Published in J Mol Biol on March 19, 2008
Optimizing protein stability in vivo. Mol Cell (2009) 2.15
Influence of pH control in the formation of inclusion bodies during production of recombinant sphingomyelinase-D in Escherichia coli. Microb Cell Fact (2014) 0.79
Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin. Proteins (2012) 0.79
Influence of the stability of a fused protein and its distance to the amyloidogenic segment on fibril formation. PLoS One (2010) 0.78
Association between foldability and aggregation propensity in small disulfide-rich proteins. Antioxid Redox Signal (2014) 0.76
Cytosolic selection systems to study protein stability. J Bacteriol (2014) 0.75
Aggregation propensity of neuronal receptors: potential implications in neurodegenerative disorders. Future Sci OA (2015) 0.75
A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation. Redox Biol (2017) 0.75
AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides. BMC Bioinformatics (2007) 3.02
Amyloid-like properties of bacterial inclusion bodies. J Mol Biol (2005) 1.90
Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins. Microb Cell Fact (2005) 1.79
Prediction of "hot spots" of aggregation in disease-linked polypeptides. BMC Struct Biol (2005) 1.34
Design, selection, and characterization of thioflavin-based intercalation compounds with metal chelating properties for application in Alzheimer's disease. J Am Chem Soc (2009) 1.32
Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities. FEBS J (2006) 1.29
Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin. Proc Natl Acad Sci U S A (2005) 1.25
Amyloids in bacterial inclusion bodies. Trends Biochem Sci (2009) 1.24
Inclusion bodies: specificity in their aggregation process and amyloid-like structure. Biochim Biophys Acta (2008) 1.24
Protein aggregation: mechanisms and functional consequences. Int J Biochem Cell Biol (2012) 1.20
Recent structural and computational insights into conformational diseases. Curr Med Chem (2008) 1.12
Prion and non-prion amyloids of the HET-s prion forming domain. J Mol Biol (2007) 1.11
Protein folding and aggregation in bacteria. Cell Mol Life Sci (2010) 1.10
Folding of small disulfide-rich proteins: clarifying the puzzle. Trends Biochem Sci (2006) 1.07
Amyloid fibril formation by a partially structured intermediate state of alpha-chymotrypsin. J Mol Biol (2004) 1.06
Effect of temperature on protein quality in bacterial inclusion bodies. FEBS Lett (2006) 1.05
Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates. J Biotechnol (2006) 1.02
Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case. Proteomics (2007) 1.02
AGGRESCAN: method, application, and perspectives for drug design. Methods Mol Biol (2012) 1.01
Bacterial inclusion bodies of Alzheimer's disease β-amyloid peptides can be employed to study native-like aggregation intermediate states. Chembiochem (2011) 1.01
Biological role of bacterial inclusion bodies: a model for amyloid aggregation. FEBS J (2011) 1.01
Prediction of the aggregation propensity of proteins from the primary sequence: aggregation properties of proteomes. Biotechnol J (2011) 0.99
Study and selection of in vivo protein interactions by coupling bimolecular fluorescence complementation and flow cytometry. Nat Protoc (2008) 0.96
Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion. Microb Cell Fact (2009) 0.95
Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains. BMC Genomics (2013) 0.95
The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells. Microb Cell Fact (2006) 0.95
Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases. PLoS Comput Biol (2009) 0.94
Sulfated polysaccharides promote the assembly of amyloid beta(1-42) peptide into stable fibrils of reduced cytotoxicity. J Biol Chem (2008) 0.93
Ile-phe dipeptide self-assembly: clues to amyloid formation. Biophys J (2006) 0.93
Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation. Mol Biosyst (2012) 0.92
Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors. Microb Cell Fact (2012) 0.92
Modulation of Abeta42 fibrillogenesis by glycosaminoglycan structure. FASEB J (2010) 0.91
Protein aggregation profile of the bacterial cytosol. PLoS One (2010) 0.90
PrionScan: an online database of predicted prion domains in complete proteomes. BMC Genomics (2014) 0.90
Evolutionary selection for protein aggregation. Biochem Soc Trans (2012) 0.89
Studies on bacterial inclusion bodies. Future Microbiol (2008) 0.88
Yeast prions form infectious amyloid inclusion bodies in bacteria. Microb Cell Fact (2012) 0.88
Linking amyloid protein aggregation and yeast survival. Mol Biosyst (2011) 0.88
Modeling amyloids in bacteria. Microb Cell Fact (2012) 0.87
Protein complementation assays: approaches for the in vivo analysis of protein interactions. FEBS Lett (2009) 0.87
Scrambled isomers as key intermediates in the oxidative folding of ligand binding module 5 of the low density lipoprotein receptor. J Biol Chem (2008) 0.86
Human kallikrein 6 activity is regulated via an autoproteolytic mechanism of activation/inactivation. Biol Chem (2004) 0.86
The effect of amyloidogenic peptides on bacterial aging correlates with their intrinsic aggregation propensity. J Mol Biol (2011) 0.84
Amyloid-like protein inclusions in tobacco transgenic plants. PLoS One (2010) 0.84
Detecting and interfering protein interactions: towards the control of biochemical pathways. Curr Med Chem (2009) 0.83
Thioflavin-T excimer formation upon interaction with amyloid fibers. Chem Commun (Camb) (2013) 0.83
The role of protein sequence and amino acid composition in amyloid formation: scrambling and backward reading of IAPP amyloid fibrils. J Mol Biol (2010) 0.83
Contribution of disulfide bonds to stability, folding, and amyloid fibril formation: the PI3-SH3 domain case. Antioxid Redox Signal (2011) 0.83
Native structure protects SUMO proteins from aggregation into amyloid fibrils. Biomacromolecules (2012) 0.83
Direct interaction between a human digestive protease and the mucoadhesive poly(acrylic acid). Acta Crystallogr D Biol Crystallogr (2008) 0.83
Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli. Biotechnol J (2014) 0.83
Kinetic and thermodynamic stability of bacterial intracellular aggregates. FEBS Lett (2008) 0.82
The aggregation properties of Escherichia coli proteins associated with their cellular abundance. Biotechnol J (2011) 0.82
Temperature dependence of the aggregation kinetics of Sup35 and Ure2p yeast prions. Biomacromolecules (2011) 0.82
Folding specificity induced by loop stiffness. Protein Sci (2003) 0.82
Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis. Int J Mol Sci (2013) 0.82
Monitoring the interference of protein-protein interactions in vivo by bimolecular fluorescence complementation: the DnaK case. Proteomics (2008) 0.82
N-terminal protein tails act as aggregation protective entropic bristles: the SUMO case. Biomacromolecules (2014) 0.81
Cross-β-sheet supersecondary structure in amyloid folds: techniques for detection and characterization. Methods Mol Biol (2013) 0.81
Design and NMR conformational study of a beta-sheet peptide based on Betanova and WW domains. Protein Sci (2006) 0.81
Deciphering the role of the thermodynamic and kinetic stabilities of SH3 domains on their aggregation inside bacteria. Proteomics (2010) 0.81
Characterizing the tick carboxypeptidase inhibitor: molecular basis for its two-domain nature. J Biol Chem (2006) 0.81
Amyloids or prions? That is the question. Prion (2015) 0.80
Protein aggregation propensity is a crucial determinant of intracellular inclusion formation and quality control degradation. Biochim Biophys Acta (2013) 0.80
Secondary binding site of the potato carboxypeptidase inhibitor. Contribution to its structure, folding, and biological properties. Biochemistry (2004) 0.79
Self-assembly of human latexin into amyloid-like oligomers. BMC Struct Biol (2007) 0.79
Role of kinetic intermediates in the folding of leech carboxypeptidase inhibitor. J Biol Chem (2004) 0.79
NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor. Structure (2005) 0.78
Effect of the surface charge of artificial model membranes on the aggregation of amyloid β-peptide. Biochimie (2012) 0.78
Designing out disulfide bonds of leech carboxypeptidase inhibitor: implications for its folding, stability and function. J Mol Biol (2009) 0.78
Oxidative folding of leech-derived tryptase inhibitor via native disulfide-bonded intermediates. Antioxid Redox Signal (2008) 0.78
About targets and causes in protein folding. J Biomol Struct Dyn (2013) 0.78
Trifluoroethanol modulates amyloid formation by the all α-helical URN1 FF domain. Int J Mol Sci (2013) 0.77
The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain. PLoS One (2013) 0.77
Zinc induced folding is essential for TIM15 activity as an mtHsp70 chaperone. Biochim Biophys Acta (2012) 0.77
The mitochondrial intermembrane space oxireductase Mia40 funnels the oxidative folding pathway of the cytochrome c oxidase assembly protein Cox19. J Biol Chem (2014) 0.77
Protein oxidative folding in the intermembrane mitochondrial space: more than protein trafficking. Curr Protein Pept Sci (2012) 0.77
Protein aggregation profile of the human kinome. Front Physiol (2012) 0.77
Deciphering the structural basis that guides the oxidative folding of leech-derived tryptase inhibitor. J Biol Chem (2009) 0.77
Protease inhibitors as models for the study of oxidative folding. Antioxid Redox Signal (2010) 0.76
Characterization of amyloid-like properties in bacterial intracellular aggregates. Methods Mol Biol (2015) 0.76
Association between foldability and aggregation propensity in small disulfide-rich proteins. Antioxid Redox Signal (2014) 0.76
The NMR structures of the major intermediates of the two-domain tick carboxypeptidase inhibitor reveal symmetry in its folding and unfolding pathways. J Biol Chem (2008) 0.76
Aggregation of the neuroblastoma-associated mutant (S120G) of the human nucleoside diphosphate kinase-A/NM23-H1 into amyloid fibrils. Naunyn Schmiedebergs Arch Pharmacol (2011) 0.76
Discovery of novel inhibitors of amyloid β-peptide 1-42 aggregation. J Med Chem (2012) 0.76
Screening for amyloid aggregation: in-silico, in-vitro and in-vivo detection. Curr Protein Pept Sci (2014) 0.75