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References from Solubility of Aβ40 peptide. Local targets link to admitted publications; unresolved targets remain external evidence.
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
10.1038/325733a0 · 1987 · External reference
Not just amyloid: physiological functions of the amyloid precursor protein family
10.1038/nrn.2017.29 · 2017 · External reference
Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein
10.1016/s0006-291x(84)80190-4 · 1984 · External reference
Amyloid plaque core protein in Alzheimer disease and Down syndrome
10.1073/pnas.82.12.4245 · 1985 · External reference
Neuritic plaques and cerebrovascular amyloid in Alzheimer disease are antigenically related
10.1073/pnas.82.24.8729 · 1985 · External reference
10.1016/b978-0-12-385883-2.00012-6
10.1016/b978-0-12-385883-2.00012-6 · External reference
The amyloid hypothesis of Alzheimer's disease at 25 years
10.15252/emmm.201606210 · 2016 · External reference
3rd, Alzheimer's disease and the amyloid-beta peptide
10.3233/jad-2010-1221 · 2010 · External reference
Clearance systems in the brain-implications for Alzheimer disease
10.1038/nrneurol.2015.119 · 2015 · External reference
Abeta truncated species: implications for brain clearance mechanisms and amyloid plaque deposition
10.1016/j.bbadis.2017.07.005 · 2018 · External reference
Measurement of phosphorylated tau epitopes in the differential diagnosisof alzheimer disease
10.1001/archpsyc.61.1.95 · 2004 · External reference
Amyloid beta-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process
10.1021/cn900015v · 2010 · External reference
Amyloid β-peptide polymerization studied using fluorescence correlation spectroscopy
10.1016/s1074-5521(99)80020-9 · 1999 · External reference
Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation
10.1016/s0021-9258(19)61939-3 · 1994 · External reference
The amyloid β peptide (Aβ1-40) is thermodynamically soluble at physiological concentrations
10.1021/bi0341410 · 2003 · External reference
The carboxy terminus of the β-amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease
10.1021/bi00069a001 · 1993 · External reference
Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis
10.1016/j.jmb.2003.11.008 · 2004 · External reference
Kinetic modeling and determination of reaction constants of alzheimer's β-amyloid fibril extension and dissociation using surface plasmon resonance†
10.1021/bi020369w · 2002 · External reference
Ca(2+) enhances Abeta polymerization rate and fibrillar stability in a dynamic manner
10.1042/bj20121583 · 2013 · External reference
Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms
10.1038/srep28658 · 2016 · External reference
Improved discrimination of AD patients using -amyloid(1-42) and tau levels in CSF
1999 · External reference
Evaluation of CSF-tau and CSF-Aβ42 as diagnostic markers for alzheimer disease in clinical practice
10.1001/archneur.58.3.373 · 2001 · External reference
Reduced cerebrospinal fluid estradiol levels are associated with increased β-amyloid levels in female patients with Alzheimer's disease
10.1016/s0304-3940(01)01896-1 · 2001 · External reference
A generic method for design of oligomer-specific antibodies
10.1371/journal.pone.0090857 · 2014 · External reference
Critical aggregation concentration for the formation of early Amyloid-beta (1-42) oligomers
10.1038/s41598-018-19961-3 · 2018 · External reference
Supersaturation in sickle cell hemoglobin solutions
10.1073/pnas.73.9.3035 · 1976 · External reference
Universality of supersaturation in protein-fiber formation
10.1038/nsmb.3197 · 2016 · External reference
Quantification of the concentration of Abeta42 propagons during the lag phase by an amyloid chain reaction assay
10.1021/ja408765u · 2014 · External reference
On the lag phase in amyloid fibril formation
10.1039/c4cp05563b · 2015 · External reference
Proteopathic seed amplification assays for neurodegenerative disorders
10.1016/j.cll.2020.04.002 · 2020 · External reference
Latent analysis of unmodified biomolecules and their complexes in solution with attomole detection sensitivity
10.1038/nchem.2344 · 2015 · External reference
A selected reaction monitoring (SRM)-Based method for absolute quantification of Aβ38, Aβ40, and Aβ42 in cerebrospinal fluid of alzheimer's disease patients and healthy controls
10.3233/jad-2012-121471 · 2013 · External reference
Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Abeta42 peptide
2020 · External reference
A facile method for expression and purification of the Alzheimer's disease-associated amyloid beta-peptide
10.1111/j.1742-4658.2008.06862.x · 2009 · External reference
Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-beta peptide
10.1038/s41557-018-0023-x · 2018 · External reference
10.1007/978-1-0716-0524-0_38
10.1007/978-1-0716-0524-0_38 · External reference
Autocatalytic amplification of Alzheimer-associated Abeta42 peptide aggregation in human cerebrospinal fluid
10.1038/s42003-019-0612-2 · 2019 · External reference
Proliferation of amyloid-beta 42 aggregates occurs through a secondary nucleation mechanism
10.1073/pnas.1218402110 · 2013 · External reference
Seeding “one-dimensional crystallization” of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?
10.1016/0092-8674(93)90635-4 · 1993 · External reference
Unresolved reference
2003 · External reference
Unresolved reference
1999 · External reference
Nucleation and crystal growth in supersaturated solutions of a model drug
10.1016/j.jcis.2008.05.034 · 2008 · External reference
Direct determination of the nucleation rates of protein crystals
10.1021/jp992786x · 1999 · External reference
Molecular mechanism of Thioflavin-T binding to amyloid fibrils
10.1016/j.bbapap.2010.04.001 · 2010 · External reference
Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Abeta 40 and Abeta42 peptides
10.1073/pnas.1401564111 · 2014 · External reference
Conserved S/T residues of the human chaperone DNAJB6 are required for effective inhibition of Aβ42 amyloid fibril formation
10.1021/acs.biochem.8b00353 · 2018 · External reference
Measuring translational diffusion coefficients of peptides and proteins by PFG-NMR using band-selective RF pulses
10.1007/s00249-014-0965-x · 2014 · External reference
Nature of the amyloid-β monomer and the monomer-oligomer equilibrium
10.1074/jbc.m110.199885 · 2011 · External reference
Amyloid β-protein (Aβ) assembly: aβ 40 and Aβ 42 oligomerize through distinct pathways
10.1073/pnas.222681699 · 2003 · External reference
Evidence of the existence of micelles in the fibrillogenesis of β-amyloid peptide
10.1021/jp050716m · 2005 · External reference
Structure determination of micelle-like intermediates in amyloid -protein fibril assembly by using small angle neutron scattering
10.1073/pnas.012584899 · 2002 · External reference
Mechanics and kinetics of dynamic instability
10.7554/elife.54077 · 2020 · External reference
Cerebrospinal fluid Aβ42 is increased early in sporadic Alzheimer's disease and declines with disease progression
10.1002/1531-8249(199904)45:4<504::aid-ana12>3.0.co;2-9 · 1999 · External reference
Quantification of Alzheimer amyloid beta peptides ending at residues 40 and 42 by novel ELISA systems
10.1007/bf03401938 · 2000 · External reference
Aqueous self-assembly within the homologous peptide series AnK
10.1021/la5016324 · 2014 · External reference
Aggregation and fibril structure of aßm01–42 and aβ1–42
10.1021/acs.biochem.7b00729 · 2017 · External reference
