Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Tau factor polymers are similar to paired helical filaments of Alzheimer's disease.

Literature DB >> 3402611

Tau factor polymers are similar to paired helical filaments of Alzheimer's disease.

E Montejo de Garcini¹, J L Carrascosa, I Correas, A Nieto, J Avila.

Abstract

Tau factor, upon urea treatment, is able to polymerize in vitro. These polymers are composed of tau factor as shown by immunogold staining. The structure of tau polymers is very similar to that of paired helical filaments (PHFs) of Alzheimer's disease in their dimensions as well as in their periodicity. Metal shadowing of both polymers shows a similar twisting. Also, similar peptide maps were found for tau factor and a 33 kDa protein that is the main component of our PHF preparations.

Entities: Chemical Disease Gene

Mesh：

Substances：

Year: 1988 PMID： 3402611 DOI： 10.1016/0014-5793(88)80304-1

Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124

Keyword Cloud
Cited

12 in total

1. Tau dephosphorylation at tau-1 site correlates with its association to cell membrane.

Authors: M Arrasate; M Pérez; J Avila
Journal: Neurochem Res Date: 2000-01 Impact factor: 3.996

2. Role of glycosaminoglycans in determining the helicity of paired helical filaments.

Authors: M Arrasate; M Pérez; J M Valpuesta; J Avila
Journal: Am J Pathol Date: 1997-10 Impact factor: 4.307

3. Fibers of tau fragments, but not full length tau, exhibit a cross beta-structure: implications for the formation of paired helical filaments.

Authors: A M Giannetti; G Lindwall; M F Chau; M J Radeke; S C Feinstein; L A Kohlstaedt
Journal: Protein Sci Date: 2000-12 Impact factor: 6.725

Tau factor polymers are similar to paired helical filaments of Alzheimer's disease.

1. Tau dephosphorylation at tau-1 site correlates with its association to cell membrane.

2. Role of glycosaminoglycans in determining the helicity of paired helical filaments.

3. Fibers of tau fragments, but not full length tau, exhibit a cross beta-structure: implications for the formation of paired helical filaments.

4. Disruption of microtubule network by Alzheimer abnormally hyperphosphorylated tau.

5. Is tau a suitable therapeutical target in tauopathies?

6. Specific Peptide from the Novel W-Tau Isoform Inhibits Tau and Amyloid β Peptide Aggregation In Vitro.

7. Ferritin is associated with the aberrant tau filaments present in progressive supranuclear palsy.

Review 8. Tau function and dysfunction in neurons: its role in neurodegenerative disorders.

9. Characterization by atomic force microscopy of Alzheimer paired helical filaments under physiological conditions.

10. Are tau aggregates toxic or protective in tauopathies?