Accumulation of aspartic acid421- and glutamic acid391-cleaved tau in neurofibrillary tangles correlates with progression in Alzheimer disease (Q36426239)

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English	Accumulation of aspartic acid421- and glutamic acid391-cleaved tau in neurofibrillary tangles correlates with progression in Alzheimer disease	scientific article

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Accumulation of aspartic acid421- and glutamic acid391-cleaved tau in neurofibrillary tangles correlates with progression in Alzheimer disease (English)

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Alzheimer's disease

0 references

Lester I Binder

4

object named as

Lester I Binder

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

author name string

Gustavo Basurto-Islas

1

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Jose Luna-Muñoz

2

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Angela L Guillozet-Bongaarts

3

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Raul Mena

5

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Francisco García-Sierra

6

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

publication date

1 May 2008

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Journal of Neuropathology & Experimental Neurology

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

67

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

5

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

470-483

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Conformational changes and cleavage of tau in Pick bodies parallel the early processing of tau found in Alzheimer pathology

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Degradation of tau protein by puromycin-sensitive aminopeptidase in vitro

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Caspase-3-mediated cleavage of PHF-1 tau during apoptosis irrespective of excitotoxicity and oxidative stress: an implication to Alzheimer's disease.

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The role of caspase cleavage of tau in Alzheimer disease neuropathology

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Tau, tangles, and Alzheimer's disease

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Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology

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ULTRASTRUCTURAL STUDIES IN ALZHEIMER'S PRESENILE DEMENTIA

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The neuronal microtubule-associated protein tau is a substrate for caspase-3 and an effector of apoptosis

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Advanced Maillard reaction end products, free radicals, and protein oxidation in Alzheimer's disease

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Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament

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Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease

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Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease

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Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau)

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Molecular analysis of neurofibrillary degeneration in Alzheimer's disease. An immunohistochemical study

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Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51

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Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease

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1 reference

https://pubmed.ncbi.nlm.nih.gov/18431250

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

AD2, a phosphorylation-dependent monoclonal antibody directed against tau proteins found in Alzheimer's disease

1 reference

https://pubmed.ncbi.nlm.nih.gov/18431250

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1097/NEN.0B013E31817275C7

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

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