Protein folding: Versatility of the cytosolic chaperonin TRiC/CCT
暂无分享,去创建一个
[1] W. Baumeister,et al. Conformational rearrangements of an archaeal chaperonin upon ATPase cycling , 2000, Current Biology.
[2] Julie Grantham,et al. Eukaryotic type II chaperonin CCT interacts with actin through specific subunits , 1999, Nature.
[3] V. Thulasiraman,et al. Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC. , 1999, Molecular cell.
[4] C. Dobson,et al. MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin , 1999, The EMBO journal.
[5] Dmitrij Frishman,et al. Identification of in vivo substrates of the chaperonin GroEL , 1999, Nature.
[6] W. Baumeister,et al. Group II chaperonins: new TRiC(k)s and turns of a protein folding machine. , 1999, Journal of molecular biology.
[7] D A Winkelmann,et al. Myosin II Folding Is Mediated by a Molecular Chaperonin* , 1999, The Journal of Biological Chemistry.
[8] Doolittle Wf. Phylogenetic Classification and the Universal Tree , 1999 .
[9] J. Vandekerckhove,et al. The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins. , 1999, Biochemistry.
[10] A. Shevchenko,et al. Compartmentation of protein folding in vivo: sequestration of non‐native polypeptide by the chaperonin–GimC system , 1999, The EMBO journal.
[11] Judith Frydman,et al. In vivo newly translated polypeptides are sequestered in a protected folding environment , 1999, The EMBO journal.
[12] H. Saibil,et al. Molecular chaperones and folding catalysts , 1999 .
[13] L. Orgel,et al. Phylogenetic Classification and the Universal Tree , 1999 .
[14] J. Vandekerckhove,et al. Prefoldin, a Chaperone that Delivers Unfolded Proteins to Cytosolic Chaperonin , 1998, Cell.
[15] Robert Huber,et al. Crystal Structure of the Thermosome, the Archaeal Chaperonin and Homolog of CCT , 1998, Cell.
[16] K. Siegers,et al. A novel protein complex promoting formation of functional α‐ and γ‐tubulin , 1998, The EMBO journal.
[17] L. Amos,et al. Crystal structure of the bacterial cell-division protein FtsZ , 1998, Nature.
[18] W. Baumeister,et al. Structure of the Substrate Binding Domain of the Thermosome, an Archaeal Group II Chaperonin , 1997, Cell.
[19] G. Farr,et al. Newly-synthesized beta-tubulin demonstrates domain-specific interactions with the cytosolic chaperonin. , 1996, Biochemistry.
[20] F. Hartl. Molecular chaperones in cellular protein folding , 1996, Nature.
[21] R. Doolittle. The origins and evolution of eukaryotic proteins. , 1995, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.
[22] W. Tap,et al. Specificity in chaperonin-mediated protein folding , 1995, Nature.
[23] 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.