Published in J Mol Biol on December 22, 2004
Nucleation of protein fibrillation by nanoparticles. Proc Natl Acad Sci U S A (2007) 3.23
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
A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proc Natl Acad Sci U S A (2007) 2.62
Folding versus aggregation: polypeptide conformations on competing pathways. Arch Biochem Biophys (2007) 1.97
Conformational conversion during amyloid formation at atomic resolution. Mol Cell (2011) 1.39
Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: parallels to precursors in amyloid disease. Proc Natl Acad Sci U S A (2006) 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
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
Protein folding: then and now. Arch Biochem Biophys (2007) 1.18
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
A common beta-sheet architecture underlies in vitro and in vivo beta2-microglobulin amyloid fibrils. J Biol Chem (2008) 1.14
Glimpses of the molecular mechanisms of beta2-microglobulin fibril formation in vitro: aggregation on a complex energy landscape. FEBS Lett (2009) 1.13
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
DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded form. Protein Sci (2010) 0.96
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
Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly. Mol Cell (2014) 0.93
A new amide proton R1rho experiment permits accurate characterization of microsecond time-scale conformational exchange. J Biomol NMR (2005) 0.88
The low-pH unfolded state of the C-terminal domain of the ribosomal protein L9 contains significant secondary structure in the absence of denaturant but is no more compact than the low-pH urea unfolded state. Biochemistry (2008) 0.87
Expanding the repertoire of amyloid polymorphs by co-polymerization of related protein precursors. J Biol Chem (2013) 0.87
The cold denatured state of the C-terminal domain of protein L9 is compact and contains both native and non-native structure. J Am Chem Soc (2010) 0.85
SOD1-associated ALS: a promising system for elucidating the origin of protein-misfolding disease. HFSP J (2008) 0.85
Dynamics of free versus complexed β2-microglobulin and the evolution of interfaces in MHC class I molecules. Immunogenetics (2012) 0.84
NMR characterizations of an amyloidogenic conformational ensemble of the PI3K SH3 domain. Protein Sci (2006) 0.82
Equilibrium unfolding thermodynamics of beta2-microglobulin analyzed through native-state H/D exchange. Biophys J (2009) 0.80
Non-native hydrophobic interactions detected in unfolded apoflavodoxin by paramagnetic relaxation enhancement. Eur Biophys J (2009) 0.80
Structure and aggregation mechanism of beta(2)-microglobulin (83-99) peptides studied by molecular dynamics simulations. Biophys J (2007) 0.78
Assessing the effect of loop mutations in the folding space of β2-microglobulin with molecular dynamics simulations. Int J Mol Sci (2013) 0.77
Direct observation of minimum-sized amyloid fibrils using solution NMR spectroscopy. Protein Sci (2010) 0.77
Dynamics and dimension of an amyloidogenic disordered state of human β(2)-microglobulin. Eur Biophys J (2013) 0.76
Stepwise unfolding of human β2-microglobulin into a disordered amyloidogenic precursor at low pH. Eur Biophys J (2016) 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
The predicted coiled-coil domain of myosin 10 forms a novel elongated domain that lengthens the head. J Biol Chem (2005) 2.11
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
Perspectives on NMR in drug discovery: a technique comes of age. Nat Rev Drug Discov (2008) 1.95
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
Ribosome clearance by FusB-type proteins mediates resistance to the antibiotic fusidic acid. Proc Natl Acad Sci U S A (2012) 1.62
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
Amyloid-forming peptides from beta2-microglobulin-Insights into the mechanism of fibril formation in vitro. J Mol Biol (2003) 1.44
An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms. Nat Struct Mol Biol (2009) 1.43
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
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
Van der Waals interactions dominate ligand-protein association in a protein binding site occluded from solvent water. J Am Chem Soc (2005) 1.24
Direct three-dimensional visualization of membrane disruption by amyloid fibrils. Proc Natl Acad Sci U S A (2012) 1.24
Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation. J Mol Biol (2008) 1.23
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
Poxvirus K7 protein adopts a Bcl-2 fold: biochemical mapping of its interactions with human DEAD box RNA helicase DDX3. J Mol Biol (2008) 1.22
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
Strong solute-solute dispersive interactions in a protein-ligand complex. J Am Chem Soc (2005) 1.19
Intermolecular alignment in β2-microglobulin amyloid fibrils. J Am Chem Soc (2010) 1.18
Tuning the elastic modulus of hydrated collagen fibrils. Biophys J (2009) 1.17
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
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
Thermodynamics of binding of 2-methoxy-3-isopropylpyrazine and 2-methoxy-3-isobutylpyrazine to the major urinary protein. J Am Chem Soc (2004) 1.13
Urea-induced unfolding of the immunity protein Im9 monitored by spFRET. Biophys J (2006) 1.11
Dissecting the cholera toxin-ganglioside GM1 interaction by isothermal titration calorimetry. J Am Chem Soc (2004) 1.10
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
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
Solution structure of the leader sequence of the patellamide precursor peptide, PatE1-34. Chembiochem (2010) 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
Global changes in local protein dynamics reduce the entropic cost of carbohydrate binding in the arabinose-binding protein. J Mol Biol (2007) 0.98
Identification of a mechanical rheostat in the hydrophobic core of protein L. J Mol Biol (2009) 0.97
Semisynthesis of a glycosylated Im7 analogue for protein folding studies. J Am Chem Soc (2005) 0.97
Donor-strand exchange in chaperone-assisted pilus assembly revealed in atomic detail by molecular dynamics. J Mol Biol (2007) 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