References on GroEL
To open the PDF files you need
2008
| 1 |
Asymmetry of the GroEL-GroES Complex under Physiological Conditions as Revealed by Small-Angle X-Ray Scattering Tomonao Inobe, Kazunobu Takahashi, Kosuke Maki, Sawako Enoki, Kiyoto Kamagata, Akio Kadooka, Munehito Arai, and Kunihiro Kuwajima Biophys. J. 94: 1392-1402 (2008) (PDF File) |
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2007
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Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner Yakov Kipnis, Niv Papo, Gilad Haran, and Amnon Horovitz Proc. Natl. Acad. Sci. USA 104:3119-3124 (2007). (PDF File) |
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2006
| 1 |
Co-translational binding of GroEL to nascent polypeptides is followed by post-translational encapsulation by GroES to mediate protein folding Bei-Wen Ying, Hideki Taguchi, and Takuya Ueda J. Biol. Chem. 281(31):21813-21819 (2006). (PDF File) |
| 2 |
GroEL-GroES-mediated protein folding Arthur L. Horwich, George W. Farr, and Wayne A. Fenton Chem. Rev. 106:1917-1930 (2006). (PDF File) |
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Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL Ayumi Koike-Takeshita, Tatsuro Shimamura, Ken Yokoyama, Masasuke Yoshida, and Hideki Taguchi J. Biol. Chem. 281:962-967 (2006) (PDF File) |
2005
| 1 |
Characterization of archaeal group II chaperonin-ADP-metal fluoride complexes: implications that group II chaperonins operates as a "two-stroke engine" Ryo Iizuka, Takao Yoshida, Moriyuki Ishii, Tamotsu Zako, Kazunobu Takahashi, Kosuke maki, Tomonao Inobe, Kunihiro Kuwajima, and Masafumi Yohda J. Biol. Chem. 280(48):40375-40383 (2005). (PDF File) |
| 2 |
Chaperonin GroEL meets the substrate protein as a "Load of the Rings" Hideki Taguchi J. Biochem. 137:543-549 (2005) (PDF File) |
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Single-molecule fluorescence spectroscopy of protein folding Benjamin Schuler ChemPhysChem 6:1206-1220 (2005). (PDF File) |
| 4 |
The 13Å Structure of a Chaperonin GroEL-Protein Substrate Complex by Cryo-electron Microscopy S. Falke, F. Tama, C.L. Brooks III, E.P. Gogol and M.T. Fisher J. Mol. Biol. 348:219-230 (2005). (PDF File) |
| 5 |
Asymmetric binding of membrane proteins to GroEL Jinhchuan Sun, Christos G. Savva, John Deaton, H. Ronald Kaback, Maja Svrakic, Ry Ypung, and Andreas Holzenburg Arch. Biochem. Biophys. 434:352-357 (2005). (PDF File) |
| 6 |
Allosteric regulation of chaperonins Amnon Horovitz, and Keith R. Willison Current Opinion Struct. Biol. 15:646-651 (2005). (PDF File) |
2004
| 1 |
Crystal structure of the native Chaperonin complex from thermus thermophilus reviealed unexpected asymmetry at the cis-cavity Tatsuro Shimamura, Ayumi Koike-Takeshita, Ken Yokoyama, Ryoji Masui, Noriyuki Murai, Masasuke Yoshida, Hideki Taguchi, and So Iwata Structure 12:1471-1480 (2004). (PDF FIle) |
| 2 |
GroEL Mediates Protein Folding with a Two Successive Timer Mechanism Taro Ueno, Hideki Taguchi, Hisashi Tadakuma, Masasuke Yoshida, and Takashi Funatsu Molecular Cell 14:423–434 (2004). (PDF File) |
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3 |
A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive disscoation B Trevor Sewell, Robert B Best, Shaoxia Chen, Alan M Roseman, Geoge W Farr, Arthur L. Horwich and Helen R. Saibil Nature Struct. Mol. Biol. 11:1128–1133 (2004). (PDF File) |
| 4 |
Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL Fumihiro Motojima, Charu chaudhry, Wayne A. Fenton, George W. Farr, and Arthur L. Horwich Proc. Natl. Acad. Sci. USA 101(42):15005-15012 (2004). (PDF File) |
| 5 |
Single molecule imaging of protein folding mediated by chaperonin GroEL Taro Ueno Thesis (Waseda University) (2004). (PDF File) |
2003
| 1 |
Chaperonin-mediated protein folding: fate of substrate polypeptide Wayne A. Fenton and Arthur L. Horwich Quarterly Reviews of Biophysics 36(2):229-256 (2003). (PDF File) |
| 2 |
Role of the γ-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics Charu chaudhry, George W. Farr, Matthew J. Todd, Hays S. Rye, Axel T. Brunger, Paul D. Adams, Arthur L. Horwich, and Paul B. Sigler EMBO J. 22(19):4877-4887 (2003). (PDF File) |
2002
2001
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1 |
Synchronized Domain-opening Motion of GroEL is Essential for Communication between the Two Rings K. Shiseki, N. Murai, F. Motojima, T. Hisabori, M. Yoshida, and H. Taguchi J. Biol. Chem. 276(14):11335-11338 (2001). (PDF File) |
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2 |
Single-molecule observation of protein–protein interactions in the chaperonin system Hideki Taguchi, Taro Ueno, Hisashi Tadakuma, Masasuke Yoshida, Takashi Funatsu Nature Biotech.19:861-865 (2001). (PDF File) |
| 3 |
GroEL/GroES-mediated folding of a protein too large to be encapsulated Tapan K. Cahudhuri, George W. Farr, Wayne A. Fenton, Sabine Rospert, and Arthur L. Horwich Cell 107:235-246 (2001). (PDF File) |
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Review: Allosteyr in Chaperonins Amnon Horvitz, Yael Fridmann, Calit Kafri, and Ofer Yifrach J. Struct. Biol. 135:104-114 (2001). (PDF File) |
| 5 |
Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1 Kafri, G., Willison KR, and Horovitz A Protein Sci. 10:445-449 (2001). (PDF File) |
| 6 |
Dual function of protein confinement in chaperonin-assisted protein folding Achim Brinker, Guenther Pfeifer, Michael J. Kerner, Dean J. Naylor, F. Ulrich Hartl, and Manajit Hayer-Hartl Cell 107: 223-233 (2001) (PDF File) |
| 7 |
Review: A Structural View of the GroEL Chaperone Cycle Holger Grallert and Johannes Buchner J. Struct. Biol. 135:95-103 (2001). (PDF File) |
2000
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1 |
A Dynamic Model for the Allosteric Mechnism of GroEL J. Ma, P.B. Sigler, Z. Xu and M. Karplus J. Mol. Biol. 302:303-313 (2000). (PDF File) |
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Probing protein-protein interactions in real time Mario B. Viani, Lia I. Pietrasanta, James B. Thompson, Ami chand, Ilse C. Gebenshuber, Jhanness H. Kindt, Michael Richter, Helen G. Hansma and Paul K. Hansma Nature Struct. Bio. 7(8):644-647 (2000). (PDF File) |
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3 |
Coupling between protein folding and allosttery in the GroE chaperonin system O. Yifrach and . Horovitz PNAS 97(4):1521-1524 (2000). (PDF File) |
| 4 |
Limits of protein folding inside GroE complexes Holger Grallert, Kerstin Rutkat, and Johannes Buchner J. Biol. Chem. 275:20424-20430 (2000). (PDF File) |
Prior to 2000
| 1 |
GroEL-GroES cycling: ATP and nonnative @olypeptide direct alternation of folding-active rings hays S. Rye, Alan M. Roseman, Shaxia Chen, Krystyna Furtak, Wayne A. Fenton, Helen R. Saibil, and Arthur L. Horwich Cell 97:325-338 (1999). (PDF File) |
| 2 |
Catalysis, commitment and encapsulation during GroE-mediated folding Martina Beissinger, Kerstin Rutkat, and Johannes Buchner J. Mol. Biol. 289:1075-1092 (1999). (PDF File) |
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3 |
The Hsp70 and HSP60 Chaperone Machines Bernd Bukau and Arthur L. Horwich Cell 92:351-366 (1998). (PDF File) |
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GroEL traps dimeric and monomeric unfolding intermediates of citrate synthase Holger Gralleret, Kerstin Rutkat, and Johannes Buchner J. Biol. Chem. 273(50):33305-33310 (1998). (PDF File) |
| 5 |
Asymmetry, commitment and inhibition in the GroE ATPase cycle impose altering functions on the two GroEL rings Neil M. kad, Neil A. Ranson, Matthew J. Cliff and Anthony R. Clarke J. Mol. Biol. 278:267-278 (1998). (PDF File) |
| 6 |
Structure and function in GroEL-mediated protein folding Paul B. Sigler, Zhaohui Xu, Hays S. Rye, Steven G. Burston, Wayne A. Fenton, and Arthur L. HorwichBernd Bukau and Arthur L. Horwich Annu. Rev. Biochem. 67:581-608 (1998). (PDF File) |
| 7 |
Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL Hays S. Rye, Steven G. Burston, Wayne A. Fenton, Joseph M. Beechem, Zhaohui Xu, Paul B. Sigler, and Arthur L. Horwich Nature 388:792-798 (1997). (PDF File) |
| 8 |
Catalysis of protein folding by symmetric chaperone complexes. Sparrer H., Rutkat K., and Buchner J. Proc. Natl. Acad. Sci. USA 94:1096-1100 (1997). (PDF File) |
| 9 |
How GroES regulates binding of nonnative protein to GroEL Helmut Sparrer and Johannes Buchner J. Biol. Chem. 272(22):14080-14086 (1997). (PDF File) |
| 10 |
The chaperonin ATPase cycle: mechanism of allosteric switching and movementts of substrate-binding domains in GroEL Alan M. Roseman, Shaoxia Chen, Helen White, Kerstin Braig, and Helen R. Saibil Cell 78:241-251 (1996). (PDF File) |
| 11 |
Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL Ofer Yifrach and Amnon Horovitz Biochemistry 34(16):5303-5308 (1995). (PDF File) |
| 12 |
Increased efficiency of GroE-assisted protein filding by manganese ions Sophia Diamant, Abdussalam Azem, Celeste Weiss, and Pierre Goloubinoff J. Biol. Chem. 270:28387-28391 (1995). (PDF File) |
| 13 |
The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 Heterooligomer A. Azem, S. Diamant, M. Kessel, C. Weiss, and P. Goloubinoff Proc. Natl. Acad. Sci. USA 92:12021-12025 (1995). (PDF File) |
| 14 |
Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes Andreas Engel, Manajit K. Hayer-Hartl, Kenneth N. Goldie, Gunter Pfeifer, Reiner Hegerl, Shirley Muller, Ana C.R. da Silva, Wolfgang baumeister, F. Ulrich Hartl Science 269:832-836 (1995). (PDF File) |
| 15 |
Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding Manajit K. Hayer-Hartl, Jorg Martin, and F. Ulrich Hartl Science 269:836-841 (1995). (PDF File) |
| 16 |
Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy Shaoxia Chen, Alan M. Roseman, Alilson S. Hunter, Stephen P. Wood, Steven G. Burston, Neil A. Ranson, Anthony R. Clarke & Helen R. Saibil Nature 371:261-264 (1994). (PDF File) |
