Zobrazeno 1 - 7
of 7
pro vyhledávání: '"María E. Chesta"'
Publikováno v:
Cytoskeleton. 70:297-303
The acetylation/deacetylation of Lys40 of the α-subunit is an important posttranslational modification undergone by tubulin during the life of a cell. Many previous studies have addressed the physiological role of this acetylation process using vari
Publikováno v:
Biochemical Journal. 449:643-648
Tubulin can be acetylated/deacetylated on Lys40 of the α-subunit. Studies of the post-translational acetylation/deacetylation of tubulin using biochemical techniques require tubulin preparations that are enriched in AcTubulin (acetylated tubulin) an
Autor:
Carlos A. Arce, Guillermo G. Zampar, Silvia A. Purro, C. Gastón Bisig, Verónica S. Santander, María E. Chesta
Publikováno v:
FEBS Journal. 276:7110-7123
In many laboratories, the requirement of microtubule-associated proteins (MAPs) and the stabilization of microtubules for the elongation of neurites has been intensively investigated, with controversial results being obtained. We have observed that t
Publikováno v:
The FEBS journal. 281(21)
Cultured catecholamine-differentiated cells [which lack the microtubule-associated proteins (MAPs): MAP1B, MAP2, Tau, STOP, and Doublecortin] proliferate in the presence of fetal bovine serum, and, in its absence, cease dividing and generate processe
Publikováno v:
Cytoskeleton (Hoboken, N.J.). 70(6)
The acetylation/deacetylation of Lys40 of the α-subunit is an important posttranslational modification undergone by tubulin during the life of a cell. Many previous studies have addressed the physiological role of this acetylation process using vari
Autor:
C Gastón, Bisig, María E, Chesta, Guillermo G, Zampar, Silvia A, Purro, Verónica S, Santander, Carlos A, Arce
Publikováno v:
The FEBS journal. 276(23)
In many laboratories, the requirement of microtubule-associated proteins (MAPs) and the stabilization of microtubules for the elongation of neurites has been intensively investigated, with controversial results being obtained. We have observed that t
Autor:
Nicolás M. Díaz, María E. Chesta, Guillermo G. Zampar, Cesar H. Casale, Carlos A. Arce, Natali L. Chanaday, Agustín Carbajal
Publikováno v:
The Biochemical journal. 422(1)
We showed previously that NKA (Na+/K+-ATPase) interacts with acetylated tubulin resulting in inhibition of its catalytic activity. In the present work we determined that membrane-acetylated tubulin, in the presence of detergent, behaves as an entity