Published in J Mol Biol on January 10, 2003
AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides. BMC Bioinformatics (2007) 3.02
Molecular basis for amyloid fibril formation and stability. Proc Natl Acad Sci U S A (2005) 3.00
Sequence determinants of amyloid fibril formation. Proc Natl Acad Sci U S A (2003) 2.71
An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril. Proc Natl Acad Sci U S A (2004) 1.85
Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences. Protein Sci (2005) 1.80
Prediction of amyloidogenic and disordered regions in protein chains. PLoS Comput Biol (2006) 1.58
A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments. Proc Natl Acad Sci U S A (2006) 1.49
The amyloid stretch hypothesis: recruiting proteins toward the dark side. Proc Natl Acad Sci U S A (2005) 1.41
Prediction of "hot spots" of aggregation in disease-linked polypeptides. BMC Struct Biol (2005) 1.34
Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation. J Mol Biol (2008) 1.23
Globular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils. J Mol Biol (2009) 1.21
Potential aggregation prone regions in biotherapeutics: A survey of commercial monoclonal antibodies. MAbs (2009) 1.20
Stacked sets of parallel, in-register beta-strands of beta2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling. J Biol Chem (2010) 1.17
Glimpses of the molecular mechanisms of beta2-microglobulin fibril formation in vitro: aggregation on a complex energy landscape. FEBS Lett (2009) 1.13
Increase in the conformational flexibility of beta 2-microglobulin upon copper binding: a possible role for copper in dialysis-related amyloidosis. Protein Sci (2004) 1.04
Competition between intramolecular and intermolecular interactions in an amyloid-forming protein. J Mol Biol (2009) 1.02
K3 fragment of amyloidogenic beta(2)-microglobulin forms ion channels: implication for dialysis related amyloidosis. J Am Chem Soc (2009) 0.97
Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases. PLoS Comput Biol (2009) 0.94
Hacking the code of amyloid formation: the amyloid stretch hypothesis. Prion (2007) 0.93
Amyloidogenic sequences in native protein structures. Protein Sci (2010) 0.91
Differences in aggregation properties of three site-specific mutants of recombinant human stefin B. Protein Sci (2004) 0.81
Phosphorylation as a tool to modulate aggregation propensity and to predict fibril architecture. Chembiochem (2011) 0.81
X-ray Crystallographic Structures of Oligomers of Peptides Derived from β2-Microglobulin. J Am Chem Soc (2015) 0.81
Simulation of pH-dependent edge strand rearrangement in human beta-2 microglobulin. Protein Sci (2005) 0.80
Structure and aggregation mechanism of beta(2)-microglobulin (83-99) peptides studied by molecular dynamics simulations. Biophys J (2007) 0.78
Regions which are Responsible for Swapping are also Responsible for Folding and Misfolding. Open Biochem J (2011) 0.78
Electrostatic screening and backbone preferences of amino acid residues in urea-denatured ubiquitin. Protein Sci (2007) 0.77
Comparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formation. J Mol Biol (2016) 0.76
Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation. Int J Mol Sci (2017) 0.75
Using a reduced dimensionality model to compute the thermodynamic properties of finite polypeptide aggregates. J Biol Phys (2012) 0.75
In vitro amyloidogenic peptides of galectin-7: possible mechanism of amyloidogenesis of primary localized cutaneous amyloidosis. J Biol Chem (2014) 0.75
Nucleation of protein fibrillation by nanoparticles. Proc Natl Acad Sci U S A (2007) 3.23
Pulling geometry defines the mechanical resistance of a beta-sheet protein. Nat Struct Biol (2003) 3.21
Im7 folding mechanism: misfolding on a path to the native state. Nat Struct Biol (2002) 3.15
Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc Natl Acad Sci U S A (2008) 2.90
Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Nat Struct Mol Biol (2006) 2.82
Structural properties of an amyloid precursor of beta(2)-microglobulin. Nat Struct Biol (2002) 2.21
Optimizing protein stability in vivo. Mol Cell (2009) 2.15
Fibril fragmentation enhances amyloid cytotoxicity. J Biol Chem (2009) 2.13
Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid. J Mol Biol (2005) 2.10
Folding versus aggregation: polypeptide conformations on competing pathways. Arch Biochem Biophys (2007) 1.97
Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci (2005) 1.91
Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism. Mol Cell (2006) 1.81
A diversity of assembly mechanisms of a generic amyloid fold. Mol Cell (2011) 1.80
The Yin and Yang of protein folding. FEBS J (2005) 1.68
Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties. Proc Natl Acad Sci U S A (2002) 1.66
Intermediates: ubiquitous species on folding energy landscapes? Curr Opin Struct Biol (2007) 1.60
Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry. J Mol Biol (2006) 1.60
Mechanically unfolding the small, topologically simple protein L. Biophys J (2005) 1.57
Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J Mol Biol (2003) 1.52
A force-activated trip switch triggers rapid dissociation of a colicin from its immunity protein. PLoS Biol (2013) 1.48
An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms. Nat Struct Mol Biol (2009) 1.43
Dynamics in the unfolded state of beta2-microglobulin studied by NMR. J Mol Biol (2004) 1.41
Mechanically unfolding proteins: the effect of unfolding history and the supramolecular scaffold. Protein Sci (2002) 1.39
Conformational conversion during amyloid formation at atomic resolution. Mol Cell (2011) 1.39
Hierarchical assembly of beta2-microglobulin amyloid in vitro revealed by atomic force microscopy. J Mol Biol (2003) 1.39
Structural insights into the polymorphism of amyloid-like fibrils formed by region 20-29 of amylin revealed by solid-state NMR and X-ray fiber diffraction. J Am Chem Soc (2008) 1.38
The transition state for folding of an outer membrane protein. Proc Natl Acad Sci U S A (2010) 1.37
The effect of core destabilization on the mechanical resistance of I27. Biophys J (2002) 1.36
A systematic study of the effect of physiological factors on beta2-microglobulin amyloid formation at neutral pH. Biochemistry (2006) 1.33
Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA. Nucleic Acids Res (2011) 1.32
pH as a trigger of peptide beta-sheet self-assembly and reversible switching between nematic and isotropic phases. J Am Chem Soc (2003) 1.32
The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro. EMBO J (2002) 1.31
Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7. Proc Natl Acad Sci U S A (2005) 1.31
Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies. J Am Chem Soc (2010) 1.30
Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry. Proc Natl Acad Sci U S A (2010) 1.29
Trapping the on-pathway folding intermediate of Im7 at equilibrium. J Mol Biol (2004) 1.29
A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation. J Mol Biol (2003) 1.28
A generic mechanism of beta2-microglobulin amyloid assembly at neutral pH involving a specific proline switch. J Mol Biol (2009) 1.26
The mechanism of folding of Im7 reveals competition between functional and kinetic evolutionary constraints. Nat Struct Mol Biol (2009) 1.26
Direct three-dimensional visualization of membrane disruption by amyloid fibrils. Proc Natl Acad Sci U S A (2012) 1.24
Switching two-state to three-state kinetics in the helical protein Im9 via the optimisation of stabilising non-native interactions by design. J Mol Biol (2004) 1.23
Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation. J Mol Biol (2008) 1.23
Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry. J Am Soc Mass Spectrom (2007) 1.22
Globular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils. J Mol Biol (2009) 1.21
Intermolecular alignment in β2-microglobulin amyloid fibrils. J Am Chem Soc (2010) 1.18
NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7. J Mol Biol (2006) 1.17
Tuning the elastic modulus of hydrated collagen fibrils. Biophys J (2009) 1.17
Stacked sets of parallel, in-register beta-strands of beta2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling. J Biol Chem (2010) 1.17
Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump. Proc Natl Acad Sci U S A (2004) 1.16
A common beta-sheet architecture underlies in vitro and in vivo beta2-microglobulin amyloid fibrils. J Biol Chem (2008) 1.14
Unraveling the molecular basis of subunit specificity in P pilus assembly by mass spectrometry. Proc Natl Acad Sci U S A (2008) 1.14
The N-terminal helix is a post-assembly clamp in the bacterial outer membrane protein PagP. J Mol Biol (2007) 1.13
Glimpses of the molecular mechanisms of beta2-microglobulin fibril formation in vitro: aggregation on a complex energy landscape. FEBS Lett (2009) 1.13
Phase I study of the effect of gastric acid pH modulators on the bioavailability of oral dasatinib in healthy subjects. J Clin Pharmacol (2009) 1.11
Urea-induced unfolding of the immunity protein Im9 monitored by spFRET. Biophys J (2006) 1.11
Viscoelastic measurements of single molecules on a millisecond time scale by magnetically driven oscillation of an atomic force microscope cantilever. Langmuir (2005) 1.10
Mechanical resistance of proteins explained using simple molecular models. Biophys J (2005) 1.10
The oligomeric state and arrangement of the active bacterial translocon. J Biol Chem (2010) 1.09
Understanding the complex mechanisms of β2-microglobulin amyloid assembly. FEBS J (2011) 1.09
Investigation into the role of macrophages in the formation and degradation of beta2-microglobulin amyloid fibrils. J Biol Chem (2007) 1.09
Fibril fragmentation in amyloid assembly and cytotoxicity: when size matters. Prion (2010) 1.06
Ion mobility spectrometry-mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitors. J Am Chem Soc (2013) 1.06
Equilibrium hydrogen exchange reveals extensive hydrogen bonded secondary structure in the on-pathway intermediate of Im7. J Mol Biol (2004) 1.05
Competition between intramolecular and intermolecular interactions in an amyloid-forming protein. J Mol Biol (2009) 1.02
Ligand binding to distinct states diverts aggregation of an amyloid-forming protein. Nat Chem Biol (2011) 1.01
Viscoelastic study of the mechanical unfolding of a protein by AFM. Biophys J (2006) 1.01
N-terminal acetylation of α-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer. Protein Sci (2012) 1.01
Perturbing the folding energy landscape of the bacterial immunity protein Im7 by site-specific N-linked glycosylation. Proc Natl Acad Sci U S A (2010) 1.00
Separation of beta2-microglobulin conformers by high-field asymmetric waveform ion mobility spectrometry (FAIMS) coupled to electrospray ionisation mass spectrometry. Rapid Commun Mass Spectrom (2004) 0.99
Investigating the structural properties of amyloid-like fibrils formed in vitro from beta2-microglobulin using limited proteolysis and electrospray ionisation mass spectrometry. Rapid Commun Mass Spectrom (2006) 0.99
Beta edge strands in protein structure prediction and aggregation. Protein Sci (2003) 0.98
Viscoelastic properties of single polysaccharide molecules determined by analysis of thermally driven oscillations of an atomic force microscope cantilever. Langmuir (2004) 0.98
Quantifying heterogeneity and conformational dynamics from single molecule FRET of diffusing molecules: recurrence analysis of single particles (RASP). Phys Chem Chem Phys (2011) 0.98
Structural plasticity and noncovalent substrate binding in the GroEL apical domain. A study using electrospay ionization mass spectrometry and fluorescence binding studies. J Biol Chem (2002) 0.98
Donor-strand exchange in chaperone-assisted pilus assembly revealed in atomic detail by molecular dynamics. J Mol Biol (2007) 0.97
Semisynthesis of a glycosylated Im7 analogue for protein folding studies. J Am Chem Soc (2005) 0.97
Identification of a mechanical rheostat in the hydrophobic core of protein L. J Mol Biol (2009) 0.97
Internal friction of single polypeptide chains at high stretch. Faraday Discuss (2008) 0.97
Amyloid fibril length distribution quantified by atomic force microscopy single-particle image analysis. Protein Eng Des Sel (2009) 0.96
Co-populated conformational ensembles of beta2-microglobulin uncovered quantitatively by electrospray ionization mass spectrometry. J Biol Chem (2004) 0.96
Thermodynamic description of polymorphism in Q- and N-rich peptide aggregates revealed by atomistic simulation. Biophys J (2009) 0.95
The effect of increasing the stability of non-native interactions on the folding landscape of the bacterial immunity protein Im9. J Mol Biol (2007) 0.95
HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein beta(2)-microglobulin upon release from the MHC-1. J Am Soc Mass Spectrom (2008) 0.94
Role of the N and C-terminal strands of beta 2-microglobulin in amyloid formation at neutral pH. J Mol Biol (2003) 0.93
Ultraviolet resonance Raman studies reveal the environment of tryptophan and tyrosine residues in the native and partially folded states of the E colicin-binding immunity protein Im7. Biochemistry (2005) 0.93
The effect of protein complexation on the mechanical stability of Im9. Biophys J (2007) 0.92
Characterisation of the conformational properties of urea-unfolded Im7: implications for the early stages of protein folding. J Mol Biol (2006) 0.92
A structural model for apolipoprotein C-II amyloid fibrils: experimental characterization and molecular dynamics simulations. J Mol Biol (2010) 0.91
Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagP. J Mol Biol (2013) 0.91
Production and characterization of RNA aptamers specific for amyloid fibril epitopes. J Biol Chem (2007) 0.90
Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6. J Am Chem Soc (2014) 0.90
Desolvation and development of specific hydrophobic core packing during Im7 folding. J Mol Biol (2010) 0.90
Helix stability and hydrophobicity in the folding mechanism of the bacterial immunity protein Im9. Protein Eng Des Sel (2005) 0.90
Conformational properties of the unfolded state of Im7 in nondenaturing conditions. J Mol Biol (2011) 0.89
TRF1 and TRF2 use different mechanisms to find telomeric DNA but share a novel mechanism to search for protein partners at telomeres. Nucleic Acids Res (2013) 0.89
Real-time single-molecule imaging reveals a direct interaction between UvrC and UvrB on DNA tightropes. Nucleic Acids Res (2013) 0.88
The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH. Rapid Commun Mass Spectrom (2012) 0.88
Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assembly. Biophys J (2011) 0.88
Amyloid under the atomic force microscope. Protein Pept Lett (2006) 0.88
Amphipathic polymers enable the study of functional membrane proteins in the gas phase. Anal Chem (2012) 0.88