ArticleThe Biochemical journal1994
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.
Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed.
- Article
- Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors.The Journal of cell biology · 1997Article
- The third member of the Tetrahymena CCT subunit gene family, TpCCT alpha, encodes a component of the hetero-oligomeric chaperonin complex.The Biochemical journal · 1997Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
beta-Tubulin synthesized in vitro in rabbit reticulocyte lysate is found associated with 900 kDa complexes (C900) containing T Complex Polypeptide 1 (TCP1), heat-shock protein (hsp) 70 and other unidentified proteins, with smaller 300 kDa complexes (C300) of unknown nature, in dimeric association with reticulocyte alpha-tubulin and in monomeric forms. Pulse-chase experiments indicated that production of fully functional beta-tubulin was preceded by its association with C900 and C300 multimolecular complexes and by the appearance of beta-monomers. The high-molecular-mass forms appeared as intermediate products in the process leading to fully functional dimerizable beta-tubulin. C300-associated tubulin can be released as beta-monomer by addition of a cofactor present in reticulocyte lysate. Here a 25 kDa protein which releases tubulin monomers from C300 has been identified and characterized. The protein specifically released monomers from C300, but not from C900, in a process favoured by GTP.
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