Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates (Q36651582)

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scientific article published on May 1994

Language	Label	Description	Also known as
English	Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates	scientific article published on May 1994

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates (English)

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

author name string

Melki R

1

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

Cowan NJ

2

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

language of work or name

0 references

publication date

1 May 1994

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

Molecular and Cellular Biology

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Europe PubMed Central

PMC publication ID

15 August 2017

14

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

5

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

2895-2904

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

1 reference

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

1 reference

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Principles that govern the folding of protein chains

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Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis-specific expression of two sister genes

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Protein folding in the cell

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TCP1 complex is a molecular chaperone in tubulin biogenesis

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A vertebrate actin-related protein is a component of a multisubunit complex involved in microtubule-based vesicle motility

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

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

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Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein.

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Binding of a chaperonin to the folding intermediates of lactate dehydrogenase

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A cytoplasmic chaperonin that catalyzes beta-actin folding

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Positive cooperativity in the functioning of molecular chaperone GroEL

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Characterization of the aluminum and beryllium fluoride species bound to F-actin and microtubules at the site of the gamma-phosphate of the nucleotide

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Muscle contraction and free energy transduction in biological systems

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Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP

1 reference

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Stabilization of microtubules by inorganic phosphate and its structural analogs, the fluoride complexes of aluminum and beryllium

1 reference

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Identifiers

10.1128/MCB.14.5.2895

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

release_3lu4vkigz5cnbmk3lbphm52t3e

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24 November 2022

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PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

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