Amyloid fibrils formation and amorphous aggregation in concanavalin A

Harper, 1997, Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins, Annu. Rev. Biochem., 66, 385, 10.1146/annurev.biochem.66.1.385

Kelly, 1998, The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways, Curr. Opin. Struct. Biol., 8, 101, 10.1016/S0959-440X(98)80016-X

Bellotti, 2000, Immunoglobulin light chain amyloidoses. The archetype of structural and pathogenic variability, J. Struct. Biol., 130, 280, 10.1006/jsbi.2000.4248

Rochet, 2000, Amyloid fibrillogenesis: themes and variations, Curr. Opin. Struct. Biol., 10, 60, 10.1016/S0959-440X(99)00049-4

Collinge, 2001, Prion diseases of humans and animals: their causes and molecular basis, Annu. Rev. Neurosci., 24, 519, 10.1146/annurev.neuro.24.1.519

Uversky, 2004, Conformational constraints for amyloid fibrillation: the importance of being unfolded, Biochim. Biophys. Acta, 1698, 131, 10.1016/j.bbapap.2003.12.008

Jiménez, 1999, Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing, EMBO J., 18, 815, 10.1093/emboj/18.4.815

Serpell, 2000, Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation, Proc. Natl. Acad. Sci. U. S. A., 97, 4897, 10.1073/pnas.97.9.4897

Stefani, 2004, Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world, Biochim. Biophys. Acta, 1739, 5, 10.1016/j.bbadis.2004.08.004

Fandrich, 2002, The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation, EMBO J., 21, 5682, 10.1093/emboj/cdf573

Chiti, 2002, Kinetic partitioning of protein folding and aggregation, Nat. Struct. Biol., 9, 137, 10.1038/nsb752

Khurana, 2001, Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates, Biochemistry, 40, 3525, 10.1021/bi001782b

Militello, 2003, Conformational changes involved in thermal aggregation processes of bovine serum albumin, Biophys. Chemist., 105, 133, 10.1016/S0301-4622(03)00153-4

Vaiana, 2004, Irreversible formation of intermediate BSA oligomers requires and induces conformational changes, Proteins, 55, 1053, 10.1002/prot.20074

Vetri, 2005, Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin, Biophys. Chem., 113, 83, 10.1016/j.bpc.2004.07.042

Booth, 1997, Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis, Nature, 385, 787, 10.1038/385787a0

Arai, 1999, Reversibility and hierarchy of thermal transition of hen egg-white lysozyme studied by small-angle X-ray scattering, Biophys. J., 76, 2192, 10.1016/S0006-3495(99)77374-1

Hamada, 2002, A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea, Protein Sci., 11, 2417, 10.1110/ps.0217702

Senear, 1981, Effects of saccharide and salt binding on dimer–tetramer equilibrium of concanavalin A, Biochemistry, 20, 3076, 10.1021/bi00514a014

Bhattacharyya, 1991, Interactions of asparagine-linked carbohydrates with concanavalin A. Nuclear magnetic relaxation dispersion and circular dichroism studies, J. Biol. Chem., 266, 9835, 10.1016/S0021-9258(18)92895-4

Hardman, 1982, Manganese and calcium binding sites of concanavalin A, J. Mol. Biol., 5, 69, 10.1016/0022-2836(82)90513-7

Sanders, 1998, Effect of metal ion substitutions in concanavalin A on the binding of carbohydrates and on thermal stability, J. Inorg. Biochem., 70, 71, 10.1016/S0162-0134(98)00016-6

Chatterjee, 2005, Quaternary association and reactivation of dimeric concanavalin A, Int. J. Biol. Macromol., 35, 103, 10.1016/j.ijbiomac.2005.01.005

Sinha, 2005, Unfolding studies on soybean agglutinin and concanavalin A tetramers: a comparative account, Biophys. J., 88, 1300, 10.1529/biophysj.104.051052

Mitra, 2002, Conformational stability of legume lectins reflect their different modes of quaternary association: solvent denaturation studies on concanavalin A and winged bean acidic agglutin, Biochemistry, 41, 9256, 10.1021/bi020240m

Emsley, 1994, Structure of pentameric human serum amyloid P component, Nature, 367, 338, 10.1038/367338a0

Pflumm, 1974, Alkali and urea induced conformation changes in concanavalin A, Biochemistry, 13, 4982, 10.1021/bi00721a017

Xu, 2005, Trifluoroethanol-induced unfolding of concanavalin A: equilibrium and time-resolved optical spectroscopic studies, Biochemistry, 44, 7976, 10.1021/bi050003u

Fink, 1998, Protein aggregation: folding aggregates, inclusion bodies and amyloid, Fold. Des., 3, 9, 10.1016/S1359-0278(98)00002-9

Richardson, 2002, Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation, Proc. Natl. Acad. Sci. U. S. A., 99, 2754, 10.1073/pnas.052706099

Dam, 2000, Binding of multivalent carbohydrates to concanavalin A and Dioclea Grandiflora lectin, J. Biol. Chem., 275, 14230, 10.1074/jbc.275.19.14223

Dam, 2002, Negative cooperativity associated with binding of multivalent carbohydrates to lectins. Thermodynamic analysis of the “multivalency effect”, Biochemistry, 41, 1351, 10.1021/bi015830j

Dam, 2002, Thermodynamic binding parameters of individual epitopes of multivalent carbohydrates to concanavalin A as determined by “reverse” isothermal titration microcalorimetry, Biochemistry, 41, 1359, 10.1021/bi015829k

Mangold, 2006, Binding of monomeric and dimeric concanavalin A to mannose-functionalized dendrimers, Org. Biomol. Chem., 4, 2458, 10.1039/b600066e

Tiegs, 1992, A T cell-dependent experimental liver injury in mice inducible by concanavalin A, J. Clin. Invest., 90, 196, 10.1172/JCI115836

Ohta, 2001, Role of G-protein-coupled adenosine receptors in downregulation of inflammation and protection from tissue damage, Nature, 414, 916, 10.1038/414916a

Song, 2003, RNA interference targeting Fas protects mice from fulminant hepatitis, Nat. Med., 9, 347, 10.1038/nm828

Moreno, 2005, CCR5 deficiency exacerbates T-cell-mediated hepatitis in mice, Hepatology, 42, 854, 10.1002/hep.20865

Fukuda, 2005, Therapeutic administration of Y-40138, a multiple cytokine modulator, inhibits concanavalin A-induced hepatitis in mice, Eur. J. Pharmacol., 523, 137, 10.1016/j.ejphar.2005.08.060

Cribbs, 1996, Cross-linking of concanavalin receptors on cortical neurons induces programmed cell death, Neuroscience, 75, 173, 10.1016/0306-4522(96)80001-P

Anderson, 1995, Differential induction of immediate early gene proteins in cultured neurons by beta-amyloid (Aβ): association of c-jun with Aβ-induced apoptosis, J. Neurochem., 65, 1487, 10.1046/j.1471-4159.1995.65041487.x

Naiki, 1989, Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T, Anal. Biochem., 177, 244, 10.1016/0003-2697(89)90046-8

Naiki, 1999, Kinetic analysis of amyloid fibril formation, Methods Enzymol., 309, 305, 10.1016/S0076-6879(99)09022-9

Kudou, 2004, Characterization of heat-induced aggregates of concanavalin A using fluorescent probes, Sci. Technol. Adv. Mater., 5, 339, 10.1016/j.stam.2003.12.012

Bouckaert, 1995, Crystallographic structure of metal-free concanavalin A at 2.5Å resolution, Proteins, 23, 510, 10.1002/prot.340230406

Sanz-Aparicio, 1997, The crystal structure of Canavalia brasiliensis lectin suggest a correlation between its quaternary conformation and its distinct biological properties from concanavalin A, FEBS Lett., 17, 114, 10.1016/S0014-5793(97)00137-3

Relini, 2004, Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils, J. Mol. Biol., 338, 943, 10.1016/j.jmb.2004.03.054

Relini, 2004, Ultrastructural organization of ex-vivo amyloid fibrils formed by the apolipoprotein A-I Leu174Ser variant: an atomic force microscopy study, Biochim. Biophys. Acta, 1690, 33, 10.1016/j.bbadis.2004.04.007

Kudou, 2005, Stretched-exponential analysis of heat-induced aggregation of apo–concanavalin A, Prot. J., 24, 193, 10.1007/s10930-005-7843-4

Kelly, 1997, Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases, Structure, 5, 595, 10.1016/S0969-2126(97)00215-3

Lashuel, 1998, Characterization of the transthyretin acid denaturation pathway by analytical ultracentrifugation: implications for wild type, V30M and L55P amyloid fibril formation, Biochemistry, 37, 17851, 10.1021/bi981876+

Quintas, 1999, The tetrameric protein transthyretin dissociates to a non-native monomer in solution, J. Biol. Chem., 274, 32943, 10.1074/jbc.274.46.32943

Quintas, 2001, Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants, J. Biol. Chem., 276, 27207, 10.1074/jbc.M101024200

Foss, 2005, The pathway by which the tetrameric protein transthyretin dissociates, Biochemistry, 44, 15525, 10.1021/bi051608t

Ferrone, 1999, Analysis of protein aggregation kinetics, Methods Enzymol., 309, 256, 10.1016/S0076-6879(99)09019-9

Padrick, 2002, Islet amyloid: phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis, Biochemistry, 41, 4694, 10.1021/bi0160462

Librizzi, 2005, The kinetic behavior of insulin fibrillation is determined by heterogeneous nucleation pathways, Protein Sci., 14, 3129, 10.1110/ps.051692305

Manno, 2006, Kinetics of insulin aggregation: disentanglement of amyloid fibrillation from large-size cluster formation, Biophys. J., 90, 4585, 10.1529/biophysj.105.077636

Carrotta, 2005, Protofibril formation of amyloid β-protein at low pH via a non-cooperative elongation mechanism, J. Biol. Chem., 280, 30001, 10.1074/jbc.M500052200