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211 related items for PubMed ID: 20638386
1. Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its beta-tubulin binding characterization. Lu L, Nan J, Mi W, Li LF, Wei CH, Su XD, Li Y. FEBS Lett; 2010 Aug 20; 584(16):3533-9. PubMed ID: 20638386 [Abstract] [Full Text] [Related]
2. Three-dimensional structure of human tubulin chaperone cofactor A. Guasch A, Aloria K, Pérez R, Avila J, Zabala JC, Coll M. J Mol Biol; 2002 May 10; 318(4):1139-49. PubMed ID: 12054808 [Abstract] [Full Text] [Related]
3. Cofactor A is a molecular chaperone required for beta-tubulin folding: functional and structural characterization. Melki R, Rommelaere H, Leguy R, Vandekerckhove J, Ampe C. Biochemistry; 1996 Aug 13; 35(32):10422-35. PubMed ID: 8756698 [Abstract] [Full Text] [Related]
4. Crystal structure of the post-chaperonin beta-tubulin binding cofactor Rbl2p. Steinbacher S. Nat Struct Biol; 1999 Nov 13; 6(11):1029-32. PubMed ID: 10542094 [Abstract] [Full Text] [Related]
5. Arabidopsis tubulin folding cofactor B interacts with alpha-tubulin in vivo. Dhonukshe P, Bargmann BO, Gadella TW. Plant Cell Physiol; 2006 Oct 13; 47(10):1406-11. PubMed ID: 16928693 [Abstract] [Full Text] [Related]
6. Parkin-co-regulated gene (PACRG) product interacts with tubulin and microtubules. Ikeda T. FEBS Lett; 2008 Apr 30; 582(10):1413-8. PubMed ID: 18387367 [Abstract] [Full Text] [Related]