Literature DB >> 9066128

Normal and pathological Tau proteins as factors for microtubule assembly.

A Delacourte1, L Buée.   

Abstract

Tau proteins are microtubule-associated proteins. They regulate the dynamics of the microtubule network, especially involved in the axonal transport and neuronal plasticity. Tau proteins belong to a family of developmentally regulated isoforms generated by alternative splicing and phosphorylation. This generates several Tau variants that interact with tubulin and other proteins. Therefore, Tau proteins are influenced by many physiological regulations. Tau proteins are also powerful markers of the neuronal physiological state. Their degree of phosphorylation is a good marker of cell integrity. It is heavily disturbed in numerous neurodegenerative disorders, leading to a collapse of the microtubule network and the presence of intraneuronal lesions resulting from Tau aggregation. However, different biochemical and immunological patterns of pathological Tau proteins found among neurodegenerative disorders are useful markers for the understanding of the role of Tau protein isoforms and the diagnosis of these pathological conditions.

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Year:  1997        PMID: 9066128     DOI: 10.1016/s0074-7696(08)62588-7

Source DB:  PubMed          Journal:  Int Rev Cytol        ISSN: 0074-7696


  19 in total

1.  Structural analysis of Pick's disease-derived and in vitro-assembled tau filaments.

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Review 2.  Amyloidogenesis of natively unfolded proteins.

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4.  Acute inactivation of tau has no effect on dynamics of microtubules in growing axons of cultured sympathetic neurons.

Authors:  I Tint; T Slaughter; I Fischer; M M Black
Journal:  J Neurosci       Date:  1998-11-01       Impact factor: 6.167

Review 5.  The tauopathies: toward an experimental animal model.

Authors:  M Goedert; M Hasegawa
Journal:  Am J Pathol       Date:  1999-01       Impact factor: 4.307

6.  Clinicopathologic discrepancies in a population-based incidence study of parkinsonism in olmsted county: 1991-2010.

Authors:  Pierpaolo Turcano; Michelle M Mielke; Keith A Josephs; James H Bower; Joseph E Parisi; Bradley F Boeve; Rodolfo Savica
Journal:  Mov Disord       Date:  2017-08-26       Impact factor: 10.338

7.  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

Review 8.  Faulty RNA splicing: consequences and therapeutic opportunities in brain and muscle disorders.

Authors:  Vittoria Pagliarini; Piergiorgio La Rosa; Claudio Sette
Journal:  Hum Genet       Date:  2017-04-22       Impact factor: 4.132

9.  Microtubule-associated protein tau in bovine retinal photoreceptor rod outer segments: comparison with brain tau.

Authors:  Akio Yamazaki; Yuji Nishizawa; Isao Matsuura; Fumio Hayashi; Jiro Usukura; Vladimir A Bondarenko
Journal:  Biochim Biophys Acta       Date:  2013-05-24

Review 10.  Tau function and dysfunction in neurons: its role in neurodegenerative disorders.

Authors:  Jesús Avila; Filip Lim; Francisco Moreno; Carlos Belmonte; A Claudio Cuello
Journal:  Mol Neurobiol       Date:  2002-06       Impact factor: 5.590

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