Literature DB >> 7566344

On the structure of microtubules, tau, and paired helical filaments.

E Mandelkow1, Y H Song, O Schweers, A Marx, E M Mandelkow.   

Abstract

Microtubules and their associated proteins form the basis of axonal transport; they are degraded during the neuronal degeneration in Alzheimer's disease. This article surveys recent results on the structure of microtubules, tau protein, and PHFs. Microtubules have been investigated by electron microscopy and image processing after labeling them with the head domain of the motor protein kinesin. This reveals the arrangement of tubulin subunits in microtubules and the shape of the tubulin-motor complex. Tau protein was studied by electron microscopy, solution X-ray scattering, and spectroscopic methods. It appears as an elongated molecule (about 35 nm) without recognizable secondary structure. Alzheimer PHFs were examined by FTIR and X-ray diffraction; they, too, show evidence for secondary structure such as beta sheets.

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Year:  1995        PMID: 7566344     DOI: 10.1016/0197-4580(95)00026-b

Source DB:  PubMed          Journal:  Neurobiol Aging        ISSN: 0197-4580            Impact factor:   4.673


  16 in total

1.  Computational modeling of axonal microtubule bundles under tension.

Authors:  Stephen J Peter; Mohammad R K Mofrad
Journal:  Biophys J       Date:  2012-02-21       Impact factor: 4.033

2.  Transcriptome analysis of a tau overexpression model in rats implicates an early pro-inflammatory response.

Authors:  David B Wang; Robert D Dayton; Richard M Zweig; Ronald L Klein
Journal:  Exp Neurol       Date:  2010-03-24       Impact factor: 5.330

3.  Tau protein degradation is catalyzed by the ATP/ubiquitin-independent 20S proteasome under normal cell conditions.

Authors:  Tilman Grune; Diana Botzen; Martina Engels; Peter Voss; Barbara Kaiser; Tobias Jung; Stefanie Grimm; Gennady Ermak; Kelvin J A Davies
Journal:  Arch Biochem Biophys       Date:  2010-05-15       Impact factor: 4.013

4.  Quantitative characterization of heparin binding to Tau protein: implication for inducer-mediated Tau filament formation.

Authors:  Hai-Li Zhu; Cristina Fernández; Jun-Bao Fan; Frank Shewmaker; Jie Chen; Allen P Minton; Yi Liang
Journal:  J Biol Chem       Date:  2009-12-03       Impact factor: 5.157

Review 5.  Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration.

Authors:  M L Billingsley; R L Kincaid
Journal:  Biochem J       Date:  1997-05-01       Impact factor: 3.857

6.  Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress.

Authors:  Diana Poppek; Susi Keck; Gennady Ermak; Tobias Jung; Alexandra Stolzing; Oliver Ullrich; Kelvin J A Davies; Tilman Grune
Journal:  Biochem J       Date:  2006-12-15       Impact factor: 3.857

Review 7.  Fast axonal transport misregulation and Alzheimer's disease.

Authors:  Gerardo Morfini; Gustavo Pigino; Uwe Beffert; Jorge Busciglio; Scott T Brady
Journal:  Neuromolecular Med       Date:  2002       Impact factor: 3.843

Review 8.  Cerebral amyloidosis: amyloid subunits, mutants and phenotypes.

Authors:  A Rostagno; J L Holton; T Lashley; T Revesz; Jorge Ghiso
Journal:  Cell Mol Life Sci       Date:  2009-11-07       Impact factor: 9.261

9.  Low micromolar zinc accelerates the fibrillization of human tau via bridging of Cys-291 and Cys-322.

Authors:  Zhong-Ying Mo; Ying-Zhu Zhu; Hai-Li Zhu; Jun-Bao Fan; Jie Chen; Yi Liang
Journal:  J Biol Chem       Date:  2009-10-13       Impact factor: 5.157

10.  Dephosphorylation of tau protein by calcineurin triturated into neural living cells.

Authors:  Qun Wei; Max Holzer; Martina K Brueckner; Yu Liu; Thomas Arendt
Journal:  Cell Mol Neurobiol       Date:  2002-02       Impact factor: 5.046

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