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Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors

published in: Journal of Cell Biology

date of publication: 1997-08-25

language: English

Cites articles 37

Date

Title

Authors

1997-07-01

Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability
1996-07-26

Pathway leading to correctly folded beta-tubulin
1996-01-01

Chaperonin-mediated folding of actin and tubulin
1996-06-13

Molecular chaperones in cellular protein folding

Franz-Ulrich Hartl
1996-07-01

Analysis of Tub4p, a yeast gamma-tubulin-like protein: implications for microtubule-organizing center function

Tim Stearns
1996-08-01

Cofactor A is a molecular chaperone required for beta-tubulin folding: functional and structural characterization.
1995-01-01

Kinesis of polypeptide during GroEL-mediated folding
1995-10-01

Precise gene disruption in Saccharomyces cerevisiae by double fusion polymerase chain reaction
1995-08-01

Rbl2p, a yeast protein that binds to beta-tubulin and participates in microtubule function in vivo.
1995-05-01

Specificity in chaperonin-mediated protein folding
1995-10-01

Quasi-native chaperonin-bound intermediates in facilitated protein folding
1994-09-01

Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo

Tim C Huffaker
1994-09-01

A yeast TCP-1-like protein is required for actin function in vivo
1994-06-01

A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin
1994-10-01

The essential yeast Tcp1 protein affects actin and microtubules
1994-07-01

Role of 300 kDa complexes as intermediates in tubulin folding and dimerization: characterization of a 25 kDa cytosolic protein involved in the GTP-dependent release of monomeric tubulin
1993-09-01

Chaperonin-mediated folding of vertebrate actin-related protein and gamma-tubulin
1993-04-01

Two cofactors and cytoplasmic chaperonin are required for the folding of alpha- and beta-tubulin
1993-05-01

Folding of bacterial luciferase involves a non-native heterodimeric intermediate in equilibrium with the native enzyme and the unfolded subunits
1993-05-01

Contribution of folding steps involving the individual subunits of bacterial luciferase to the assembly of the active heterodimeric enzyme
1993-10-01

Incorporation of tubulin subunits into dimers requires GTP hydrolysis
1992-09-18

CLIP-170 links endocytic vesicles to microtubules
1992-12-01

Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits

Franz-Ulrich Hartl
1992-06-01

A cytoplasmic chaperonin that catalyzes beta-actin folding
1992-01-01

Tubulin dimer formation via the release of alpha- and beta-tubulin monomers from multimolecular complexes

Juan C Zabala
1990-02

Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function

David Botstein
1990-01-01

Chromosome instability mutants of Saccharomyces cerevisiae that are defective in microtubule-mediated processes

David Botstein
1989-05

A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
1986-05-01

Beyond self-assembly: from microtubules to morphogenesis
1985-01-01

Tubulin subunit carboxyl termini determine polymerization efficiency.
1985-08-01

Tubulin, hybrid dimers, and tubulin S. Stepwise charge reduction and polymerization.
1983-01-01

Transformation of intact yeast cells treated with alkali cations

Article - wd:Q24679614

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