Cargando…
Tubulin Subunits Exist in an Activated Conformational State Generated and Maintained by Protein Cofactors
The production of native α/β tubulin heterodimer in vitro depends on the action of cytosolic chaperonin and several protein cofactors. We previously showed that four such cofactors (termed A, C, D, and E) together with native tubulin act on β-tubulin folding intermediates generated by the chaperonin...
Autores principales: | Tian, Guoling, Lewis, Sally A., Feierbach, Becket, Stearns, Timothy, Rommelaere, Heidi, Ampe, Christophe, Cowan, Nicholas J. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1997
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138046/ https://www.ncbi.nlm.nih.gov/pubmed/9265649 |
Ejemplares similares
-
Alf1p, a CLIP-170 Domain-containing Protein, Is Functionally and Physically Associated with α-Tubulin
por: Feierbach, Becket, et al.
Publicado: (1999) -
Adp Ribosylation Factor-like Protein 2 (Arl2) Regulates the Interaction of Tubulin-Folding Cofactor D with Native Tubulin
por: Bhamidipati, Arunashree, et al.
Publicado: (2000) -
Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization
por: Grynberg, Marcin, et al.
Publicado: (2003) -
Colchicine Blocks Tubulin Heterodimer Recycling by Tubulin Cofactors TBCA, TBCB, and TBCE
por: Nolasco, Sofia, et al.
Publicado: (2021) -
Spatio-temporal distribution of tubulin-binding cofactors and posttranslational modifications of tubulin in the cochlea of mice
por: Juergens, Lukas, et al.
Publicado: (2020)