Emerging ideas on the molecular basis of protein and peptide aggregation.

[1]  J. Griffith,et al.  Nature of the Scrapie Agent: Self-replication and Scrapie , 1967, Nature.

[2]  J. Griffith,et al.  Self-replication and scrapie. , 1967, Nature.

[3]  C. Anfinsen.  Principles that govern the folding of protein chains. , 1973, Science.

[4]  P. Y. Chou,et al.  Empirical predictions of protein conformation. , 1978, Annual review of biochemistry.

[5]  J. Hofrichter,et al.  Sickle cell hemoglobin polymerization. , 1990, Advances in protein chemistry.

[6]  P. Kraulis.  A program to produce both detailed and schematic plots of protein structures , 1991 .

[7]  B. Rost,et al.  Prediction of protein secondary structure at better than 70% accuracy. , 1993, Journal of molecular biology.

[8]  P. Lansbury,et al.  The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. , 1993, Biochemistry.

[9]  P. Lansbury,et al.  The C‐Terminus of the β Protein is Critical in Amyloidogenesis a , 1993 .

[10]  E. Mandelkow,et al.  Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. , 1994, The Journal of biological chemistry.

[11]  J. Thornton,et al.  Satisfying hydrogen bonding potential in proteins. , 1994, Journal of molecular biology.

[12]  Eric J. Simon,et al.  Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide , 1995, Nature Structural Biology.

[13]  J R Ghilardi,et al.  1H NMR of A beta amyloid peptide congeners in water solution. Conformational changes correlate with plaque competence. , 1995, Biochemistry.

[14]  P. Lansbury,et al.  Non-genetic propagation of strain-specific properties of scrapie prion protein , 1995, Nature.

[15]  J. Hofrichter,et al.  The biophysics of sickle cell hydroxyurea therapy. , 1995, Science.

[16]  Andrew F. Hill,et al.  Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD , 1996, Nature.

[17]  J. Kelly,et al.  Alternative conformations of amyloidogenic proteins govern their behavior. , 1996, Current opinion in structural biology.

[18]  G. Lorimer,et al.  A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo , 1996, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[19]  C. Sander,et al.  Errors in protein structures , 1996, Nature.

[20]  M. Billeter,et al.  MOLMOL: a program for display and analysis of macromolecular structures. , 1996, Journal of molecular graphics.

[21]  W. Surewicz,et al.  pH-dependent Stability and Conformation of the Recombinant Human Prion Protein PrP(90–231)* , 1997, The Journal of Biological Chemistry.

[22]  Rolf Apweiler,et al.  The SWISS-PROT protein sequence data bank and its supplement TrEMBL , 1997, Nucleic Acids Res..

[23]  P. Lansbury,et al.  Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. , 1997, Annual review of biochemistry.

[24]  D. Selkoe,et al.  Heparin-binding properties of the amyloidogenic peptides Abeta and amylin. Dependence on aggregation state and inhibition by Congo red. , 1997, The Journal of biological chemistry.

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

[26]  S. Hornemann,et al.  A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[27]  T. Benzinger,et al.  Propagating structure of Alzheimer’s β-amyloid(10–35) is parallel β-sheet with residues in exact register , 1998 .

[28]  T. Morgan,et al.  Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[29]  F. Cohen,et al.  Eight prion strains have PrPSc molecules with different conformations , 1998, Nature Medicine.

[30]  J. Kelly,et al.  The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. , 1998, Current opinion in structural biology.

[31]  T. Benzinger,et al.  Propagating structure of Alzheimer's beta-amyloid(10-35) is parallel beta-sheet with residues in exact register. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[32]  C. Dobson.  Protein misfolding, evolution and disease. , 1999, Trends in biochemical sciences.

[33]  M. Hecht,et al.  De novo amyloid proteins from designed combinatorial libraries. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[34]  D. Selkoe,et al.  Title Amyloid β-protein fibrillogenesis . Structure and biological activity of protofibrillar intermediates , 1999 .

[35]  C M Dobson,et al.  Designing conditions for in vitro formation of amyloid protofilaments and fibrils. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[36]  Peter T. Lansbury,et al.  Assembly of Aβ Amyloid Protofibrils: An in Vitro Model for a Possible Early Event in Alzheimer's Disease† , 1999 .

[37]  Inyoul Y. Lee,et al.  Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel. , 1999, Journal of molecular biology.

[38]  D. Selkoe,et al.  Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. , 1999, The Journal of biological chemistry.

[39]  D. Otzen,et al.  Salt-induced detour through compact regions of the protein folding landscape. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[40]  S. Prusiner,et al.  A mouse prion protein transgene rescues mice deficient for the prion protein gene from purkinje cell degeneration and demyelination. , 1999, Laboratory investigation; a journal of technical methods and pathology.

[41]  S. Prusiner,et al.  Compelling transgenetic evidence for transmission of bovine spongiform encephalopathy prions to humans. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[42]  R. Leapman,et al.  Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils , 2000 .

[43]  J R Ghilardi,et al.  Activation barriers to structural transition determine deposition rates of Alzheimer's disease a beta amyloid. , 2000, Journal of structural biology.

[44]  R. Tycko.  Solid-state NMR as a probe of amyloid fibril structure. , 2000, Current opinion in chemical biology.

[45]  D. M. Morgan,et al.  Structure of the β-Amyloid(10-35) Fibril , 2000 .

[46]  Rolf Apweiler,et al.  The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000 , 2000, Nucleic Acids Res..

[47]  D. Thirumalai,et al.  Native topology determines force-induced unfolding pathways in globular proteins. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[48]  P. Lansbury,et al.  Amyloid fibrillogenesis: themes and variations. , 2000, Current opinion in structural biology.

[49]  B Frangione,et al.  Substitutions at codon 22 of Alzheimer's abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells. , 2000, The Journal of biological chemistry.

[50]  L. Regan,et al.  A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[51]  S. Lindquist,et al.  Nucleated conformational conversion and the replication of conformational information by a prion determinant. , 2000, Science.

[52]  D. Otzen,et al.  Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[53]  J. M. Smith,et al.  Direct visualisation of the beta-sheet structure of synthetic Alzheimer's amyloid. , 2000, Journal of molecular biology.

[54]  B. Austen,et al.  Oligomerization of beta-amyloid of the Alzheimer's and the Dutch-cerebral-haemorrhage types. , 2000, The Biochemical journal.

[55]  R. Leapman,et al.  Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer's β-Amyloid Peptide, and Structural Characterization by Solid State NMR† , 2000 .

[56]  Giuliano Siligardi,et al.  Oligomerization of β-amyloid of the Alzheimer’s and the Dutch-cerebral-haemorrhage types , 2000 .

[57]  R. Kisilevsky.  Review: amyloidogenesis-unquestioned answers and unanswered questions. , 2000, Journal of structural biology.

[58]  F E Cohen,et al.  Mapping the early steps in the pH-induced conformational conversion of the prion protein , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[59]  Y. Kallberg,et al.  Prediction of Amyloid Fibril-forming Proteins* , 2001, The Journal of Biological Chemistry.

[60]  M. Kirkitadze,et al.  Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis. , 2001, Journal of molecular biology.

[61]  F E Cohen,et al.  Folding of prion protein to its native alpha-helical conformation is under kinetic control. , 2001, The Journal of biological chemistry.

[62]  D. Selkoe.  Alzheimer's disease: genes, proteins, and therapy. , 2001, Physiological reviews.

[63]  J. Straub,et al.  Probing the origins of increased activity of the E22Q "Dutch" mutant Alzheimer's beta-amyloid peptide. , 2001, Biophysical journal.

[64]  F. Cohen,et al.  Two different neurodegenerative diseases caused by proteins with similar structures , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[65]  J. Straub,et al.  Energy landscape theory for Alzheimer's amyloid beta-peptide fibril elongation. , 2001, Proteins.

[66]  R. Riek,et al.  NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, A beta(1-40)(ox) and A beta(1-42)(ox). , 2001, European journal of biochemistry.

[67]  J. Straub,et al.  Simulation study of the structure and dynamics of the Alzheimer's amyloid peptide congener in solution. , 2001, Biophysical journal.

[68]  Witold K. Surewicz,et al.  Crystal structure of the human prion protein reveals a mechanism for oligomerization , 2002, Nature Structural Biology.

[69]  J. King,et al.  Frequencies of amino acid strings in globular protein sequences indicate suppression of blocks of consecutive hydrophobic residues , 2001, Protein science : a publication of the Protein Society.

[70]  F. Cohen,et al.  Conformational propagation with prion‐like characteristics in a simple model of protein folding , 2001, Protein science : a publication of the Protein Society.

[71]  David Eisenberg,et al.  A domain-swapped RNase A dimer with implications for amyloid formation , 2001, Nature Structural Biology.

[72]  J T Finch,et al.  Amyloid fibers are water-filled nanotubes , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[73]  T. Yeates,et al.  Arrangement of subunits and ordering of β-strands in an amyloid sheet , 2002, Nature Structural Biology.

[74]  W. Goux.  The conformations of filamentous and soluble tau associated with Alzheimer paired helical filaments. , 2002, Biochemistry.

[75]  J. Straub,et al.  Charge states rather than propensity for beta-structure determine enhanced fibrillogenesis in wild-type Alzheimer's beta-amyloid peptide compared to E22Q Dutch mutant. , 2002, Protein science : a publication of the Protein Society.

[76]  W. K. Cullen,et al.  Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo , 2002, Nature.

[77]  M. Kirkitadze,et al.  Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[78]  C. Dobson,et al.  Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases , 2002, Nature.

[79]  Christopher M. Dobson,et al.  The protofilament structure of insulin amyloid fibrils , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[80]  D. Thirumalai,et al.  Exploring the Propensities of Helices in PrP to Form Sheet Using NMR Structures and Sequence Alignments , 2002 .

[81]  R. Leapman,et al.  A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[82]  R. Nussinov,et al.  Stabilities and conformations of Alzheimer's β-amyloid peptide oligomers (Aβ16–22, Aβ16–35, and Aβ10–35): Sequence effects , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[83]  J. Hardy,et al.  The Amyloid Hypothesis of Alzheimer ’ s Disease : Progress and Problems on the Road to Therapeutics , 2009 .

[84]  M. Hecht,et al.  Rationally designed mutations convert de novo amyloid-like fibrils into monomeric β-sheet proteins , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[85]  S. Prusiner,et al.  Locally disordered conformer of the hamster prion protein: a crucial intermediate to PrPSc? , 2002, Biochemistry.

[86]  R. Nussinov,et al.  Molecular dynamics simulations of alanine rich β‐sheet oligomers: Insight into amyloid formation , 2002, Protein science : a publication of the Protein Society.

[87]  D. Thirumalai,et al.  Exploring protein aggregation and self‐propagation using lattice models: Phase diagram and kinetics , 2002, Protein science : a publication of the Protein Society.

[88]  J. Richardson,et al.  Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[89]  D. Thirumalai,et al.  Exploring the propensities of helices in PrP(C) to form beta sheet using NMR structures and sequence alignments. , 2002, Biophysical journal.

[90]  Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity , 2002 .

[91]  V. Muñoz,et al.  Alpha-helix structure in Alzheimer's disease aggregates of tau-protein. , 2002, Biochemistry.

[92]  D. Thirumalai,et al.  Dissecting the Assembly of Aβ16–22 Amyloid Peptides into Antiparallel β Sheets , 2003 .

[93]  J. Kelly,et al.  Prevention of Transthyretin Amyloid Disease by Changing Protein Misfolding Energetics , 2003, Science.

[94]  D. Thirumalai,et al.  Dissecting the assembly of Abeta16-22 amyloid peptides into antiparallel beta sheets. , 2003, Structure.

[95]  M. Kirkitadze,et al.  Amyloid b-protein (Ab) assembly: Ab40 and Ab42 oligomerize through distinct pathways , 2003 .