Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 136

The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.

Soluble pre-fibrillar tau and β-amyloid species emerge in early human Alzheimer’s disease and track disease progression and cognitive decline

Koss, David J., Jones, Glynn, Cranston, Anna, Gardner, Heidi, Kanaan, Nicholas M., Platt, Bettina·2016·Acta Neuropathologica
DOI 10.1007/s00401-016-1632-3PMC PMC5106509
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1007/s00401-016-1632-3

Cites

21 of 21 references verified0 citation errors · 0 not checkable

Statistics

Figures

Fig. 1 Cognitive performance during disease progression. Assessment scores from ‘Mini Mental State Exam’ (MMSE, a) as well as global and memory scores from the ‘Clinical Dementia Rating’ (CDR, b) are correlated with disease progression based on Braak stage. Significances (p) and Spearman’s correlation index (r) are provided within each graph. Data are expressed as mean ± SEM, ****p < 0.0001
Fig. 1 Cognitive performance during disease progression. Assessment scores from ‘Mini Mental State Exam’ (MMSE, a) as well as global and memory scores from the ‘Clinical Dementia Rating’ (CDR, b) are correlated with disease progression based on Braak stage. Significances (p) and Spearman’s correlation index (r) are provided within each graph. Data are expressed as mean ± SEM, ****p < 0.0001CC BY · PubMed Central
Fig. 2 Phospho-tau pathology. Dot blots for a AT8, b PHF-1, c CP13 phospho-tau immunoreactivity. Cases within example dot blots are labelled for diagnosis [non-AD control cases (‘C’) and AD] and Braak stage (Br). Analyses stratified for ii) diagnosis, iii) severity (Low: Br 0–2, Intermediate (Inter): Br 3–4 and High: Br 5–6), and (iv) correlation with individual Braak stages are shown. Statistical outcomes are depicted as **p < 0.01, ***p < 0.001, ****p < 0.0001 and Spearman’s correlation (r). The earliest Braak stage at which immunoreactivity was significantly elevated from Braak 0 is also indicated ($)
Fig. 2 Phospho-tau pathology. Dot blots for a AT8, b PHF-1, c CP13 phospho-tau immunoreactivity. Cases within example dot blots are labelled for diagnosis [non-AD control cases (‘C’) and AD] and Braak stage (Br). Analyses stratified for ii) diagnosis, iii) severity (Low: Br 0–2, Intermediate (Inter): Br 3–4 and High: Br 5–6), and (iv) correlation with individual Braak stages are shown. Statistical outcomes are depicted as **p < 0.01, ***p < 0.001, ****p < 0.0001 and Spearman’s correlation (r). The earliest Braak stage at which immunoreactivity was significantly elevated from Braak 0 is also indicated ($)CC BY · PubMed Central
Fig. 3 Conformational and oligomeric tau pathology. a Alz-50 and b MC-1 conformational tau and c oligomeric tau (tau-oligomeric-complex 1; TOC1) dot blots. The inset (C) illustrates an example Western blot for TOC1 run under non-reducing, non-denaturing conditions, labels show diagnosis status (C = non-AD and AD). In A–C, quantifications of immunoreactivity is categorised according to diagnosis (ii), severity (iii, low: Br 0–2, intermediate (Inter): Br 3–4 and High: Br 5–6) and correlation with Braak stage (iv). Significances are indicated as follows: *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001 and Spearman’s correlation (r). The lowest Braak stage at which immunoreactivity was significantly elevated from Braak 0 is indicated by $
Fig. 3 Conformational and oligomeric tau pathology. a Alz-50 and b MC-1 conformational tau and c oligomeric tau (tau-oligomeric-complex 1; TOC1) dot blots. The inset (C) illustrates an example Western blot for TOC1 run under non-reducing, non-denaturing conditions, labels show diagnosis status (C = non-AD and AD). In A–C, quantifications of immunoreactivity is categorised according to diagnosis (ii), severity (iii, low: Br 0–2, intermediate (Inter): Br 3–4 and High: Br 5–6) and correlation with Braak stage (iv). Significances are indicated as follows: *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001 and Spearman’s correlation (r). The lowest Braak stage at which immunoreactivity was significantly elevated from Braak 0 is indicated by $CC BY · PubMed Central
Fig. 4 Amyloid precursor protein cleavage. Exemplary Western blots for a full-length APP detected via 6E10 immunoreactivity, and b β-secretase (BACE1) are illustrated. Braak stage (Br) and diagnosis (non-AD (C) cf. AD) are stated above each sample. Positive (+ve) control: human APP overexpressing mouse and negative (−ve) control (in a: wild-type C57/BL6 mouse and in b: BACE1−/− mouse) are included. Total protein normalised immunoblot signals were analysed according to diagnosis (ii), severity (iii, low: Br 0–2, intermediate (Inter): Br 3–4 and high: Br 5–6) and Braak stage correlation (iv). Statistical results are presented as *p < 0.05, **p < 0.01 and Spearman’s correlation (r) are stated in the graphs. $ indicates the lowest Braak stage at which immunoreactivity differed significantly from Braak 0
Fig. 4 Amyloid precursor protein cleavage. Exemplary Western blots for a full-length APP detected via 6E10 immunoreactivity, and b β-secretase (BACE1) are illustrated. Braak stage (Br) and diagnosis (non-AD (C) cf. AD) are stated above each sample. Positive (+ve) control: human APP overexpressing mouse and negative (−ve) control (in a: wild-type C57/BL6 mouse and in b: BACE1−/− mouse) are included. Total protein normalised immunoblot signals were analysed according to diagnosis (ii), severity (iii, low: Br 0–2, intermediate (Inter): Br 3–4 and high: Br 5–6) and Braak stage correlation (iv). Statistical results are presented as *p < 0.05, **p < 0.01 and Spearman’s correlation (r) are stated in the graphs. $ indicates the lowest Braak stage at which immunoreactivity differed significantly from Braak 0CC BY · PubMed Central
Fig. 5 Monomeric β-amyloid (Aβ). Immunoblot for a monomeric Aβ (6E10 antibody). Diagnosis (Non-AD (C) cf. AD) and Braak stage is stated for each case. Positive (+ve) control: human APP overexpressing mouse and negative (−ve) control (wild-type mouse) samples are also shown. Size comparison was established via a Coomassie stained low molecular weight protein ladder (insert). Quantification was conducted either for all cases (b) or only for samples where a band was evident (c), the percentage (%) of cases in which monomeric Aβ was detected is stated below the graph. Total protein adjusted immunosignal stratified to i) diagnosis ii) severity (Low: Br 0–2, Intermediate (Inter): Br 3–4 and High: Br 5–6) and iii) correlation with individual Braak stage. Significances are illustrated as ***p < 0.001, ****p < 0.0001, Spearman’s correlation is also stated. $: indicates the earliest Braak stage at which immunoreactivity was higher than that observed at Braak stage 0
Fig. 5 Monomeric β-amyloid (Aβ). Immunoblot for a monomeric Aβ (6E10 antibody). Diagnosis (Non-AD (C) cf. AD) and Braak stage is stated for each case. Positive (+ve) control: human APP overexpressing mouse and negative (−ve) control (wild-type mouse) samples are also shown. Size comparison was established via a Coomassie stained low molecular weight protein ladder (insert). Quantification was conducted either for all cases (b) or only for samples where a band was evident (c), the percentage (%) of cases in which monomeric Aβ was detected is stated below the graph. Total protein adjusted immunosignal stratified to i) diagnosis ii) severity (Low: Br 0–2, Intermediate (Inter): Br 3–4 and High: Br 5–6) and iii) correlation with individual Braak stage. Significances are illustrated as ***p < 0.001, ****p < 0.0001, Spearman’s correlation is also stated. $: indicates the earliest Braak stage at which immunoreactivity was higher than that observed at Braak stage 0CC BY · PubMed Central
Fig. 6 Heat-dependent detection of Aβ oligomers. a Side by side comparison of 6E10 immunoreactivty following boiling and non-boiling of samples prior to SDS-PAGE separation. Monomeric, trimeric and *56 Aβ bands are indicated alongside individual diagnosis (C non-AD control and AD cases) and Braak stage (Br) classifications. Quantification of *56 oligomeric Aβ levels according to i) diagnosis, ii) severity (Low: Br 0–2, intermediate (Inter): Br 3–4 and High: Br 5–6) and iii) correlation to individual Braak stage for boiled (b) and non-boiled (c) samples
Fig. 6 Heat-dependent detection of Aβ oligomers. a Side by side comparison of 6E10 immunoreactivty following boiling and non-boiling of samples prior to SDS-PAGE separation. Monomeric, trimeric and *56 Aβ bands are indicated alongside individual diagnosis (C non-AD control and AD cases) and Braak stage (Br) classifications. Quantification of *56 oligomeric Aβ levels according to i) diagnosis, ii) severity (Low: Br 0–2, intermediate (Inter): Br 3–4 and High: Br 5–6) and iii) correlation to individual Braak stage for boiled (b) and non-boiled (c) samplesCC BY · PubMed Central
Fig. 7 Soluble Aβ detection. Example immunoblots for a i) MOAB-2 and b i) pyro-glu reactive Aβ; each case is labelled with corresponding diagnosis [Non-AD (C) cf. AD] and Braak stage. Quantified signals normalised to total protein are shown stratified to ii) diagnosis iii), severity (Low: Br 0–2, Intermediate (Inter): Br 3–4 and High: Br 5–6) and iv) correlation with Braak stage. *p < 0.05, ***p < 0.001, ****p < 0.0001 and Spearman’s correlation r is stated in iv. $ denotes lowest Braak stage at which immunoreactivity differed from Braak 0
Fig. 7 Soluble Aβ detection. Example immunoblots for a i) MOAB-2 and b i) pyro-glu reactive Aβ; each case is labelled with corresponding diagnosis [Non-AD (C) cf. AD] and Braak stage. Quantified signals normalised to total protein are shown stratified to ii) diagnosis iii), severity (Low: Br 0–2, Intermediate (Inter): Br 3–4 and High: Br 5–6) and iv) correlation with Braak stage. *p < 0.05, ***p < 0.001, ****p < 0.0001 and Spearman’s correlation r is stated in iv. $ denotes lowest Braak stage at which immunoreactivity differed from Braak 0CC BY · PubMed Central
Fig. 8 Heat sensitivity of soluble Aβ (MOAB-2 epitope). (i) Dot blots of either boiled or non-boiled samples probed with MOAB-2 for oligomeric Aβ. Diagnosis [non-AD (C) and AD] and Braak stage (Br) are shown for each sample. Matched samples for boiled vs non-boiled conditions were analysed according to diagnosis (ii) and severity (low: Br 0–2, intermediate (Inter): Br 3–4 and high: Br 5–6) (iii). Statistical outcome of a two-way ANOVA is reported in the corresponding graph. *p < 0.05 and ***p < 0.001
Fig. 8 Heat sensitivity of soluble Aβ (MOAB-2 epitope). (i) Dot blots of either boiled or non-boiled samples probed with MOAB-2 for oligomeric Aβ. Diagnosis [non-AD (C) and AD] and Braak stage (Br) are shown for each sample. Matched samples for boiled vs non-boiled conditions were analysed according to diagnosis (ii) and severity (low: Br 0–2, intermediate (Inter): Br 3–4 and high: Br 5–6) (iii). Statistical outcome of a two-way ANOVA is reported in the corresponding graph. *p < 0.05 and ***p < 0.001CC BY · PubMed Central

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

1 retracted

Show all 21 references

Research works printed but not linked: 63

  1. Ahmed RR, Holler CJ, Webb RL, Li F, Beckett TL, Murphy MP (2010) BACE1 and BACE2 enzymatic activities in Alzheimer’s disease. J Neurochem 112:1045–1053 · DOI
  2. Arai H, Lee VM, Messinger ML, Greenberg BD, Lowery DE, Trojanowski JQ (1991) Expression patterns of β-amyloid precursor protein (β-APP) in neural and nonneural human tissues from Alzheimer’s disease and control subjects. Ann Neurol 30:686–693 · DOI · Paper page
  3. Baker-Nigh A, Vahedi S, Davis EG, Weintraub S, Bigio EH, Klein WL et al (2015) Neuronal amyloid-β accumulation within cholinergic basal forebrain in ageing and Alzheimer’s disease. Brain 138:1722–1737 · DOI · Paper page
  4. Barghorn S, Nimmrich V, Striebinger A, Krantz C, Keller P, Janson B et al (2005) Globular amyloid beta-peptide oligomer—a homogenous and stable neuropathological protein in Alzheimer’s disease. J Neurochem 95:834–847 · DOI · Paper page
  5. Berger Z, Roder H, Hanna A, Carlson A, Rangachari V, Yue M et al (2007) Accumulation of pathological tau species and memory loss in a conditional model of tauopathy. J Neurosci 27:3650–3662 · DOI · Paper page
  6. Beyer K, Lao JI, Carrato C, Mate JL, Lopez D, Ferrer I et al (2004) Upregulation of amyloid precursor protein isoforms containing Kunitz protease inhibitor in dementia with Lewy bodies. Brain Res Mol Brain Res 131:131–135 · DOI
  7. Biernat J, Mandelkow EM, Schroter C, Lichtenberg-Kraag B, Steiner B, Berling B et al (1992) The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region. EMBO J 11:1593–1597 · DOI · Paper page
  8. Bloom GS (2014) Amyloid-beta and tau: the trigger and bullet in Alzheimer disease pathogenesis. JAMA Neurol 71:505–508 · DOI
  9. Boluda S, Toledo JB, Irwin DJ, Raible KM, Byrne MD, Lee EB et al (2014) A comparison of Aβ amyloid pathology staging systems and correlation with clinical diagnosis. Acta Neuropathol 128:543–550 · DOI
  10. Borzova VA, Markossian KA, Kara DA, Kurganov B (2015) Kinetic regime of dithiothreitol-induced aggregation of bovine serum albumin. Int J BiolMacromol 80:130–138 · doi:10.1016/j.ijbiomac.2015.06.040
  11. Bowser R, Giambrone A, Davies P (1995) FAC1, a novel gene identified with the monoclonal antibody Alz50, is developmentally regulated in human brain. Dev Neurosci 17:20–37 · DOI
  12. Braak H, Braak E (1995) Staging of Alzheimer’s disease-related neurofibrillary changes. Neurobiol Aging 16:271–284 · DOI · Paper page
  13. Buee L, Bussiere T, Buee-Scherrer V, Delacourte A, Hof PR (2000) Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res Brain Res Rev 33:95–130 · DOI · Paper page
  14. Cheng IH, Scearce-Levie K, Legleiter J, Palop JJ, Gerstein H, Bien-Ly N et al (2007) Accelerating amyloid-β fibrillization reduces oligomer levels and functional deficits in Alzheimer disease mouse models. J Biol Chem 282:23818–23828 · DOI · Paper page
  15. Collins-Praino LE, Francis YI, Griffith EY, Wiegman AF, Urbach J, Lawton A et al. (2014) Soluble amyloid beta levels are elevated in the white matter of Alzheimer’s patients, independent of cortical plaque severity. Acta Neuropathol Commun 2:83. doi: 10.1186/s40478-014-0083-0 · DOI · Paper page
  16. Crowther RA, Olesen OF, Smith MJ, Jakes R, Goedert M (1994) Assembly of Alzheimer-like filaments from full-length tau protein. FEBS Lett 337:135–138 · DOI
  17. Cynis H, Scheel E, Saido TC, Schilling S, Demuth HU (2008) Amyloidogenic processing of amyloid precursor protein: evidence of a pivotal role of glutaminyl cyclase in generation of pyroglutamate-modified amyloid-beta. Biochemistry 47:7405–7413 · DOI
  18. Fa M, Puzzo D, Piacentini R, Staniszewski A, Zhang H, Baltrons MA et al (2016) Extracellular Tau oligomers produce an immediate impairment of LTP and memory. Sci Rep 6:19393 · DOI · Paper page
  19. Ferrer I, Santpere G, Arzberger T, Bell J, Blanco R, Boluda S et al (2007) Brain protein preservation largely depends on the postmortem storage temperature: implications for study of proteins in human neurologic diseases and management of brain banks: a BrainNet Europe Study. J Neuropathol Exp Neurol 66:35–46 · DOI · Paper page
  20. Fukumoto H, Cheung BS, Hyman BT, Irizarry MC (2002) β-Secretase protein and activity are increased in the neocortex in Alzheimer disease. Arch Neurol 59:1381–1389 · DOI · Paper page
  21. Ghoshal N, Garcia-Sierra F, Wuu J, Leurgans S, Bennett DA, Berry RW et al (2002) Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer’s disease. Exp Neurol 177:475–493 · DOI · Paper page
  22. Guillozet-Bongaarts AL, Cahill ME, Cryns VL, Reynolds MR, Berry RW, Binder LI (2006) Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: in vitro evidence and implications for tangle formation in vivo. J Neurochem 97:1005–1014 · DOI · Paper page
  23. Haroutunian V, Davies P, Vianna C, Buxbaum JD, Purohit DP (2007) Tau protein abnormalities associated with the progression of alzheimer disease type dementia. Neurobiol Aging 28:1–7 · DOI · Paper page
  24. Hatami A, 3rd Albay R, Monjazeb S, Milton S, Glabe C (2014) Monoclonal antibodies against Aβ42 fibrils distinguish multiple aggregation state polymorphisms in vitro and in Alzheimer disease brain. J Biol Chem 289:32131–32143 · DOI
  25. Hepler RW, Grimm KM, Nahas DD, Breese R, Dodson EC, Acton P et al (2006) Solution state characterization of amyloid β-derived diffusible ligands. Biochemistry 45:15157–15167 · DOI · Paper page
  26. Holden P, Horton WA (2009) Crude subcellular fractionation of cultured mammalian cell lines. BMC Res Notes 2:243 · DOI · Paper page
  27. Holsinger RM, McLean CA, Beyreuther K, Masters CL, Evin G (2002) Increased expression of the amyloid precursor beta-secretase in Alzheimer’s disease. Ann Neurol 51:783–786 · DOI · Paper page
  28. Iqbal K, Gong CX, Liu F (2013) Hyperphosphorylation-induced tau oligomers. Front Neurol 4:112 · DOI
  29. Jicha GA, Bowser R, Kazam IG, Davies P (1997) Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau. J Neurosci Res 48:128–132 · doi:10.1002/(sici)1097-4547(19970415)48:2<128::aid-jnr5>3.0.co;2-e
  30. Jimenez S, Navarro V, Moyano J, Sanchez-Mico M, Torres M, Davila JC et al (2014) Disruption of amyloid plaques integrity affects the soluble oligomers content from Alzheimer disease brains. PLoS One 9:e114041 · DOI
  31. Jyoti A, Plano A, Riedel G, Platt B (2010) EEG, activity, and sleep architecture in a transgenic AbetaPPswe/PSEN1A246E Alzheimer’s disease mouse. J Alzheimers Dis 22:873–887 · DOI
  32. Kanaan NM, Cox K, Alvarez VE, Stein TD, Poncil S, McKee AC (2016) Characterization of early pathological Tau conformations and phosphorylation in chronic traumatic encephalopathy. J Neuropathol Exp Neurol 75:19–34 · DOI
  33. Kanaan NM, Morfini GA, LaPointe NE, Pigino GF, Patterson KR, Song Y et al (2011) Pathogenic forms of tau inhibit kinesin-dependent axonal transport through a mechanism involving activation of axonal phosphotransferases. J Neurosci 31:9858–9868 · DOI · Paper page
  34. King ME, Gamblin TC, Kuret J, Binder LI (2000) Differential assembly of human tau isoforms in the presence of arachidonic acid. J Neurochem 74:1749–1757 · DOI · Paper page
  35. Koss DJ, Robinson L, Drever BD, Plucinska K, Stoppelkamp S, Veselcic P et al (2016) Mutant Tau knock-in mice display frontotemporal dementia relevant behaviour and histopathology. Neurobiol Dis 91:105–123 · DOI
  36. Koss DJ, Robinson L, Mietelska-Porowska A, Gasiorowska A, Sepcic K, Turk T et al (2015) Polymeric alkylpyridinium salts permit intracellular delivery of human Tau in rat hippocampal neurons: requirement of Tau phosphorylation for functional deficits. Cell Mol Life Sci 72:4613–4632 · DOI
  37. Kumar S, Ravi VK, Swaminathan R (2008) How do surfactants and DTT affect the size, dynamics, activity and growth of soluble lysozyme aggregates? Biochem J 415:275–288 · DOI
  38. Lesne SE, Sherman MA, Grant M, Kuskowski M, Schneider JA, Bennett DA et al (2013) Brain amyloid-β oligomers in ageing and Alzheimer’s disease. Brain 136:1383–1398 · DOI · Paper page
  39. Lue LF, Kuo YM, Roher AE, Brachova L, Shen Y, Sue L et al (1999) Soluble amyloid β peptide concentration as a predictor of synaptic change in Alzheimer’s disease. Am J Pathol 155:853–862 · DOI · Paper page
  40. Luna-Munoz J, Garcia-Sierra F, Falcon V, Menendez I, Chavez-Macias L, Mena R (2005) Regional conformational change involving phosphorylation of tau protein at the Thr231, precedes the structural change detected by Alz-50 antibody in Alzheimer’s disease. J Alzheimers Dis 8:29–41 · DOI
  41. Mandler M, Walker L, Santic R, Hanson P, Upadhaya AR, Colloby SJ et al (2014) Pyroglutamylated amyloid-β is associated with hyperphosphorylated tau and severity of Alzheimer’s disease. Acta Neuropathol 128:67–79 · DOI
  42. Meakin PJ, Harper AJ, Hamilton DL, Gallagher J, McNeilly AD, Burgess LA et al (2012) Reduction in BACE1 decreases body weight, protects against diet-induced obesity and enhances insulin sensitivity in mice. Biochem J 441:285–296 · DOI · Paper page
  43. Mufson EJ, Malek-Ahmadi M, Perez SE, Chen K (2016) Braak staging, plaque pathology, and APOE status in elderly persons without cognitive impairment. Neurobiol Aging 37:147–153 · DOI
  44. Nordstedt C, Gandy SE, Alafuzoff I, Caporaso GL, Iverfeldt K, Grebb JA et al (1991) Alzheimer beta/A4 amyloid precursor protein in human brain: aging-associated increases in holoprotein and in a proteolytic fragment. Proc Natl Acad Sci USA 88:8910–8914 · DOI
  45. Parvathy S, Davies P, Haroutunian V, Purohit DP, Davis KL, Mohs RC et al (2001) Correlation between Abetax-40-, Abetax-42-, and Abetax-43-containing amyloid plaques and cognitive decline. Arch Neurol 58:2025–2032 · DOI
  46. Patterson KR, Remmers C, Fu Y, Brooker S, Kanaan NM, Vana L et al (2011) Characterization of prefibrillar Tau oligomers in vitro and in Alzheimer disease. J Biol Chem 286:23063–23076 · DOI · Paper page
  47. Patterson KR, Ward SM, Combs B, Voss K, Kanaan NM, Morfini G et al (2011) Heat shock protein 70 prevents both tau aggregation and the inhibitory effects of preexisting tau aggregates on fast axonal transport. Biochemistry 50:10300–10310 · DOI
  48. Plucinska K, Crouch B, Koss D, Robinson L, Siebrecht M, Riedel G et al (2014) Knock-in of human BACE1 cleaves murine APP and reiterates Alzheimer-like phenotypes. J Neurosci 34:10710–10728 · DOI
  49. Pujol-Pina R, Vilaprinyo-Pascual S, Mazzucato R, Arcella A, Vilaseca M, Orozco M et al (2015) SDS-PAGE analysis of Aβ oligomers is disserving research into Alzheimer s disease: appealing for ESI-IM-MS. Sci Rep 5:14809 · DOI
  50. RijalUpadhaya A, Kosterin I, Kumar S, von Arnim CA, Yamaguchi H, Fandrich M et al (2014) Biochemical stages of amyloid-beta peptide aggregation and accumulation in the human brain and their association with symptomatic and pathologically preclinical Alzheimer’s disease. Brain 137:887–903 · DOI · Paper page
  51. Santacruz K, Lewis J, Spires T, Paulson J, Kotilinek L, Ingelsson M et al (2005) Tau suppression in a neurodegenerative mouse model improves memory function. Science 309:476–481 · DOI · Paper page
  52. Sasahara K, Yagi H, Naiki H, Goto Y (2007) Heat-induced conversion of β(2)-microglobulin and hen egg-white lysozyme into amyloid fibrils. J MolBiol 372:981–991 · DOI
  53. Serrano-Pozo A, Qian J, Muzikansky A, Monsell SE, Montine TJ, Frosch MP et al (2016) Thal amyloid stages do not significantly impact the correlation between neuropathological change and cognition in the Alzheimer disease continuum. J Neuropathol Exp Neurol 75:516–526 · DOI
  54. Stockley JH, Ravid R, O’Neill C (2006) Altered β-secretase enzyme kinetics and levels of both BACE1 and BACE2 in the Alzheimer’s disease brain. FEBS Lett 580:6550–6560 · DOI
  55. Tharp WG, Lee YH, Greene SM, Vincellete E, Beach TG, Pratley RE (2012) Measurement of altered AβPP isoform expression in frontal cortex of patients with Alzheimer’s disease by absolute quantification real-time PCR. J Alzheimers Dis 29:449–457 · DOI
  56. Toledo JB, Zetterberg H, van Harten AC, Glodzik L, Martinez-Lage P, Bocchio-Chiavetto L et al (2015) Alzheimer’s disease cerebrospinal fluid biomarker in cognitively normal subjects. Brain 138:2701–2715 · DOI · Paper page
  57. Villemagne VL, Burnham S, Bourgeat P, Brown B, Ellis KA, Salvado O et al (2013) Amyloid beta deposition, neurodegeneration, and cognitive decline in sporadic Alzheimer’s disease: a prospective cohort study. Lancet Neurol 12:357–367 · DOI · Paper page
  58. Ward SM, Himmelstein DS, Lancia JK, Fu Y, Patterson KR, Binder LI (2013) TOC1: characterization of a selective oligomeric tau antibody. J Alzheimers Dis 37:593–602 · DOI
  59. Watt AD, Perez KA, Rembach A, Sherrat NA, Hung LW, Johanssen T et al (2013) Oligomers, fact or artefact? SDS-PAGE induces dimerization of β-amyloid in human brain samples. Acta Neuropathol 125:549–564 · DOI
  60. Weaver CL, Espinoza M, Kress Y, Davies P (2000) Conformational change as one of the earliest alterations of tau in Alzheimer’s disease. Neurobiol Aging 21:719–727 · DOI · Paper page
  61. Webster MT, Francis PT, Procter AW, Stratmann GC, Doshi R, Mann DM et al (1994) Postmortem brains reveal similar but not identical amyloid precursor protein-like immunoreactivity in Alzheimer compared with other dementias. Brain Res 644:347–351 · DOI
  62. Xu H, Rosler TW, Carlsson T, de Andrade A, Bruch J, Hollerhage M et al (2014) Memory deficits correlate with tau and spine pathology in P301S MAPT transgenic mice. Neuropathol Appl Neurobiol 40:833–843 · DOI
  63. Zhou XW, Li X, Bjorkdahl C, Sjogren MJ, Alafuzoff I, Soininen H et al (2006) Assessments of the accumulation severities of amyloid β-protein and hyperphosphorylated tau in the medial temporal cortex of control and Alzheimer’s brains. Neurobiol Dis 22:657–668 · DOI

Cited by

See all 136

Metadata

Authors
Koss, D. J., Jones, G., Cranston, A., Gardner, H., Kanaan, N. M., & Platt, B.
Venue
Acta Neuropathologica
Publisher
Springer Science and Business Media LLC
Published
2016-10-21
Volume
132
Issue
6
Pages
875-895
ISSN
  • 0001-6322
  • 1432-0533
DOI
10.1007/s00401-016-1632-3
PMC
PMC5106509
Cited by
136
References
21
Language
en
Licence
Funders
  • Alzheimer’s Research UK (ARUK-PPG2014A-21, ARUK-NSG2015-1)
  • National Institute on Aging (NIH/NINDS R01 NS082730, NIH/NINDS R01 AG044372)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Soluble pre-fibrillar tau and β-amyloid species emerge in early human Alzheimer’s disease and track disease progression and cognitive decline. https://app.cochat.ai/papers/10.1007/s00401-016-1632-3
The paper
Koss, D. J., Jones, G., Cranston, A., Gardner, H., Kanaan, N. M., & Platt, B. (2016). Soluble pre-fibrillar tau and β-amyloid species emerge in early human Alzheimer’s disease and track disease progression and cognitive decline. Acta Neuropathologica. https://doi.org/10.1007/s00401-016-1632-3

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.