Unified theoretical description of the kinetics of protein aggregation

[1]  S. Michnick,et al.  Why does biopolymer condensation matter? , 2018, Nature Reviews Molecular Cell Biology.

[2]  A. Kinjo,et al.  A new look at an old view of denaturant induced protein unfolding. , 2018, Analytical biochemistry.

[3]  L. Rezabkova,et al.  Mechanistic Origin of the Combined Effect of Surfaces and Mechanical Agitation on Amyloid Formation. , 2017, ACS nano.

[4]  C. Brangwynne,et al.  Liquid phase condensation in cell physiology and disease , 2017, Science.

[5]  D. Hall.  A composite polynomial approach for analyzing the indefinite self-association of macromolecules studied by sedimentation equilibrium. , 2017, Biophysical chemistry.

[6]  Michael R Sawaya,et al.  Structural Studies of Amyloid Proteins at the Molecular Level. , 2017, Annual review of biochemistry.

[7]  R. Finke,et al.  Sigmoidal Nucleation and Growth Curves Across Nature Fit by the Finke–Watzky Model of Slow Continuous Nucleation and Autocatalytic Growth: Explicit Formulas for the Lag and Growth Times Plus Other Key Insights , 2017 .

[8]  R. Wickner,et al.  Prion Transfection of Yeast. , 2017, Cold Spring Harbor protocols.

[9]  J. Carver,et al.  Measurement of amyloid formation by turbidity assay—seeing through the cloud , 2016, Biophysical Reviews.

[10]  G. Rivas,et al.  Recognizing and analyzing variability in amyloid formation kinetics: Simulation and statistical methods. , 2016, Analytical biochemistry.

[11]  J. Carver,et al.  A multi‐pathway perspective on protein aggregation: Implications for control of the rate and extent of amyloid formation , 2015, FEBS letters.

[12]  Ivan Usov,et al.  FiberApp: An Open-Source Software for Tracking and Analyzing Polymers, Filaments, Biomacromolecules, and Fibrous Objects , 2015 .

[13]  R. Wickner,et al.  Yeast Prions: Structure, Biology, and Prion-Handling Systems , 2015, Microbiology and Molecular Reviews.

[14]  W. Cao,et al.  Rapid generation of amyloid from native proteins in vitro. , 2013, Journal of visualized experiments : JoVE.

[15]  Jian-Min Yuan,et al.  A kinetic study of amyloid formation: fibril growth and length distributions. , 2013, The journal of physical chemistry. B.

[16]  Peter Fischer,et al.  The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions , 2013, Reports on progress in physics. Physical Society.

[17]  R. Tycko,et al.  Molecular structures of amyloid and prion fibrils: consensus versus controversy. , 2013, Accounts of chemical research.

[18]  S. Auer,et al.  Two-step nucleation of amyloid fibrils: omnipresent or not? , 2012, Journal of molecular biology.

[19]  D. Hall,et al.  Computational modeling of the relationship between amyloid and disease , 2012, Biophysical Reviews.

[20]  D. Hall,et al.  On the use of size exclusion chromatography for the resolution of mixed amyloid aggregate distributions: I. equilibrium partition models. , 2012, Analytical biochemistry.

[21]  C. Brangwynne,et al.  Getting RNA and Protein in Phase , 2012, Cell.

[22]  D. Hall.  Semi-automated methods for simulation and measurement of amyloid fiber distributions obtained from transmission electron microscopy experiments. , 2012, Analytical biochemistry.

[23]  Joan-Emma Shea,et al.  Coarse-grained models for protein aggregation. , 2011, Current opinion in structural biology.

[24]  Beat Meier,et al.  Prions , 2010 .

[25]  David Eisenberg,et al.  Identifying the amylome, proteins capable of forming amyloid-like fibrils , 2010, Proceedings of the National Academy of Sciences.

[26]  D. Hall,et al.  Effects of macromolecular crowding on intracellular diffusion from a single particle perspective , 2010, Biophysical Reviews.

[27]  R. Leblanc,et al.  Surface chemistry of Alzheimer's disease: a Langmuir monolayer approach. , 2009, Colloids and surfaces. B, Biointerfaces.

[28]  D. Hall,et al.  Multi-scale modelling of amyloid formation from unfolded proteins using a set of theory derived rate constants. , 2009, Biophysical chemistry.

[29]  M. Tarlov,et al.  Aggregation kinetics of colloidal particles measured by gas-phase differential mobility analysis. , 2009, Langmuir : the ACS journal of surfaces and colloids.

[30]  Michele Vendruscolo,et al.  A Generic Mechanism of Emergence of Amyloid Protofilaments from Disordered Oligomeric Aggregates , 2008, PLoS Comput. Biol..

[31]  S. Radford,et al.  Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly , 2008, Proceedings of the National Academy of Sciences.

[32]  G. Belfort,et al.  Surface-enhanced nucleation of insulin amyloid fibrillation. , 2008, Biochemical and biophysical research communications.

[33]  D. Hall.  Chapter 4:Kinetic Models Describing Biomolecular Interactions at Surfaces , 2008 .

[34]  M. Leone,et al.  Secondary nucleation and accessible surface in insulin amyloid fibril formation. , 2008, The journal of physical chemistry. B.

[35]  M. Bailey,et al.  Apolipoprotein C-II amyloid fibrils assemble via a reversible pathway that includes fibril breaking and rejoining. , 2008, Journal of molecular biology.

[36]  Michele Vendruscolo,et al.  Structural Reorganisation and Potential Toxicity of Oligomeric Species Formed during the Assembly of Amyloid Fibrils , 2007, PLoS Comput. Biol..

[37]  S. Radford,et al.  Nucleation of protein fibrillation by nanoparticles , 2007, Proceedings of the National Academy of Sciences.

[38]  Min Zhu,et al.  Structural characterization of the partially folded intermediates of an immunoglobulin light chain leading to amyloid fibrillation and amorphous aggregation. , 2007, Biochemistry.

[39]  A. Gliozzi,et al.  Amyloid fibrils formation and amorphous aggregation in concanavalin A. , 2007, Biophysical chemistry.

[40]  T. Ban,et al.  Direct observation of amyloid growth monitored by total internal reflection fluorescence microscopy. , 2006, Methods in enzymology.

[41]  C. Dobson,et al.  A toy model for predicting the rate of amyloid formation from unfolded protein. , 2005, Journal of molecular biology.

[42]  Christopher M. Dobson,et al.  Molecular recycling within amyloid fibrils , 2005, Nature.

[43]  C. Hall,et al.  Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides. , 2004, Proceedings of the National Academy of Sciences of the United States of America.

[44]  M. R. Nilsson.  Techniques to study amyloid fibril formation in vitro. , 2004, Methods.

[45]  Michele Vendruscolo,et al.  Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. , 2004, Journal of molecular biology.

[46]  D. Hall,et al.  Silent prions lying in wait: a two-hit model of prion/amyloid formation and infection. , 2004, Journal of molecular biology.

[47]  A. Minton,et al.  Effects of inert volume-excluding macromolecules on protein fiber formation. II. Kinetic models for nucleated fiber growth. , 2004, Biophysical chemistry.

[48]  C. Ionescu-Zanetti,et al.  Surface-catalyzed Amyloid Fibril Formation* , 2002, The Journal of Biological Chemistry.

[49]  A. Minton,et al.  Effects of inert volume-excluding macromolecules on protein fiber formation. I. Equilibrium models. , 2002, Biophysical chemistry.

[50]  R. Murphy,et al.  A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state. , 2001, Biophysical journal.

[51]  J. Lewis,et al.  Nanoparticle halos: A new colloid stabilization mechanism , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[52]  D. Hall,et al.  Use of optical biosensors for the study of mechanistically concerted surface adsorption processes. , 2001, Analytical biochemistry.

[53]  P. Lansbury.  Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[54]  M A Nowak,et al.  Quantifying the kinetic parameters of prion replication. , 1999, Biophysical chemistry.

[55]  A. Fink.  Protein aggregation: folding aggregates, inclusion bodies and amyloid. , 1998, Folding & design.

[56]  K. Dill,et al.  From Levinthal to pathways to funnels , 1997, Nature Structural Biology.

[57]  D. Kirschner,et al.  On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[58]  R. L. Baldwin,et al.  On-pathway versus off-pathway folding intermediates. , 1996, Folding & design.

[59]  D. Oxtoby.  Homogeneous nucleation: theory and experiment , 1992 .

[60]  S Sugai,et al.  Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroism , 1987, FEBS letters.

[61]  P. S. Kim,et al.  Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. , 1982, Annual review of biochemistry.

[62]  Fumio Oosawa,et al.  Thermodynamics of the polymerization of protein , 1975 .

[63]  Charles H. Bennett,et al.  Serially Deposited Amorphous Aggregates of Hard Spheres , 1972 .

[64]  F. Oosawa,et al.  A theory of linear and helical aggregations of macromolecules. , 1962, Journal of molecular biology.

[65]  E. Rideal,et al.  The coalescence of drops at an oil-water interface , 1956 .

[66]  Henry Eyring,et al.  Conformation Changes of Proteins , 1954 .

[67]  M. Smoluchowski.  Versuch einer mathematischen Theorie der Koagulationskinetik kolloider Lösungen , 1918 .