Crossref journal-article
Elsevier BV
Structure (78)
Bibliography

Clare, D. K., Stagg, S., Quispe, J., Farr, G. W., Horwich, A. L., & Saibil, H. R. (2008). Multiple States of a Nucleotide-Bound Group 2 Chaperonin. Structure, 16(4), 528–534.

Authors 6
  1. Daniel K. Clare (first)
  2. Scott Stagg (additional)
  3. Joel Quispe (additional)
  4. George W. Farr (additional)
  5. Arthur L. Horwich (additional)
  6. Helen R. Saibil (additional)
References 40 Referenced 31
  1. 10.1016/j.jmb.2005.01.066 / J. Mol. Biol. / Cooperativity in the thermosome by Bigotti (2005)
  2. 10.1038/371578a0 / Nature / The crystal structure of the bacterial chaperonin GroEL at 2.8 Å by Braig (1994)
  3. 10.1016/S0092-8674(00)80928-9 / Cell / The Hsp70 and Hsp60 chaperone machines by Bukau (1998)
  4. 10.1074/jbc.M601605200 / J. Biol. Chem. / Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE by Cliff (2006)
  5. 10.1006/jsbi.1996.0003 / J. Struct. Biol. / MRC image processing programs by Crowther (1996)
  6. 10.1016/S0092-8674(00)81152-6 / Cell / Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT by Ditzel (1998)
  7. 10.1016/j.molcel.2007.04.004 / Mol. Cell / Topologies of a substrate protein bound to the chaperonin GroEL by Elad (2007)
  8. 10.1038/371614a0 / Nature / Residues in chaperonin GroEL required for polypeptide binding and release by Fenton (1994)
  9. 10.1006/jsbi.1996.0030 / J. Struct. Biol. / SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields by Frank (1996)
  10. 10.1146/annurev.biochem.70.1.603 / Annu. Rev. Biochem. / Folding of newly translated proteins in vivo: the role of molecular chaperones by Frydman (2001)
  11. 10.1006/jmbi.1999.3008 / J. Mol. Biol. / Group II chaperonins: new TRiC(k)s and turns of a protein folding machine by Gutsche (1999)
  12. 10.1006/jsbi.2001.4373 / J. Struct. Biol. / ATP-induced structural change of the thermosome is temperature-dependent by Gutsche (2001)
  13. 10.1016/j.jmb.2003.12.035 / J. Mol. Biol. / Studies on the substrate-binding domains of the thermosome: structural plasticity in the protrusion region by Heller (2004)
  14. 10.1016/j.sbi.2005.10.001 / Curr. Opin. Struct. Biol. / Allosteric regulation of chaperonins by Horovitz (2005)
  15. 10.1146/annurev.cellbio.23.090506.123555 / Annu. Rev. Cell. Dev. Biol. / Two families of chaperonin: physiology and mechanism by Horwich (2007)
  16. 10.1110/ps.44401 / Protein Sci. / Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1 by Kafri (2001)
  17. 10.1016/S0092-8674(00)80408-0 / Cell / Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin by Klumpp (1997)
  18. 10.1016/S0014-5793(03)00722-1 / FEBS Lett. / Nested cooperativity and salt dependence of the ATPase activity of the archaeal chaperonin Mm-cpn by Kusmierczyk (2003)
  19. 10.1042/bj20030230 / Biochem. J. / Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis by Kusmierczyk (2003)
  20. 10.1074/jbc.273.17.10091 / J. Biol. Chem. / ATP binding induces large conformational changes in the apical and equatorial domains of the eukaryotic chaperonin containing TCP-1 complex by Llorca (1998)
  21. 10.1038/10689 / Nat. Struct. Biol. / 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin by Llorca (1999)
  22. 10.1038/45294 / Nature / Eukaryotic type II chaperonin CCT interacts with actin through specific subunits by Llorca (1999)
  23. 10.1093/emboj/20.15.4065 / EMBO J. / The ‘sequential allosteric ring’ mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin by Llorca (2001)
  24. 10.1016/S0092-8674(03)00307-6 / Cell / Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis by Meyer (2003)
  25. 10.1016/S1047-8477(03)00069-8 / J. Struct. Biol. / Accurate determination of local defocus and specimen tilt in electron microscopy by Mindell (2003)
  26. 10.1107/S0907444902013707 / Acta Crystallogr. D. Biol. Crystallogr. / On the fitting of model electron densities into EM reconstructions: a reciprocal-space formulation by Navaza (2002)
  27. 10.1016/S0092-8674(01)00617-1 / Cell / ATP-bound states of GroEL captured by cryo-electron microscopy by Ranson (2001)
  28. 10.1038/nsmb1046 / Nat. Struct. Mol. Biol. / Allosteric signalling of ATP hydrolysis in GroEL-GroES complexes by Ranson (2006)
  29. 10.1038/nsmb901 / Nat. Struct. Mol. Biol. / Sequential ATP-induced allosteric transition of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis by Rivenzon-Segal (2005)
  30. 10.1016/j.jsb.2003.11.007 / J. Struct. Biol. / FindEM—a fast, efficient program for automatic selection of particles from electron micrographs by Roseman (2004)
  31. 10.1126/science.7913554 / Science / Symmetric complexes of GroE chaperonins as part of the functional cycle by Schmidt (1994)
  32. 10.1006/jmbi.2000.3952 / J. Mol. Biol. / Domain rotations between open, closed and bullet-shaped forms of the thermosome, an archaeal chaperonin by Schoehn (2000)
  33. 10.1006/jmbi.2000.3505 / J. Mol. Biol. / Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae by Schoehn (2000)
  34. 10.1146/annurev.biochem.67.1.581 / Annu. Rev. Biochem. / Structure and function in GroEL-mediated protein folding by Sigler (1998)
  35. 10.1016/j.tcb.2004.09.015 / Trends Cell Biol. / Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets by Spiess (2004)
  36. 10.1016/j.molcel.2006.09.003 / Mol. Cell / Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins by Spiess (2006)
  37. 10.1016/j.jsb.2005.03.010 / J. Struct. Biol. / Automated molecular microscopy: the new Leginon system by Suloway (2005)
  38. 10.1006/jsbi.1996.0004 / J. Struct. Biol. / A new generation of the IMAGIC image processing system by van Heel (1996)
  39. 10.1038/41944 / Nature / The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex by Xu (1997)
  40. 10.1006/jmbi.1996.0028 / J. Mol. Biol. / Allosteric control by ATP of non-folded protein binding to GroEL by Yifrach (1996)
Dates
Type When
Created 17 years, 4 months ago (April 9, 2008, 10:02 a.m.)
Deposited 6 years, 8 months ago (Dec. 30, 2018, 7:30 a.m.)
Indexed 1 year, 2 months ago (June 10, 2024, 2:35 a.m.)
Issued 17 years, 5 months ago (April 1, 2008)
Published 17 years, 5 months ago (April 1, 2008)
Published Print 17 years, 5 months ago (April 1, 2008)
Funders 0

None

@article{Clare_2008, title={Multiple States of a Nucleotide-Bound Group 2 Chaperonin}, volume={16}, ISSN={0969-2126}, url={http://dx.doi.org/10.1016/j.str.2008.01.016}, DOI={10.1016/j.str.2008.01.016}, number={4}, journal={Structure}, publisher={Elsevier BV}, author={Clare, Daniel K. and Stagg, Scott and Quispe, Joel and Farr, George W. and Horwich, Arthur L. and Saibil, Helen R.}, year={2008}, month=apr, pages={528–534} }