Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Katrien Neirynck"'
Publikováno v:
Journal of Molecular Biology. 355:124-138
The chaperones prefoldin and the cytosolic chaperonin CCT-containing TCP-1 (CCT) guide the cytoskeletal protein actin to its native conformation. Performing an alanine scan of actin, we identified discrete recognition determinants for CCT interaction
Publikováno v:
Biological Procedures Online, Vol 6, Iss 1, Pp 235-249 (2004)
Biological Procedures
Biological Procedures
Recombinant production and biochemical analysis of actin mutants has been hampered by the fact that actin has an absolute requirement for the eukaryotic chaperone CCT to reach its native state. We therefore have developed a method to rapidly screen t
Autor:
M Goethals, Katrien Neirynck, Christophe Ampe, Danny Peelaers, Heidi Rommelaere, Davy Waterschoot, Joël Vandekerckhove, Norbert Fraeyman, Myriam De Neve
Publikováno v:
Journal of Biological Chemistry. 276:41023-41028
Nascent actin and tubulin molecules undergo a series of complex interactions with chaperones and are thereby guided to their native conformation. These cytoskeletal proteins have the initial part of the pathway in common: both interact with prefoldin
Autor:
Heidi, Rommelaere, Davy, Waterschoot, Katrien, Neirynck, Joël, Vandekerckhove, Christophe, Ampe
Publikováno v:
Structure (London, England : 1993). 11(10)
Actin is one of the most conserved and versatile proteins capable of forming homopolymers and interacting with numerous other proteins in the cell. We performed an alanine mutagenesis scan covering the entire beta-actin molecule. Somewhat surprisingl
Publikováno v:
Structure. 12:1547
Actin is one of the most conserved and versatile proteins capable of forming homopolymers and interacting with numerous other proteins in the cell. We performed an alanine mutagenesis scan covering the entire β-actin molecule. Somewhat surprisingly,