McCormack EA - Search Results

1

The chaperonin containing TCP-1 (CCT) displays a single-ring mediated disassembly and reassembly cycle.

Liou AK, McCormack EA, Willison KR. Liou AK, et al. Among authors: mccormack ea. Biol Chem. 1998 Mar;379(3):311-9. doi: 10.1515/bchm.1998.379.3.311. Biol Chem. 1998. PMID: 9563827

2

Equivalent mutations in the eight subunits of the chaperonin CCT produce dramatically different cellular and gene expression phenotypes.

Amit M, Weisberg SJ, Nadler-Holly M, McCormack EA, Feldmesser E, Kaganovich D, Willison KR, Horovitz A. Amit M, et al. Among authors: mccormack ea. J Mol Biol. 2010 Aug 20;401(3):532-43. doi: 10.1016/j.jmb.2010.06.037. Epub 2010 Jun 25. J Mol Biol. 2010. PMID: 20600117

3

ATP-induced allostery in the eukaryotic chaperonin CCT is abolished by the mutation G345D in CCT4 that renders yeast temperature-sensitive for growth.

Shimon L, Hynes GM, McCormack EA, Willison KR, Horovitz A. Shimon L, et al. Among authors: mccormack ea. J Mol Biol. 2008 Mar 21;377(2):469-77. doi: 10.1016/j.jmb.2008.01.011. Epub 2008 Jan 15. J Mol Biol. 2008. PMID: 18272176

4

The interaction network of the chaperonin CCT.

Dekker C, Stirling PC, McCormack EA, Filmore H, Paul A, Brost RL, Costanzo M, Boone C, Leroux MR, Willison KR. Dekker C, et al. Among authors: mccormack ea. EMBO J. 2008 Jul 9;27(13):1827-39. doi: 10.1038/emboj.2008.108. Epub 2008 May 29. EMBO J. 2008. PMID: 18511909 Free PMC article.

5

The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.

Dekker C, Roe SM, McCormack EA, Beuron F, Pearl LH, Willison KR. Dekker C, et al. Among authors: mccormack ea. EMBO J. 2011 Jun 24;30(15):3078-90. doi: 10.1038/emboj.2011.208. EMBO J. 2011. PMID: 21701561 Free PMC article.

6

Yeast phosducin-like protein 2 acts as a stimulatory co-factor for the folding of actin by the chaperonin CCT via a ternary complex.

McCormack EA, Altschuler GM, Dekker C, Filmore H, Willison KR. McCormack EA, et al. J Mol Biol. 2009 Aug 7;391(1):192-206. doi: 10.1016/j.jmb.2009.06.003. Epub 2009 Jun 6. J Mol Biol. 2009. PMID: 19501098

7

Quantitative actin folding reactions using yeast CCT purified via an internal tag in the CCT3/gamma subunit.

Pappenberger G, McCormack EA, Willison KR. Pappenberger G, et al. Among authors: mccormack ea. J Mol Biol. 2006 Jul 7;360(2):484-96. doi: 10.1016/j.jmb.2006.05.003. Epub 2006 May 17. J Mol Biol. 2006. PMID: 16762366

8

A single amino acid residue is responsible for species-specific incompatibility between CCT and alpha-actin.

Altschuler GM, Dekker C, McCormack EA, Morris EP, Klug DR, Willison KR. Altschuler GM, et al. Among authors: mccormack ea. FEBS Lett. 2009 Feb 18;583(4):782-6. doi: 10.1016/j.febslet.2009.01.031. Epub 2009 Feb 5. FEBS Lett. 2009. PMID: 19183552 Free article.

9

Point mutations in a hinge linking the small and large domains of beta-actin result in trapped folding intermediates bound to cytosolic chaperonin CCT.

McCormack EA, Llorca O, Carrascosa JL, Valpuesta JM, Willison KR. McCormack EA, et al. J Struct Biol. 2001 Aug;135(2):198-204. doi: 10.1006/jsbi.2001.4385. J Struct Biol. 2001. PMID: 11580269

10

Mutational screen identifies critical amino acid residues of beta-actin mediating interaction between its folding intermediates and eukaryotic cytosolic chaperonin CCT.

McCormack EA, Rohman MJ, Willison KR. McCormack EA, et al. J Struct Biol. 2001 Aug;135(2):185-97. doi: 10.1006/jsbi.2001.4389. J Struct Biol. 2001. PMID: 11580268

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