Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins

[1]  L. Serrano,et al.  Sequence determinants of amyloid fibril formation , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[2]  P. Lansbury,et al.  Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. , 2003, Annual review of neuroscience.

[3]  C. Dobson,et al.  Rationalization of the effects of mutations on peptide andprotein aggregation rates , 2003, Nature.

[4]  Fabrizio Chiti,et al.  Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[5]  Christopher M. Dobson,et al.  Protein-misfolding diseases: Getting out of shape , 2002, Nature.

[6]  R. Samudrala Faculty Opinions recommendation of Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations. , 2002 .

[7]  L. Serrano,et al.  Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations. , 2002, Journal of molecular biology.

[8]  C. Dobson,et al.  Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme , 2002, Nature Structural Biology.

[9]  Christopher M. Dobson,et al.  Kinetic partitioning of protein folding and aggregation , 2002, Nature Structural Biology.

[10]  Christopher M Dobson,et al.  Getting out of shape. , 2002, Nature.

[11]  C Redfield,et al.  Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy , 2001, Protein science : a publication of the Protein Society.

[12]  J. Kelly,et al.  Trans-Suppression of Misfolding in an Amyloid Disease , 2001, Science.

[13]  L Serrano,et al.  Computer-aided design of beta-sheet peptides. , 2001, Journal of molecular biology.

[14]  S. Younkin,et al.  The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation , 2001, Nature Neuroscience.

[15]  C. Dobson The structural basis of protein folding and its links with human disease. , 2001, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[16]  V. Shnyrov,et al.  Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin. , 2000, Biophysical chemistry.

[17]  C. Dobson,et al.  Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants. , 2000, Journal of structural biology.

[18]  M. Saraiva,et al.  Comparative studies of two transthyretin variants with protective effects on familial amyloidotic polyneuropathy: TTR R104H and TTR T119M. , 2000, Biochemical and biophysical research communications.

[19]  J. Treanor,et al.  Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. , 1999, Science.

[20]  L Serrano,et al.  Elucidating the folding problem of alpha-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters. , 1998, Journal of molecular biology.

[21]  R. Brito,et al.  The amyloidogenic potential of transthyretin variants correlates with their tendency to aggregate in solution , 1997, FEBS letters.

[22]  L Serrano,et al.  Role of beta-turn residues in beta-hairpin formation and stability in designed peptides. , 1997, Journal of molecular biology.

[23]  R. L. Baldwin,et al.  Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. , 1997, Biochemistry.

[24]  Christopher M. Dobson,et al.  Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis , 1997, Nature.

[25]  H. Naiki,et al.  First-order kinetic model of Alzheimer's beta-amyloid fibril extension in vitro. , 1996, Laboratory investigation; a journal of technical methods and pathology.

[26]  J. Kelly,et al.  Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease. , 1995, Biochemistry.

[27]  L Serrano,et al.  Folding of protein G B1 domain studied by the conformational characterization of fragments comprising its secondary structure elements. , 1995, European journal of biochemistry.

[28]  D. Booth,et al.  Human lysozyme gene mutations cause hereditary systemic amyloidosis , 1993, Nature.

[29]  B. Matthews Comparison of the predicted and observed secondary structure of T4 phage lysozyme. , 1975, Biochimica et biophysica acta.