Functional amyloid--from bacteria to humans.
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Atanas V Koulov | Douglas M Fowler | D. Fowler | J. Kelly | W. Balch | A. Koulov | William E Balch | Jeffery W Kelly | Atanas V. Koulov | J. Kelly
[1] Scott J. Hultgren,et al. Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation , 2002, Science.
[2] J. Mackay,et al. Structural basis for rodlet assembly in fungal hydrophobins. , 2006, Proceedings of the National Academy of Sciences of the United States of America.
[3] Y. Chernoff. Amyloidogenic domains, prions and structural inheritance: rudiments of early life or recent acquisition? , 2004, Current opinion in chemical biology.
[4] V. Uversky. Natively unfolded proteins: A point where biology waits for physics , 2002, Protein science : a publication of the Protein Society.
[5] Atanas V Koulov,et al. Functional Amyloid Formation within Mammalian Tissue , 2005, PLoS biology.
[6] Matthew R Chapman,et al. Curli biogenesis and function. , 2006, Annual review of microbiology.
[7] E. Coissac,et al. Conservation of the prion properties of Ure2p through evolution. , 2003, Molecular biology of the cell.
[8] Hong Zhang,et al. The yeast prion protein Ure2: structure, function and folding. , 2006, Biochimica et biophysica acta.
[9] P. Butko,et al. Spectroscopic evidence for amyloid-like interfacial self-assembly of hydrophobin Sc3. , 2001, Biochemical and biophysical research communications.
[10] L. Serpell,et al. Alzheimer's amyloid fibrils: structure and assembly. , 2000, Biochimica et biophysica acta.
[11] Y. Chernoff,et al. Modulation of Prion-dependent Polyglutamine Aggregation and Toxicity by Chaperone Proteins in the Yeast Model* , 2005, Journal of Biological Chemistry.
[12] G. Robillard,et al. Structural and Functional Role of the Disulfide Bridges in the Hydrophobin SC3* , 2000, The Journal of Biological Chemistry.
[13] J. Carpenter,et al. Survival of water stress in annual fish embryos: dehydration avoidance and egg envelope amyloid fibers. , 2001, American journal of physiology. Regulatory, integrative and comparative physiology.
[14] Christopher M Dobson,et al. Characterization of the nanoscale properties of individual amyloid fibrils , 2006, Proceedings of the National Academy of Sciences.
[15] P. Lansbury,et al. Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? , 1993, Cell.
[16] Susan Lindquist,et al. Prions as protein-based genetic elements. , 2002, Annual review of microbiology.
[17] G Ramachandraiah,et al. Sequence and structural determinants of mannose recognition , 2000, Proteins.
[18] I D Campbell,et al. Amyloid fibril formation by an SH3 domain. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[19] E. Kandel,et al. A Neuronal Isoform of the Aplysia CPEB Has Prion-Like Properties , 2003, Cell.
[20] P. Westermark,et al. Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[21] Laura Zanetti Polzi,et al. Calcitonin forms oligomeric pore-like structures in lipid membranes. , 2006, Biophysical journal.
[22] V. Hearing,et al. MART-1 Is Required for the Function of the Melanosomal Matrix Protein PMEL17/GP100 and the Maturation of Melanosomes* , 2005, Journal of Biological Chemistry.
[23] Gerd Krause,et al. General structural motifs of amyloid protofilaments , 2006, Proceedings of the National Academy of Sciences.
[24] U. Gophna,et al. The formation of Escherichia coli curli amyloid fibrils is mediated by prion-like peptide repeats. , 2005, Journal of molecular biology.
[25] R. Riek,et al. 3D structure of Alzheimer's amyloid-beta(1-42) fibrils. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[26] Christiane Ritter,et al. Domain organization and structure–function relationship of the HET‐s prion protein of Podospora anserina , 2003, The EMBO journal.
[27] Dennis Claessen,et al. A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils. , 2003, Genes & development.
[28] E. Voest,et al. Tissue-Type Plasminogen Activator Is a Multiligand Cross-β Structure Receptor , 2002, Current Biology.
[29] K. Wüthrich,et al. Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[30] Kenneth H. Johnson,et al. Staining methods for identification of amyloid in tissue. , 1999, Methods in enzymology.
[31] E. Peerschke,et al. Zinc-dependent activation of the plasma kinin-forming cascade by aggregated beta amyloid protein. , 1999, Clinical immunology.
[32] G. Raposo,et al. Pmel17 initiates premelanosome morphogenesis within multivesicular bodies. , 2001, Molecular biology of the cell.
[33] I. Lascu,et al. The HET-s Prion Protein of the Filamentous Fungus Podospora anserina Aggregates in Vitro into Amyloid-like Fibrils* , 2002, The Journal of Biological Chemistry.
[34] John D. Venable,et al. Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis , 2006, Cell.
[35] R. Hoekstra,et al. Non-mendelian inheritance of the HET-s prion or HET-s prion domains determines the het-S spore killing system in Podospora anserina. , 2005, Fungal genetics and biology : FG & B.
[36] R. Riek,et al. 3D structure of Alzheimer's amyloid-β(1–42) fibrils , 2005 .
[37] G. Vriend,et al. Amyloids protect the silkmoth oocyte and embryo , 2000, FEBS letters.
[38] A. Mitraki,et al. Natural Triple -Stranded Fibrous Folds 1 , 2006 .
[39] Dennis C Winkler,et al. Filaments of the Ure2p prion protein have a cross-β core structure , 2005 .
[40] C. Anfinsen. Principles that govern the folding of protein chains. , 1973, Science.
[41] S. Lindquist,et al. Rnq1: an epigenetic modifier of protein function in yeast. , 2000, Molecular cell.
[42] R. Hoekstra,et al. Sexual transmission of the [Het-s] prion leads to meiotic drive in Podospora anserina , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[43] G. Raposo,et al. The Dark Side of Lysosome‐Related Organelles: Specialization of the Endocytic Pathway for Melanosome Biogenesis , 2002, Traffic.
[44] R. Tycko,et al. Amyloid of the prion domain of Sup35p has an in-register parallel β-sheet structure , 2006, Proceedings of the National Academy of Sciences.
[45] Susan Lindquist,et al. Prions as adaptive conduits of memory and inheritance , 2005, Nature Reviews Genetics.
[46] Dennis Claessen,et al. Amyloids — a functional coat for microorganisms , 2005, Nature Reviews Microbiology.
[47] S. Lindquist,et al. Nucleated conformational conversion and the replication of conformational information by a prion determinant. , 2000, Science.
[48] L. Serpell,et al. Structure and morphology of the Alzheimer's amyloid fibril , 2005, Microscopy research and technique.
[49] R. Wickner,et al. Prion domain initiation of amyloid formation in vitro from native Ure2p. , 1999, Science.
[50] J. Keen,et al. Variations in the csgD Promoter of Escherichia coli O157:H7 Associated with Increased Virulence in Mice and Increased Invasion of HEp-2 Cells , 2002, Infection and Immunity.
[51] R. R. Bowers,et al. Premature avian melanocyte death due to low antioxidant levels of protection: fowl model for vitiligo. , 1994, Pigment cell research.
[52] Fabrizio Chiti,et al. Sequence and structural determinants of amyloid fibril formation. , 2006, Accounts of chemical research.
[53] Stanley B. Prusiner,et al. Nobel Lecture: Prions , 1998 .
[54] K. Iwata,et al. 3D structure of amyloid protofilaments of β2-microglobulin fragment probed by solid-state NMR , 2006, Proceedings of the National Academy of Sciences.
[55] G. Raposo,et al. The Silver locus product Pmel17/gp100/Silv/ME20: controversial in name and in function. , 2005, Pigment cell research.
[56] V. Coustou,et al. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[57] Thorsten Lührs,et al. Correlation of structural elements and infectivity of the HET-s prion , 2005, Nature.
[58] Ž. Eva. Amyloid-fibril formation: Proposed mechanisms and relevance to conformational disease , 2002 .
[59] P. Lansbury,et al. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? , 2006, Quarterly Reviews of Biophysics.
[60] M. Jensen,et al. Molecular population genetics and evolution of a prion-like protein in Saccharomyces cerevisiae. , 2001, Genetics.
[61] 芝山 洋二. Zinc-dependent activation of the plasma kinin-forming cascade by aggregated β amyloid protein , 2000 .
[62] Andreas Hoenger,et al. Amyloid fibril formation propensity is inherent into the hexapeptide tandemly repeating sequence of the central domain of silkmoth chorion proteins of the A-family. , 2006, Journal of structural biology.
[63] O. Bocharova,et al. Amyloid Fibrils of Mammalian Prion Protein Are Highly Toxic to Cultured Cells and Primary Neurons* , 2006, Journal of Biological Chemistry.
[64] H. True,et al. A yeast prion provides a mechanism for genetic variation and phenotypic diversity , 2000, Nature.
[65] R. R. Bowers,et al. Fowl model for vitiligo: genetic regulation on the fate of the melanocytes. , 2008, Pigment cell research.
[66] C. Dobson,et al. Protein misfolding, functional amyloid, and human disease. , 2006, Annual review of biochemistry.
[67] Robert A. Grothe,et al. Structure of the cross-β spine of amyloid-like fibrils , 2005, Nature.
[68] S. Lindquist,et al. Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. , 2006, Molecular cell.
[69] C. Colaco,et al. Amyloid fibril formation , 1994, Bio/Technology.
[70] F. Vollrath,et al. Amyloidogenic nature of spider silk. , 2002, European journal of biochemistry.
[71] Heather L. True,et al. Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits , 2004, Nature.
[72] R. Wickner,et al. Yeast prions [URE3] and [PSI+] are diseases. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[73] Gary W. Jones,et al. Yeast prions , 1995 .
[74] J. Mackay,et al. The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures. , 2001, Structure.
[75] Fred E. Cohen,et al. Therapeutic approaches to protein-misfolding diseases , 2003, Nature.
[76] S. Müller,et al. Hsp70 Chaperones as Modulators of Prion Life Cycle , 2005, Genetics.
[77] 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.
[78] Peter Chien,et al. Emerging principles of conformation-based prion inheritance. , 2004, Annual review of biochemistry.
[79] G. Raposo,et al. Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis , 2003, The Journal of cell biology.
[80] S. Lindquist,et al. The role of Sis1 in the maintenance of the [RNQ+] prion , 2001, The EMBO journal.
[81] M. Aigle,et al. The [URE3] Prion Is Not Conserved Among Saccharomyces Species , 2005, Genetics.