Crossref journal-article
Elsevier BV
Journal of Molecular Biology (78)
Bibliography

Päiviö, A., Jarvet, J., Gräslund, A., Lannfelt, L., & Westlind-Danielsson, A. (2004). Unique Physicochemical Profile of β-Amyloid Peptide Variant Aβ1–40E22G Protofibrils: Conceivable Neuropathogen in Arctic Mutant Carriers. Journal of Molecular Biology, 339(1), 145–159.

Authors 5
  1. A Päiviö (first)
  2. J Jarvet (additional)
  3. A Gräslund (additional)
  4. L Lannfelt (additional)
  5. A Westlind-Danielsson (additional)
References 62 Referenced 70
  1. 10.1038/ng0692-218 / Nature Genet. / Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the beta-amyloid precursor protein gene by Hendriks (1992)
  2. 10.1126/science.2111584 / Science / Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type by Levy (1990)
  3. 10.1126/science.1971458 / Science / Amyloid beta protein precursor gene and hereditary cerebral hemorrhage with amyloidosis (Dutch) by Van Broeckhoven (1990)
  4. 10.1212/WNL.50.3.688 / Neurology / Fatal familial insomnia: genetic, neuropathologic, and biochemical study of a patient from a new Italian kindred. by Rossi (1998)
  5. 10.1038/nn0901-887 / Nature Neurosci. / The Arctic APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation by Nilsberth (2001)
  6. 10.1002/ana.1009 / Ann. Neurol. / Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy by Grabowski (2001)
  7. 10.1002/ana.10040 / Ann. Neurol. / Dementia in hereditary cerebral hemorrhage with amyloidosis—Dutch type is associated with cerebral amyloid angiopathy but is independent of plaques and neurofibrillary tangles by Natte (2001)
  8. 10.1016/S0002-9440(10)64207-1 / Am. J. Pathol. / Dense-core senile plaques in the Flemish variant of Alzheimer's disease are vasocentric by Kumar-Singh (2002)
  9. 10.1007/s00401-002-0639-0 / Acta Neuropathol. (Berl) / Abeta species, including IsoAsp23 Abeta, in Iowa-type familial cerebral amyloid angiopathy by Shin (2003)
  10. 10.1074/jbc.271.50.32185 / J. Biol. Chem. / The length of amyloid-beta in hereditary cerebral hemorrhage with amyloidosis, Dutch type. Implications for the role of amyloid-beta 1–42 in Alzheimer's disease by Castano (1996)
  11. 10.1111/j.1749-6632.2002.tb04810.x / Ann. NY Acad. Sci. / Enhanced Abeta40 deposition was associated with increased Abeta42–43 in cerebral vasculature with Dutch-type hereditary cerebral hemorrhage with amyloidosis (HCHWA-D) by Ozawa (2002)
  12. 10.1111/j.1750-3639.1996.tb00794.x / Brain Pathol. / Hereditary cerebral hemorrhage with amyloidosis-Dutch type (HCHWA-D). II. A review of histopathological aspects by Maat-Schieman (1996)
  13. 10.1007/BF00310382 / Acta Neuropathol. (Berl) / Hereditary cerebral hemorrhage with amyloidosis (Dutch): a model for congophilic plaque formation without neurofibrillary pathology by Maat-Schieman (1994)
  14. 10.1016/0006-291X(91)91706-I / Biochem. Biophys. Res. Commun. / Peptides homologous to the amyloid protein of Alzheimer's disease containing a glutamine for glutamic acid substitution have accelerated amyloid fibril formation by Wisniewski (1991)
  15. 10.1021/bi00159a011 / Biochemistry / Fibril formation by primate, rodent, and Dutch-hemorrhagic analogues of Alzheimer amyloid beta-protein by Fraser (1992)
  16. 10.1042/bj3550869 / Biochem. J. / In vitro studies of amyloid beta-protein fibril assembly and toxicity provide clues to the aetiology of Flemish variant (Ala692→Gly) Alzheimer's disease by Walsh (2001)
  17. 10.1016/S0021-9258(19)61486-9 / J. Biol. Chem. / Substitutions at codon 22 of Alzheimer's abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells by Miravalle (2000)
  18. 10.1074/jbc.M104135200 / J. Biol. Chem. / Pathogenic effects of D23N Iowa mutant amyloid beta-protein by Van Nostrand (2001)
  19. 10.1006/jmbi.2001.4970 / J. Mol. Biol. / Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis by Kirkitadze (2001)
  20. 10.1016/S0021-9258(17)32503-6 / J. Biol. Chem. / Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid beta-protein precursor by Haass (1994)
  21. 10.1097/00001756-200210280-00005 / Neuroreport / The Arctic mutation interferes with processing of the amyloid precursor protein by Stenh (2002)
  22. 10.1016/S0140-6736(03)13555-6 / Lancet / Dutch, Flemish, Italian, and Arctic mutations of APP and resistance of Abeta to physiologically relevant proteolytic degradation by Tsubuki (2003)
  23. 10.1016/S0197-4580(01)00317-7 / Neurobiol. Aging / Substitution at codon 22 reduces clearance of Alzheimer's amyloid-beta peptide from the cerebrospinal fluid and prevents its transport from the central nervous system into blood by Monro (2002)
  24. 10.1161/01.STR.31.2.534 / Stroke / Toxicity of Dutch (E22Q) and Flemish (A21G) mutant amyloid beta proteins to human cerebral microvessel and aortic smooth muscle cells by Wang (2000)
  25. 10.1073/pnas.93.7.2996 / Proc. Natl Acad. Sci. USA / Enhanced pathologic properties of Dutch-type mutant amyloid beta-protein by Davis (1996)
  26. 10.1046/j.1471-4159.2000.0742209.x / J. Neurochem. / Charge alterations of E22 enhance the pathogenic properties of the amyloid beta-protein by Melchor (2000)
  27. 10.1046/j.1471-4159.1997.68031135.x / J. Neurochem. / Rapid degeneration of cultured human brain pericytes by amyloid beta protein by Verbeek (1997)
  28. 10.1042/bse0380037 / Essays Biochem. / Proteolytic processing of the amyloid-beta protein precursor of Alzheimer's disease by Nunan (2002)
  29. 10.1016/0092-8674(93)90635-4 / Cell / Seeding one-dimensional crystallization of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? by Jarrett (1993)
  30. 10.1074/jbc.272.35.22364 / J. Biol. Chem. / Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate by Walsh (1997)
  31. 10.1016/S1074-5521(97)90255-6 / Chem. Biol. / Observation of metastable Abeta amyloid protofibrils by atomic force microscopy by Harper (1997)
  32. 10.1073/pnas.95.11.6448 / Proc. Natl Acad. Sci. USA / Diffusible nonfibrillar ligands derived from Abeta1–42 are potent central nervous system neurotoxins by Lambert (1998)
  33. 10.1074/jbc.M210207200 / J. Biol. Chem. / In vitro characterization of conditions for amyloid-peptide oligomerization and fibrillogenesis by Stine (2003)
  34. 10.1074/jbc.274.36.25945 / J. Biol. Chem. / Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates by Walsh (1999)
  35. 10.1016/S1074-5521(97)90303-3 / Chem. Biol. / Observation of metastable Abeta amyloid protofibrils by atomic force microscopy by Harper (1997)
  36. 10.1523/JNEUROSCI.19-20-08876.1999 / J. Neurosci. / Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons by Hartley (1999)
  37. 10.1016/S0969-9961(03)00068-8 / Neurobiol. Dis. / Protofibrils of amyloid beta-protein inhibit specific K+ currents in neocortical cultures by Ye (2003)
  38. 10.1016/0003-2697(91)90045-U / Anal. Biochem. / Development of hydrophobicity parameters to analyze proteins which bear post- or co-translational modifications by Black (1991)
  39. 10.1016/0022-2836(91)90881-6 / J. Mol. Biol. / Aggregation and secondary structure of synthetic amyloid beta A4 peptides of Alzheimer's disease by Hilbich (1991)
  40. 10.1006/jmbi.1997.1050 / J. Mol. Biol. / Fibrillogenesis of Alzheimer Abeta peptides studied by fluorescence energy transfer by Huang (1997)
  41. 10.1074/jbc.272.34.21037 / J. Biol. Chem. / Soluble amyloid Abeta-(1–40) exists as a stable dimer at low concentrations by Garzon-Rodriguez (1997)
  42. 10.1074/jbc.M000756200 / J. Biol. Chem. / A conformation change in the carboxyl terminus of Alzheimer's Abeta (1–40) accompanies the transition from dimer to fibril as revealed by fluorescence quenching analysis by Garzon-Rodriguez (2000)
  43. 10.1074/jbc.M112218200 / J. Biol. Chem. / Oxidation of methionine 35 attenuates formation of amyloid beta-peptide 1–40 oligomers by Palmblad (2002)
  44. 10.1038/nbt0995-988 / Biotechnol. (NY) / A biotechnological method provides access to aggregation competent monomeric Alzheimer's 1–42 residue amyloid peptide by Dobeli (1995)
  45. 10.1021/bi990718v / Biochemistry / Deposition of monomeric, not oligomeric, Abeta mediates growth of Alzheimer's disease amyloid plaques in human brain preparations by Tseng (1999)
  46. 10.1080/07391102.1999.10508369 / J. Biomol. Struct. Dynam. / Comparison of the structures of beta amyloid peptide (25–35) and substance P in trifluoroethanol/water solution by Lee (1999)
  47. 10.1002/mrc.1132 / Magn. Reson. Chem. / Translational diffusion measured by PFG-NMR on full length and fragments of the Alzheimer Aβ(1–40) peptide. Determination of hydrodynamic radii of random coil peptides of varying length by Danielsson (2002)
  48. 10.1074/jbc.M100175200 / J. Biol. Chem. / Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits by Curtain (2001)
  49. 10.1042/0264-6021:3490299 / Biochem. J. / Oligomerization of beta-amyloid of the Alzheimer's and the Dutch-cerebral-haemorrhage types by Sian (2000)
  50. 10.1016/S0014-5793(03)01293-6 / FEBS Letters / A left-handed 31 helical conformation in the Alzheimer Aβ(12–28) peptide by Jarvet (2003)
  51. 10.1016/S0006-3495(91)82154-3 / Biophys. J. / pH-dependent structural transitions of Alzheimer amyloid peptides by Fraser (1991)
  52. 10.1006/jmbi.1994.1704 / J. Mol. Biol. / Conformation and fibrillogenesis of Alzheimer A beta peptides with selected substitution of charged residues by Fraser (1994)
  53. 10.1016/0006-291X(87)91008-4 / Biochem. Biophys. Res. Commun. / Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic Xray diffraction pattern by Gorevic (1987)
  54. 10.1073/pnas.84.19.6953 / Proc. Natl Acad. Sci. USA / Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro by Kirschner (1987)
  55. 10.1021/ja991167z / J. Am. Chem. Soc. / Reversible random coil to β-sheet transition and the early stage of aggregation of the Aβ(12–28) fragment from the Alzheimer peptide by Jarvet (2000)
  56. 10.1021/bi00069a001 / Biochemistry / The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease by Jarrett (1993)
  57. 10.1042/bj3550869 / Biochem. J. / In vitro studies of amyloid beta-protein fibril assembly and toxicity provide clues to the aetiology of Flemish variant (Ala692–>Gly) Alzheimer's disease by Walsh (2001)
  58. 10.1515/REVNEURO.2000.11.4.329 / Rev. Neurosci. / Mechanisms of beta-amyloid neurotoxicity: perspectives of pharmacotherapy by Harkany (2000)
  59. 10.1016/S0925-4439(00)00030-2 / Biochim. Biophys. Acta / Oligomerizaiton and fibril asssembly of the amyloid-beta protein by Roher (2000)
  60. 10.1016/S0006-3495(01)76036-5 / Biophys. J. / Poly[N-(2-hydroxypropyl)methacrylamide] polymers diffuse in brain extracellular space with same tortuosity as small molecules by Prokopova-Kubinova (2001)
  61. 10.1073/pnas.1834302100 / Proc. Natl Acad. Sci. USA / Alzheimer's disease-affected brain: presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss by Gong (2003)
  62. 10.1126/science.1079469 / Science / Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis by Kayed (2003)
Dates
Type When
Created 21 years, 4 months ago (April 10, 2004, 6:51 a.m.)
Deposited 4 years, 2 months ago (June 15, 2021, 10:10 a.m.)
Indexed 1 month ago (July 30, 2025, 10:11 a.m.)
Issued 21 years, 4 months ago (May 1, 2004)
Published 21 years, 4 months ago (May 1, 2004)
Published Print 21 years, 4 months ago (May 1, 2004)
Funders 0

None

@article{P_ivi__2004, title={Unique Physicochemical Profile of β-Amyloid Peptide Variant Aβ1–40E22G Protofibrils: Conceivable Neuropathogen in Arctic Mutant Carriers}, volume={339}, ISSN={0022-2836}, url={http://dx.doi.org/10.1016/j.jmb.2004.03.028}, DOI={10.1016/j.jmb.2004.03.028}, number={1}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Päiviö, A and Jarvet, J and Gräslund, A and Lannfelt, L and Westlind-Danielsson, A}, year={2004}, month=may, pages={145–159} }