Tau Phosphorylation by GSK3 in Different Conditions | Zendy

Jesús Ávila | Zendy; Gonzalo LeónEspinosa | Zendy; Esther García | Zendy; Vega GarcíaEscudero | Zendy; Félix Hernández | Zendy; Javier DeFelipe | Zendy

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Tau Phosphorylation by GSK3 in Different Conditions

Author(s) -

Jesús Ávila,

Gonzalo LeónEspinosa,

Esther García,

Vega GarcíaEscudero,

Félix Hernández,

Javier DeFelipe

Publication year - 2012

Publication title -

international journal of alzheimer s disease

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.657

H-Index - 49

eISSN - 2090-8024

pISSN - 2090-0252

DOI - 10.1155/2012/578373

Subject(s) - phosphorylation , serine , phosphoprotein , threonine , tyrosine , hyperphosphorylation , residue (chemistry) , amino acid residue , biochemistry , medicine , microbiology and biotechnology , biology , peptide sequence , gene

Almost a 20% of the residues of tau protein are phosphorylatable amino acids: serine, threonine, and tyrosine. In this paper we comment on the consequences for tau of being a phosphoprotein. We will focus on serine/threonine phosphorylation. It will be discussed that, depending on the modified residue in tau molecule, phosphorylation could be protective, in processes like hibernation, or toxic like in development of those diseases known as tauopathies, which are characterized by an hyperphosphorylation and aggregation of tau.

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