Published in Nat Struct Mol Biol on February 19, 2006
Amyloid formation by globular proteins under native conditions. Nat Chem Biol (2009) 3.72
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
An unfolded CH1 domain controls the assembly and secretion of IgG antibodies. Mol Cell (2009) 1.90
How antibodies fold. Trends Biochem Sci (2009) 1.88
3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR. Proc Natl Acad Sci U S A (2006) 1.70
Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape. Chem Rev (2010) 1.62
Conformational conversion during amyloid formation at atomic resolution. Mol Cell (2011) 1.39
Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic beta2-microglobulin variant. Proc Natl Acad Sci U S A (2011) 1.38
Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies. J Am Chem Soc (2010) 1.30
A regulatable switch mediates self-association in an immunoglobulin fold. Nat Struct Mol Biol (2008) 1.30
A two-step path to inclusion formation of huntingtin peptides revealed by number and brightness analysis. Biophys J (2010) 1.27
Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation. J Mol Biol (2008) 1.23
β₂-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages. Nat Struct Mol Biol (2010) 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
Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts. J Biomol NMR (2009) 1.16
Amyloid fibrils: abnormal protein assembly. Prion (2008) 1.15
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
Amyloid oligomer conformation in a group of natively folded proteins. PLoS One (2008) 1.10
Understanding the complex mechanisms of β2-microglobulin amyloid assembly. FEBS J (2011) 1.09
Differences in prion strain conformations result from non-native interactions in a nucleus. Nat Chem Biol (2010) 1.08
Biophysics of protein evolution and evolutionary protein biophysics. J R Soc Interface (2014) 1.08
Structure, folding dynamics, and amyloidogenesis of D76N β2-microglobulin: roles of shear flow, hydrophobic surfaces, and α-crystallin. J Biol Chem (2013) 1.04
Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization. Proc Natl Acad Sci U S A (2009) 1.04
Amyloid in neurodegenerative diseases: friend or foe? Semin Cell Dev Biol (2011) 1.02
Defined DNA sequences promote the assembly of a bacterial protein into distinct amyloid nanostructures. Proc Natl Acad Sci U S A (2007) 1.01
Metal binding sheds light on mechanisms of amyloid assembly. Prion (2009) 0.99
Localization of a conformational epitope common to non-native and fibrillar immunoglobulin light chains. Biochemistry (2007) 0.98
Molecular dynamics simulation suggests possible interaction patterns at early steps of beta2-microglobulin aggregation. Biophys J (2006) 0.96
Effect of tetracyclines on the dynamics of formation and destructuration of beta2-microglobulin amyloid fibrils. J Biol Chem (2010) 0.96
Cu(II) organizes beta-2-microglobulin oligomers but is released upon amyloid formation. Protein Sci (2008) 0.96
Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein beta2-microglobulin revealed by real-time two-dimensional NMR. J Biol Chem (2009) 0.95
Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases. PLoS Comput Biol (2009) 0.94
Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways. Elife (2015) 0.94
Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly. Mol Cell (2014) 0.93
Population of nonnative states of lysozyme variants drives amyloid fibril formation. J Am Chem Soc (2011) 0.93
Energy landscapes of functional proteins are inherently risky. Nat Chem Biol (2014) 0.92
Phage display and peptide mapping of an immunoglobulin light chain fibril-related conformational epitope. Biochemistry (2007) 0.91
Propensity to form amyloid fibrils is encoded as excitations in the free energy landscape of monomeric proteins. J Mol Biol (2014) 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
Substrate protein folds while it is bound to the ATP-independent chaperone Spy. Nat Struct Mol Biol (2015) 0.90
Systemic amyloidosis: lessons from β2-microglobulin. J Biol Chem (2015) 0.89
A hinge region cis-proline in ribonuclease A acts as a conformational gatekeeper for C-terminal domain swapping. J Mol Biol (2010) 0.89
The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH. Rapid Commun Mass Spectrom (2012) 0.88
The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity. Proc Natl Acad Sci U S A (2008) 0.88
A single mutation at residue 25 populates the folding intermediate of E. coli RNase H and reveals a highly dynamic partially folded ensemble. J Mol Biol (2009) 0.86
An accidental breach of a protein's natural defenses. Nat Struct Mol Biol (2006) 0.86
Delineating the conformational elements responsible for Cu(2+)-induced oligomerization of beta-2 microglobulin. Biochemistry (2009) 0.85
Transient misfolding dominates multidomain protein folding. Nat Commun (2015) 0.85
Protein aggregation/crystallization and minor structural changes: universal versus specific aspects. Biophys J (2007) 0.84
Characterizing intermolecular interactions that initiate native-like protein aggregation. Biophys J (2012) 0.84
Assessing the causes and consequences of co-polymerization in amyloid formation. Prion (2013) 0.83
A simulated intermediate state for folding and aggregation provides insights into ΔN6 β2-microglobulin amyloidogenic behavior. PLoS Comput Biol (2014) 0.83
Inhibition of beta2-microglobulin amyloid fibril formation by alpha2-macroglobulin. J Biol Chem (2011) 0.82
Structure of an early native-like intermediate of β2-microglobulin amyloidogenesis. Protein Sci (2013) 0.81
C. elegans expressing human β2-microglobulin: a novel model for studying the relationship between the molecular assembly and the toxic phenotype. PLoS One (2012) 0.80
Mechanism of protein kinetic stabilization by engineered disulfide crosslinks. PLoS One (2013) 0.80
Both the cis-trans equilibrium and isomerization dynamics of a single proline amide modulate β2-microglobulin amyloid assembly. Proc Natl Acad Sci U S A (2013) 0.80
Mechanisms of amyloid formation revealed by solution NMR. Prog Nucl Magn Reson Spectrosc (2015) 0.80
The Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids. J Biol Chem (2015) 0.79
A nonessential role for Arg 55 in cyclophilin18 for catalysis of proline isomerization during protein folding. Protein Sci (2009) 0.79
Amyloid formation in denatured single-mutant lysozymes where residual structures are modulated. Protein Sci (2006) 0.78
A Native-like Intermediate Serves as a Branching Point between the Folding and Aggregation Pathways of the Mouse Prion Protein. Structure (2015) 0.78
NMR-based characterization of a refolding intermediate of beta2-microglobulin labeled using a wheat germ cell-free system. Protein Sci (2009) 0.78
Identifying protein stabilizing ligands using GroEL. Biopolymers (2010) 0.77
Misfolding of amyloidogenic proteins and their interactions with membranes. Biomolecules (2013) 0.77
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
Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR. J Biol Chem (2015) 0.77
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
Distinguishing closely related amyloid precursors using an RNA aptamer. J Biol Chem (2014) 0.76
Mapping local structural perturbations in the native state of stefin B (cystatin B) under amyloid forming conditions. Front Mol Neurosci (2012) 0.76
Insights into the folding and unfolding processes of wild-type and mutated SH3 domain by molecular dynamics and replica exchange molecular dynamics simulations. PLoS One (2013) 0.76
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
The beta-strand-loop-beta-strand conformation is marginally populated in beta2-microglobulin (20-41) peptide in solution as revealed by replica exchange molecular dynamics simulations. Biophys J (2008) 0.76
The Folding process of Human Profilin-1, a novel protein associated with familial amyotrophic lateral sclerosis. Sci Rep (2015) 0.76
A Population Shift between Sparsely Populated Folding Intermediates Determines Amyloidogenicity. J Am Chem Soc (2016) 0.76
4-Fluoroprolines: Conformational Analysis and Effects on the Stability and Folding of Peptides and Proteins. Top Heterocycl Chem (2016) 0.76
Historical and Current Concepts of Fibrillogenesis and In vivo Amyloidogenesis: Implications of Amyloid Tissue Targeting. Front Mol Biosci (2016) 0.75
Formation of ordered biomolecular structures by the self-assembly of short peptides. J Vis Exp (2013) 0.75
Morphological differences between β(2) -microglobulin in fibrils and inclusion bodies. Chembiochem (2011) 0.75
Identification of fibrillogenic regions in human triosephosphate isomerase. PeerJ (2016) 0.75
Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of β-2-Microglobulin. Sci Rep (2015) 0.75
Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation. Int J Mol Sci (2017) 0.75
Dialysis-related amyloidosis: challenges and solutions. Int J Nephrol Renovasc Dis (2016) 0.75
How one bad protein spoils the barrel: structural details of β2-microglobulin amyloidogenicity. Mol Cell (2011) 0.75
Theoretical Insights into the Biophysics of Protein Bi-stability and Evolutionary Switches. PLoS Comput Biol (2016) 0.75
Increased β-Sheet Dynamics and D-E Loop Repositioning Are Necessary for Cu(II)-Induced Amyloid Formation by β-2-Microglobulin. Biochemistry (2017) 0.75
Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid. Biochemistry (2016) 0.75
Optimized fast mixing device for real-time NMR applications. J Magn Reson (2017) 0.75
Stepwise unfolding of human β2-microglobulin into a disordered amyloidogenic precursor at low pH. Eur Biophys J (2016) 0.75
MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors. PLoS One (2017) 0.75
Refolding the unfoldable: A systematic approach for renaturation of Bacillus circulans xylanase. Protein Sci (2017) 0.75
Amyloidogenesis of Tau protein. Protein Sci (2017) 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
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
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
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
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
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
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
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
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
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
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
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
Thermodynamic description of polymorphism in Q- and N-rich peptide aggregates revealed by atomistic simulation. Biophys J (2009) 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
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
Role of the N and C-terminal strands of beta 2-microglobulin in amyloid formation at neutral pH. J Mol Biol (2003) 0.93
The effect of protein complexation on the mechanical stability of Im9. Biophys J (2007) 0.92