Eukaryotic type II chaperonin CCT interacts with actin through specific subunits

[1]  Michael Radermacher,et al.  3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin , 1999, Nature Structural Biology.

[2]  J. Vandekerckhove,et al.  The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins. , 1999, Biochemistry.

[3]  H. Saibil,et al.  Molecular chaperones and folding catalysts , 1999 .

[4]  L. Szekely,et al.  Epstein-Barr virus-encoded nuclear protein EBNA-3 interacts with the epsilon-subunit of the T-complex protein 1 chaperonin complex. , 1999, Journal of human virology.

[5]  K. Willison,et al.  ATP Binding Induces Large Conformational Changes in the Apical and Equatorial Domains of the Eukaryotic Chaperonin Containing TCP-1 Complex* , 1998, The Journal of Biological Chemistry.

[6]  Robert Huber,et al.  Crystal Structure of the Thermosome, the Archaeal Chaperonin and Homolog of CCT , 1998, Cell.

[7]  J M Carazo,et al.  3D reconstruction in electron microscopy using ART with smooth spherically symmetric volume elements (blobs). , 1998, Ultramicroscopy.

[8]  Bernd Bukau,et al.  The Hsp70 and Hsp60 Chaperone Machines , 1998, Cell.

[9]  W. Baumeister,et al.  Structure of the Substrate Binding Domain of the Thermosome, an Archaeal Group II Chaperonin , 1997, Cell.

[10]  K. Willison,et al.  Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro‐complexes , 1997, The EMBO journal.

[11]  A Leith,et al.  SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. , 1996, Journal of structural biology.

[12]  K. Willison,et al.  The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol. , 1995, European journal of biochemistry.

[13]  K. Willison,et al.  Antibody characterisation of two distinct conformations of the chaperonin‐containing TCP‐1 from mouse testis , 1995, FEBS letters.

[14]  Zbyszek Otwinowski,et al.  The crystal structure of the bacterial chaperonln GroEL at 2.8 Å , 1994, Nature.

[15]  D. Drubin,et al.  A yeast TCP-1-like protein is required for actin function in vivo. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[16]  J M Carazo,et al.  Pattern recognition and classification of images of biological macromolecules using artificial neural networks. , 1994, Biophysical journal.

[17]  N. Cowan,et al.  Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates , 1994, Molecular and cellular biology.

[18]  W. Kabsch,et al.  Atomic structure of the actin: DNase I complex , 1990, Nature.

[19]  M. Lyon,et al.  The t complex polypeptide 1 (TCP-1) is associated with the cytoplasmic aspect of Golgi membranes , 1989, Cell.