about
TBCCD1, a new centrosomal protein, is required for centrosome and Golgi apparatus positioning.The structure of the complex between α-tubulin, TBCE and TBCB reveals a tubulin dimer dissociation mechanismReview: postchaperonin tubulin folding cofactors and their role in microtubule dynamicsAssisted protein folding at low temperature: evolutionary adaptation of the Antarctic fish chaperonin CCT and its client proteinsTBCD links centriologenesis, spindle microtubule dynamics, and midbody abscission in human cellsThe solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.The expression of tubulin cofactor A (TBCA) is regulated by a noncoding antisense Tbca RNA during testis maturation.Tubulin cofactor A gene silencing in mammalian cells induces changes in microtubule cytoskeleton, cell cycle arrest and cell death.Role of cofactors B (TBCB) and E (TBCE) in tubulin heterodimer dissociation.Structure and non-structure of centrosomal proteins.Autoinhibition of TBCB regulates EB1-mediated microtubule dynamics.Tubulin cofactor B regulates microtubule densities during microglia transition to the reactive states.Native tubulin-folding cofactor E purified from baculovirus-infected Sf9 cells dissociates tubulin dimers.Expression of an altered form of tau in Sf9 insect cells results in the assembly of polymers resembling Alzheimer's paired helical filaments.Binding of heat-shock protein 70 (hsp70) to tubulin.Tubulin cofactor B plays a role in the neuronal growth cone.Regulated expression of p14 (cofactor A) during spermatogenesis.Characterization of the new insertion sequence IS91 from an alpha-hemolysin plasmid of Escherichia coli.Purification of α-hemolysin from an overproducing E. coli strainEscherichia coli alpha-haemolysin synthesis and export genes are flanked by a direct repetition of IS91-like elements1H, 13C, and 15N resonance assignments of the N-terminal domain of human Tubulin Binding Cofactor CThe molecular relatedness among alpha-hemolytic plasmids from various incompatibility groupsBeta-tubulin folding is modulated by the isotype-specific carboxy-terminal domainA 14 kDa release factor is involved in GTP-dependent beta-tubulin foldingA putative beta-tubulin phosphate-binding motif is involved in lateral microtubule protofilament interactions
P50
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P50
description
onderzoeker
@nl
researcher, ORCID id # 0000-0003-2679-5473
@en
name
Juan C Zabala
@ast
Juan C Zabala
@en
Juan C Zabala
@nl
type
label
Juan C Zabala
@ast
Juan C Zabala
@en
Juan C Zabala
@nl
prefLabel
Juan C Zabala
@ast
Juan C Zabala
@en
Juan C Zabala
@nl
P106
P21
P31
P496
0000-0003-2679-5473