril formation of alpha-synuclein is accelerated by preformed amyloid seeds of other proteins: implications for the mechanism of transmissible conformational diseases. J Biol Chem (2005) 1.14
Uniform and residue-specific 15N-labeling of proteins on a highly deuterated background. J Biomol NMR (2004) 1.05
Mechanism of amyloidogenesis: nucleation-dependent fibrillation versus double-concerted fibrillation. BMB Rep (2009) 0.98
Deamidation of asparagine and glutamine residues in proteins and peptides: structural determinants and analytical methodology. J Chromatogr B Biomed Appl (1994) 0.98
Proton-proton Overhauser NMR spectroscopy with polypeptide chains in large structures. Proc Natl Acad Sci U S A (2006) 0.96
Molecular pathogenesis of protein misfolding diseases: pathological molecular environments versus quality control systems against misfolded proteins. J Biochem (2009) 0.96
The disordered mobile loop of GroES folds into a defined beta-hairpin upon binding GroEL. J Biol Chem (2001) 0.95
Age-related changes of alpha-crystallin aggregate in human lens. Amino Acids (2006) 0.92
Synthetic post-translationally modified human A beta peptide exhibits a markedly increased tendency to form beta-pleated sheets in vitro. Eur J Biochem (1994) 0.92
Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model. J Mol Biol (1999) 0.89
Deamidation of calmodulin at neutral and alkaline pH: quantitative relationships between ammonia loss and the susceptibility of calmodulin to modification by protein carboxyl methyltransferase. Arch Biochem Biophys (1989) 0.88
Structural stability and solution structure of chaperonin GroES heptamer studied by synchrotron small-angle X-ray scattering. J Mol Biol (2003) 0.87
Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES. J Mol Biol (1999) 0.86
Characterization of fibrillation process of alpha-synuclein at the initial stage. Biochem Biophys Res Commun (2008) 0.84
Fibril formation of hsp10 homologue proteins and determination of fibril core regions: differences in fibril core regions dependent on subtle differences in amino acid sequence. J Mol Biol (2008) 0.83
Amyloid-like fibril formation of co-chaperonin GroES: nucleation and extension prefer different degrees of molecular compactness. J Mol Biol (2005) 0.82
Spontaneous deamidation and isomerization of Asn108 in prion peptide 106-126 and in full-length prion protein. Biochem Biophys Res Commun (1999) 0.81
Amyloid oligomers: dynamics and toxicity in the cytosol and nucleus. FEBS J (2010) 0.81
Deamidation of alpha-synuclein. Protein Sci (2009) 0.80
Measurement of altered aspartyl residues in the scrapie associated form of prion protein. Biochem Biophys Res Commun (1998) 0.76
Aluminum induces tau aggregation in vitro but not in vivo. J Alzheimers Dis (2007) 2.10
Amyloid fibril formation of alpha-synuclein is accelerated by preformed amyloid seeds of other proteins: implications for the mechanism of transmissible conformational diseases. J Biol Chem (2005) 1.14
Heat-shock protein 60 is required for blastema formation and maintenance during regeneration. Proc Natl Acad Sci U S A (2005) 1.07
Induction of AApoAII amyloidosis by various heterogeneous amyloid fibrils. FEBS Lett (2004) 1.03
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
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. J Biol Chem (2004) 0.95
A novel enzyme, 2'-hydroxybiphenyl-2-sulfinate desulfinase (DszB), from a dibenzothiophene-desulfurizing bacterium Rhodococcus erythropolis KA2-5-1: gene overexpression and enzyme characterization. Biochim Biophys Acta (2002) 0.92
Heavy metal analysis of groundwater from Warri, Nigeria. Int J Environ Health Res (2002) 0.90
GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle. J Biol Chem (2002) 0.89
Structural stability of covalently linked GroES heptamer: advantages in the formation of oligomeric structure. J Mol Biol (2007) 0.89
Structural stability and solution structure of chaperonin GroES heptamer studied by synchrotron small-angle X-ray scattering. J Mol Biol (2003) 0.87
Automated graphic image generation system for effective representation of infectious disease surveillance data. Comput Methods Programs Biomed (2003) 0.86
Crystal structure of thermostable aspartase from Bacillus sp. YM55-1: structure-based exploration of functional sites in the aspartase family. J Mol Biol (2003) 0.86
Structural stability of oligomeric chaperonin 10: the role of two beta-strands at the N and C termini in structural stabilization. J Mol Biol (2004) 0.84
Evidence for proteasomal degradation of Kv1.5 channel protein. Biochem Biophys Res Commun (2005) 0.84
Fibril formation of hsp10 homologue proteins and determination of fibril core regions: differences in fibril core regions dependent on subtle differences in amino acid sequence. J Mol Biol (2008) 0.83
Amyloid-like fibril formation of co-chaperonin GroES: nucleation and extension prefer different degrees of molecular compactness. J Mol Biol (2005) 0.82
Crystal structure of the cambialistic superoxide dismutase from Aeropyrum pernix K1--insights into the enzyme mechanism and stability. FEBS J (2010) 0.82
Gly192 at hinge 2 site in the chaperonin GroEL plays a pivotal role in the dynamic apical domain movement that leads to GroES binding and efficient encapsulation of substrate proteins. Biochim Biophys Acta (2008) 0.81
High-resolution nuclear magnetic resonance spectroscopic study of metabolites in the cerebrospinal fluid of patients with cervical myelopathy and lumbar radiculopathy. Eur Spine J (2010) 0.81
Effects of GroESL coexpression on the folding of nicotinoprotein formaldehyde dismutase from Pseudomonas putida F61. Biosci Biotechnol Biochem (2002) 0.80
Role of C-terminal negative charges and tyrosine residues in fibril formation of α-synuclein. Brain Behav (2012) 0.80
A novel ATP/ADP hydrolysis activity of hyperthermostable group II chaperonin in the presence of cobalt or manganese ion. FEBS Lett (2005) 0.80
Metals accelerate production of the aberrant splicing isoform of the presenilin-2. J Neurochem (2004) 0.80
Gene expression in primary cultured astrocytes affected by aluminum: alteration of chaperons involved in protein folding. Environ Health Prev Med (2010) 0.79
Chaperonin-encapsulation of proteins for NMR. Biochim Biophys Acta (2010) 0.79
Multiple structural transitions of the GroEL subunit are sensitive to intermolecular interactions with cochaperonin and refolding polypeptide. J Biochem (2006) 0.79
Accumulation of aluminum by primary cultured astrocytes from aluminum amino acid complex and its apoptotic effect. Brain Res (2005) 0.79
Cold denaturation of α-synuclein amyloid fibrils. Angew Chem Int Ed Engl (2014) 0.78
Isolation of short peptide fragments from alpha-synuclein fibril core identifies a residue important for fibril nucleation: a possible implication for diagnostic applications. Biochim Biophys Acta (2010) 0.78
Probing the functional mechanism of Escherichia coli GroEL using circular permutation. PLoS One (2011) 0.78
Some aspects of astroglial functions and aluminum implications for neurodegeneration. Brain Res Rev (2006) 0.78
Evaluation of the stability of an SR398/GroES chaperonin complex. J Biochem (2014) 0.77
Functional stabilization of Kv1.5 protein by Hsp70 in mammalian cell lines. Biochem Biophys Res Commun (2008) 0.77
Mechanical unfolding of covalently linked GroES: evidence of structural subunit intermediates. Protein Sci (2009) 0.77
Varied effects of Pyrococcus furiosus prefoldin and P. furiosus chaperonin on the refolding reactions of substrate proteins. J Biochem (2011) 0.76
Up-regulation in the expression of renin gene by the influence of aluminium. J Inorg Biochem (2009) 0.76
Bilberry anthocyanins neutralize the cytotoxicity of co-chaperonin GroES fibrillation intermediates. Biochemistry (2013) 0.76
Development of computerized Kana Pick-out Test for the neuropsychological examination. Comput Methods Programs Biomed (2003) 0.76
A potentially versatile nucleotide hydrolysis activity of group II chaperonin monomers from Thermoplasma acidophilum. Biochemistry (2009) 0.76
Probing the dynamic process of encapsulation in Escherichia coli GroEL. PLoS One (2013) 0.75
Anthocyanin suppresses the toxicity of Aβ deposits through diversion of molecular forms in in vitro and in vivo models of Alzheimer's disease. Nutr Neurosci (2015) 0.75
Synthesis and some properties of binuclear ruthenocenes bridged by oligoynes: formation of bis(cyclopentadienylidene)cumulene diruthenium complexes in the two-electron oxidation. Chemistry (2006) 0.75
Evaluation of Aβ fibrillization inhibitory effect by a PEG-peptide conjugate based on an Aβ peptide fragment with intramolecular FRET. Chem Commun (Camb) (2011) 0.75
[Two faces of Janus: Recent studies on the characteristics of E. coli GroEL and its apical domain]. Seikagaku (2010) 0.75
Functional characterization of the recombinant group II chaperonin alpha from Thermoplasma acidophilum. J Biochem (2008) 0.75