Literature DB >> 15044677

Role of tau protein in both physiological and pathological conditions.

Jesus Avila1, Jose J Lucas, Mar Perez, Felix Hernandez.   

Abstract

The morphology of a neuron is determined by its cytoskeletal scaffolding. Thus proteins that associate with the principal cytoskeletal components such as the microtubules have a strong influence on both the morphology and physiology of neurons. Tau is a microtubule-associated protein that stabilizes neuronal microtubules under normal physiological conditions. However, in certain pathological situations, tau protein may undergo modifications, mainly through phosphorylation, that can result in the generation of aberrant aggregates that are toxic to neurons. This process occurs in a number of neurological disorders collectively known as tauopathies, the most commonly recognized of which is Alzheimer's disease. The purpose of this review is to define the role of tau protein under normal physiological conditions and to highlight the role of the protein in different tauopathies.

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Year:  2004        PMID: 15044677     DOI: 10.1152/physrev.00024.2003

Source DB:  PubMed          Journal:  Physiol Rev        ISSN: 0031-9333            Impact factor:   37.312


  252 in total

1.  Okadaic acid induces tau phosphorylation in SH-SY5Y cells in an estrogen-preventable manner.

Authors:  Zhang Zhang; James W Simpkins
Journal:  Brain Res       Date:  2010-05-07       Impact factor: 3.252

2.  SPM1 stabilizes subpellicular microtubules in Toxoplasma gondii.

Authors:  Johnson Q Tran; Catherine Li; Alice Chyan; Lawton Chung; Naomi S Morrissette
Journal:  Eukaryot Cell       Date:  2011-10-21

3.  Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration.

Authors:  Brian R Hoover; Miranda N Reed; Jianjun Su; Rachel D Penrod; Linda A Kotilinek; Marianne K Grant; Rose Pitstick; George A Carlson; Lorene M Lanier; Li-Lian Yuan; Karen H Ashe; Dezhi Liao
Journal:  Neuron       Date:  2010-12-22       Impact factor: 17.173

4.  Protein structural and surface water rearrangement constitute major events in the earliest aggregation stages of tau.

Authors:  Anna Pavlova; Chi-Yuan Cheng; Maia Kinnebrew; John Lew; Frederick W Dahlquist; Songi Han
Journal:  Proc Natl Acad Sci U S A       Date:  2015-12-28       Impact factor: 11.205

5.  FLEXITau: Quantifying Post-translational Modifications of Tau Protein in Vitro and in Human Disease.

Authors:  Waltraud Mair; Jan Muntel; Katharina Tepper; Shaojun Tang; Jacek Biernat; William W Seeley; Kenneth S Kosik; Eckhard Mandelkow; Hanno Steen; Judith A Steen
Journal:  Anal Chem       Date:  2016-03-07       Impact factor: 6.986

6.  Transglutaminase 1 and its regulator tazarotene-induced gene 3 localize to neuronal tau inclusions in tauopathies.

Authors:  Micha M M Wilhelmus; Mieke de Jager; Annemieke J M Rozemuller; John Brevé; John G J M Bol; Richard L Eckert; Benjamin Drukarch
Journal:  J Pathol       Date:  2011-10-18       Impact factor: 7.996

Review 7.  It's all about tau.

Authors:  Cheril Tapia-Rojas; Fabian Cabezas-Opazo; Carol A Deaton; Erick H Vergara; Gail V W Johnson; Rodrigo A Quintanilla
Journal:  Prog Neurobiol       Date:  2018-12-31       Impact factor: 11.685

Review 8.  Flavonoids as therapeutic compounds targeting key proteins involved in Alzheimer's disease.

Authors:  Filipa I Baptista; Ana G Henriques; Artur M S Silva; Jens Wiltfang; Odete A B da Cruz e Silva
Journal:  ACS Chem Neurosci       Date:  2014-01-03       Impact factor: 4.418

9.  Can zebrafish be used as animal model to study Alzheimer's disease?

Authors:  Soraya Santana; Eduardo P Rico; Javier S Burgos
Journal:  Am J Neurodegener Dis       Date:  2012-05-15

10.  Tau interconverts between diffusive and stable populations on the microtubule surface in an isoform and lattice specific manner.

Authors:  Derrick P McVicker; Gregory J Hoeprich; Andrew R Thompson; Christopher L Berger
Journal:  Cytoskeleton (Hoboken)       Date:  2014-02-24
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