Willison KR - Search Results

1

The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin.

Llorca O, Martín-Benito J, Grantham J, Ritco-Vonsovici M, Willison KR, Carrascosa JL, Valpuesta JM. Llorca O, et al. Among authors: willison kr. EMBO J. 2001 Aug 1;20(15):4065-75. doi: 10.1093/emboj/20.15.4065. EMBO J. 2001. PMID: 11483510 Free PMC article.

2

The inter-ring arrangement of the cytosolic chaperonin CCT.

Martín-Benito J, Grantham J, Boskovic J, Brackley KI, Carrascosa JL, Willison KR, Valpuesta JM. Martín-Benito J, et al. Among authors: willison kr. EMBO Rep. 2007 Mar;8(3):252-7. doi: 10.1038/sj.embor.7400894. Epub 2007 Feb 16. EMBO Rep. 2007. PMID: 17304242 Free PMC article.

3

Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT.

Valpuesta JM, Martín-Benito J, Gómez-Puertas P, Carrascosa JL, Willison KR. Valpuesta JM, et al. Among authors: willison kr. FEBS Lett. 2002 Oct 2;529(1):11-6. doi: 10.1016/s0014-5793(02)03180-0. FEBS Lett. 2002. PMID: 12354605 Free article. Review.

4

The substrate recognition mechanisms in chaperonins.

Gómez-Puertas P, Martín-Benito J, Carrascosa JL, Willison KR, Valpuesta JM. Gómez-Puertas P, et al. Among authors: willison kr. J Mol Recognit. 2004 Mar-Apr;17(2):85-94. doi: 10.1002/jmr.654. J Mol Recognit. 2004. PMID: 15027029 Review.

5

Eukaryotic type II chaperonin CCT interacts with actin through specific subunits.

Llorca O, McCormack EA, Hynes G, Grantham J, Cordell J, Carrascosa JL, Willison KR, Fernandez JJ, Valpuesta JM. Llorca O, et al. Among authors: willison kr. Nature. 1999 Dec 9;402(6762):693-6. doi: 10.1038/45294. Nature. 1999. PMID: 10604479

6

Partial occlusion of both cavities of the eukaryotic chaperonin with antibody has no effect upon the rates of beta-actin or alpha-tubulin folding.

Grantham J, Llorca O, Valpuesta JM, Willison KR. Grantham J, et al. Among authors: willison kr. J Biol Chem. 2000 Feb 18;275(7):4587-91. doi: 10.1074/jbc.275.7.4587. J Biol Chem. 2000. PMID: 10671484 Free article.

7

Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations.

Llorca O, Martín-Benito J, Ritco-Vonsovici M, Grantham J, Hynes GM, Willison KR, Carrascosa JL, Valpuesta JM. Llorca O, et al. Among authors: willison kr. EMBO J. 2000 Nov 15;19(22):5971-9. doi: 10.1093/emboj/19.22.5971. EMBO J. 2000. PMID: 11080144 Free PMC article.

8

Analysis of the interaction between the eukaryotic chaperonin CCT and its substrates actin and tubulin.

Llorca O, Martín-Benito J, Gómez-Puertas P, Ritco-Vonsovici M, Willison KR, Carrascosa JL, Valpuesta JM. Llorca O, et al. Among authors: willison kr. J Struct Biol. 2001 Aug;135(2):205-18. doi: 10.1006/jsbi.2001.4359. J Struct Biol. 2001. PMID: 11580270

9

ATP binding induces large conformational changes in the apical and equatorial domains of the eukaryotic chaperonin containing TCP-1 complex.

Llorca O, Smyth MG, Marco S, Carrascosa JL, Willison KR, Valpuesta JM. Llorca O, et al. Among authors: willison kr. J Biol Chem. 1998 Apr 24;273(17):10091-4. doi: 10.1074/jbc.273.17.10091. J Biol Chem. 1998. PMID: 9553054 Free article.

10

3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin.

Llorca O, Smyth MG, Carrascosa JL, Willison KR, Radermacher M, Steinbacher S, Valpuesta JM. Llorca O, et al. Among authors: willison kr. Nat Struct Biol. 1999 Jul;6(7):639-42. doi: 10.1038/10689. Nat Struct Biol. 1999. PMID: 10404219

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