Amyloid-forming peptides from beta2-microglobulin-Insights into the mechanism of fibril formation in vitro.
暂无分享,去创建一个
Susan Jones | Sheena E Radford | James Manning | S. Radford | Susan Jones | N. Kad | J. Manning | Neil M Kad
[1] C M Dobson,et al. Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain. , 2000, Journal of molecular biology.
[2] B. Chesebro,et al. Species-Independent Inhibition of Abnormal Prion Protein (PrP) Formation by a Peptide Containing a Conserved PrP Sequence , 1999, Journal of Virology.
[3] 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.
[4] G Deléage,et al. An algorithm for protein secondary structure prediction based on class prediction. , 1987, Protein engineering.
[5] A. Miranker,et al. Kidney dialysis-associated amyloidosis: a molecular role for copper in fiber formation. , 2001, Journal of molecular biology.
[6] Ehud Gazit,et al. Analysis of the Minimal Amyloid-forming Fragment of the Islet Amyloid Polypeptide , 2001, The Journal of Biological Chemistry.
[7] L Serrano,et al. Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms. , 1997, Biopolymers.
[8] Partho Ghosh,et al. The Structure and Stability of an HLA-A*0201/Octameric Tax Peptide Complex with an Empty Conserved Peptide-N-Terminal Binding Site1 , 2000, The Journal of Immunology.
[9] B. Frangione,et al. Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[10] L Serrano,et al. Protein engineering as a strategy to avoid formation of amyloid fibrils , 2000, Protein science : a publication of the Protein Society.
[11] G. Merlini,et al. Use of anti-(beta2 microglobulin) mAb to study formation of amyloid fibrils. , 1997, European journal of biochemistry.
[12] J. Floege,et al. Beta-2-microglobulin-associated amyloidosis. , 1996, Nephron.
[13] Yoshihisa Hagihara,et al. Investigation of a Peptide Responsible for Amyloid Fibril Formation of β2-Microglobulin byAchromobacter Protease I* , 2002, The Journal of Biological Chemistry.
[14] M. Skinner,et al. In vitro formation of amyloid fibrils from intact beta 2-microglobulin. , 1985, Biochemical and biophysical research communications.
[15] L. Tjernberg,et al. Arrest of -Amyloid Fibril Formation by a Pentapeptide Ligand (*) , 1996, The Journal of Biological Chemistry.
[16] C. Robinson,et al. Beta2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils. , 1998, European journal of biochemistry.
[17] T. Kawai,et al. The role of disulfide bond in the amyloidogenic state of β2‐microglobulin studied by heteronuclear NMR , 2002, Protein science : a publication of the Protein Society.
[18] M. Hoshino,et al. Mapping the core of the β2-microglobulin amyloid fibril by H/D exchange , 2002, Nature Structural Biology.
[19] P. Y. Chou,et al. Empirical predictions of protein conformation. , 1978, Annual review of biochemistry.
[20] A. Miranker,et al. Formation of a copper specific binding site in non-native states of beta-2-microglobulin. , 2002, Biochemistry.
[21] P. Kraulis. A program to produce both detailed and schematic plots of protein structures , 1991 .
[22] C. Blake,et al. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. , 1997, Advances in protein chemistry.
[23] S. Radford,et al. Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro. , 2000, Biochemistry.
[24] Y. Kallberg,et al. Prediction of Amyloid Fibril-forming Proteins* , 2001, The Journal of Biological Chemistry.
[25] W. Kabsch,et al. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.
[26] Richard B. Sessions,et al. A Designed System for Assessing How Sequence Affects α to β Conformational Transitions in Proteins* , 2002, The Journal of Biological Chemistry.
[27] Ehud Gazit,et al. A possible role for π‐stacking in the self‐assembly of amyloid fibrils , 2002, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[28] E. Lorenzi,et al. Capillary electrophoresis investigation of a partially unfolded conformation of β2‐microglobulin , 2002, Electrophoresis.
[29] S. Radford,et al. Crystal structure of monomeric human β-2-microglobulin reveals clues to its amyloidogenic properties , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[30] S. Radford,et al. Responsive gels formed by the spontaneous self-assembly of peptides into polymeric β-sheet tapes , 1997, Nature.
[31] M. Hecht,et al. Nature disfavors sequences of alternating polar and non-polar amino acids: implications for amyloidogenesis. , 2000, Journal of molecular biology.
[32] S. Radford,et al. Role of the single disulphide bond of β2‐microglobulin in amyloidosis in vitro , 2001 .
[33] Y. Argon,et al. Inhibition of amyloid fiber assembly by both BiP and its target peptide. , 2000, Immunity.
[34] J. Weissman,et al. Conformational diversity in a yeast prion dictates its seeding specificity , 2001, Nature.
[35] 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.
[36] J Q Trojanowski,et al. A Hydrophobic Stretch of 12 Amino Acid Residues in the Middle of α-Synuclein Is Essential for Filament Assembly* , 2001, The Journal of Biological Chemistry.
[37] C M Dobson,et al. Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin. , 2000, Journal of molecular biology.
[38] C. Dobson,et al. A Partially Structured Species of β2-Microglobulin Is Significantly Populated under Physiological Conditions and Involved in Fibrillogenesis* , 2001, The Journal of Biological Chemistry.
[39] 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.
[40] 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.
[41] M Levitt. Protein conformation, dynamics, and folding by computer simulation. , 1982, Annual review of biophysics and bioengineering.
[42] D A Smith,et al. Beta(2)-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro. , 2001, Journal of molecular biology.
[43] E A Merritt,et al. Raster3D Version 2.0. A program for photorealistic molecular graphics. , 1994, Acta crystallographica. Section D, Biological crystallography.
[44] Satoru Suzuki,et al. Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro , 1997 .
[45] F. Gejyo,et al. Interaction between Aβ (1-42) and Aβ (1-40) in Alzheimer's β-amyloid fibril formation in vitro , 1999 .
[46] C. Robinson,et al. Removal of the N‐terminal hexapeptide from human β2‐microglobulin facilitates protein aggregation and fibril formation , 2000, Protein science : a publication of the Protein Society.
[47] R. Doolittle,et al. A simple method for displaying the hydropathic character of a protein. , 1982, Journal of molecular biology.
[48] Robert A. Grothe,et al. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[49] S. Radford,et al. Structural properties of an amyloid precursor of β2-microglobulin , 2002, Nature Structural Biology.