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Items: 1 to 20 of 59

1.
GroEL actively stimulates folding of the endogenous substrate protein PepQ
Jeremy Weaver, Mengqiu Jiang, Andrew Roth, Jason Puchalla, Junjie Zhang, Hays S. Rye
Nat Commun. 2017; 8: 15934. Published online 2017 Jun 30. doi: 10.1038/ncomms15934
PMCID:
PMC5497066
AbstractArticlePDF–1.7M
2.
Single-molecule Observation of Protein Folding in Symmetric GroEL-(GroES)2 Complexes
Yodai Takei, Ryo Iizuka, Taro Ueno, Takashi Funatsu
J Biol Chem. 2012 Nov 30; 287(49): 41118–41125. Published online 2012 Oct 9. doi: 10.1074/jbc.M112.398628
PMCID:
PMC3510812
AbstractArticlePDF–1.0M
3.
Revisiting the GroEL-GroES Reaction Cycle via the Symmetric Intermediate Implied by Novel Aspects of the GroEL(D398A) Mutant
Ayumi Koike-Takeshita, Masasuke Yoshida, Hideki Taguchi
J Biol Chem. 2008 Aug 29; 283(35): 23774–23781. doi: 10.1074/jbc.M802542200
PMCID:
PMC3259786
AbstractArticlePDF–341K
4.
Football- and Bullet-shaped GroEL-GroES Complexes Coexist during the Reaction Cycle
Tomoya Sameshima, Taro Ueno, Ryo Iizuka, Noriyuki Ishii, Naofumi Terada, Kohki Okabe, Takashi Funatsu
J Biol Chem. 2008 Aug 29; 283(35): 23765–23773. doi: 10.1074/jbc.M802541200
PMCID:
PMC3259762
AbstractArticlePDF–334K
5.
Stimulating the Substrate Folding Activity of a Single Ring GroEL Variant by Modulating the Cochaperonin GroES
Melissa Illingworth, Andrew Ramsey, Zhida Zheng, Lingling Chen
J Biol Chem. 2011 Sep 2; 286(35): 30401–30408. Published online 2011 Jul 10. doi: 10.1074/jbc.M111.255935
PMCID:
PMC3162399
AbstractArticlePDF–1.1M
6.
Covalent Structural Changes in Unfolded GroES That Lead to Amyloid Fibril Formation Detected by NMR: INSIGHT INTO INTRINSICALLY DISORDERED PROTEINS
Hisanori Iwasa, Shunsuke Meshitsuka, Kunihiro Hongo, Tomohiro Mizobata, Yasushi Kawata
J Biol Chem. 2011 Jun 17; 286(24): 21796–21805. Published online 2011 Apr 20. doi: 10.1074/jbc.M111.228445
PMCID:
PMC3122234
AbstractArticlePDF–3.3M
7.
Structure of a chaperonin complex with a newly folded protein encapsulated in the folding chamber
D.K. Clare, P.J. Bakkes, H. van Heerikhuizen, S. M. van der Vies, H.R. Saibil
Nature. Author manuscript; available in PMC 2009 Aug 19.
Published in final edited form as: Nature. 2009 Jan 1; 457(7225): 107–110. doi: 10.1038/nature07479
PMCID:
PMC2728927
AbstractArticlePDF–1.6M
8.
Location and Flexibility of the Unique C-Terminal Tail of Aquifex aeolicus Co-Chaperonin Protein 10 as Derived by Cryo-Electron Microscopy and Biophysical Techniques
Dong-Hua Chen, Kathryn Luke, Junjie Zhang, Wah Chiu, Pernilla Wittung-Stafshede
J Mol Biol. Author manuscript; available in PMC 2008 Dec 31.
Published in final edited form as: J Mol Biol. 2008 Sep 5; 381(3): 707–717. Published online 2008 Jun 17. doi: 10.1016/j.jmb.2008.06.021
PMCID:
PMC2612737
AbstractArticlePDF–2.4M
9.
Essential role of the chaperonin folding compartment in vivo
Yun-Chi Tang, Hung-Chun Chang, Kausik Chakraborty, F Ulrich Hartl, Manajit Hayer-Hartl
EMBO J. 2008 May 21; 27(10): 1458–1468. Published online 2008 Apr 17. doi: 10.1038/emboj.2008.77
PMCID:
PMC2396394
AbstractArticlePDF–353K
10.
A mobile loop order–disorder transition modulates the speed of chaperonin cycling
Frank Shewmaker, Michael J. Kerner, Manajit Hayer-Hartl, Gracjana Klein, Costa Georgopoulos, Samuel J. Landry
Protein Sci. 2004 Aug; 13(8): 2139–2148. doi: 10.1110/ps.04773204
PMCID:
PMC2279813
AbstractArticlePDF–218K
11.
Identifying natural substrates for chaperonins using a sequence-based approach
George Stan, Bernard R. Brooks, George H. Lorimer, D. Thirumalai
Protein Sci. 2005 Jan; 14(1): 193–201. doi: 10.1110/ps.04933205
PMCID:
PMC2253340
AbstractArticlePDF–195K
12.
Multiple equilibria of the Escherichia coli chaperonin GroES revealed by mass spectrometry
Lynda J. Donald, David J. Stokell, Neil J. Holliday, Werner Ens, Kenneth G. Standing, Harry W. Duckworth
Protein Sci. 2005 May; 14(5): 1375–1379. doi: 10.1110/ps.041164305
PMCID:
PMC2253275
AbstractArticlePDF–86K
13.
Conservation among HSP60 sequences in relation to structure, function, and evolution.
L. Brocchieri, S. Karlin
Protein Sci. 2000 Mar; 9(3): 476–486. doi: 10.1110/ps.9.3.476
PMCID:
PMC2144576
SummaryPDF–2.1M
14.
Allosteric Transitions in the Chaperonin GroEL are Captured by a Dominant Normal Mode that is Most Robust to Sequence Variations
Wenjun Zheng, Bernard R. Brooks, D. Thirumalai
Biophys J. 2007 Oct 1; 93(7): 2289–2299. Published online 2007 Jun 8. doi: 10.1529/biophysj.107.105270
PMCID:
PMC1965427
AbstractArticlePDF–1.5M
15.
Filamentous Morphology in GroE-Depleted Escherichia coli Induced by Impaired Folding of FtsE
Kei Fujiwara, Hideki Taguchi
J Bacteriol. 2007 Aug; 189(16): 5860–5866. Published online 2007 Jun 8. doi: 10.1128/JB.00493-07
PMCID:
PMC1952032
AbstractArticlePDF–319K
16.
Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein
George Stan, George H. Lorimer, D. Thirumalai, Bernard R. Brooks
Proc Natl Acad Sci U S A. 2007 May 22; 104(21): 8803–8808. Published online 2007 May 11. doi: 10.1073/pnas.0700607104
PMCID:
PMC1885583
AbstractArticlePDF–1.8M
17.
GroEL/S substrate specificity based on substrate unfolding propensity
Kristin N. Parent, Carolyn M. Teschke
Cell Stress Chaperones. 2007 Mar; 12(1): 20–32. doi: 10.1379/CSC-219R.1
PMCID:
PMC1852890
AbstractArticlePDF–545K
18.
Dynamics of allosteric transitions in GroEL
Changbong Hyeon, George H. Lorimer, D. Thirumalai
Proc Natl Acad Sci U S A. 2006 Dec 12; 103(50): 18939–18944. Published online 2006 Nov 29. doi: 10.1073/pnas.0608759103
PMCID:
PMC1748156
AbstractArticlePDF–3.4M
19.
Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection
Tomoya Baba, Takeshi Ara, Miki Hasegawa, Yuki Takai, Yoshiko Okumura, Miki Baba, Kirill A Datsenko, Masaru Tomita, Barry L Wanner, Hirotada Mori
Mol Syst Biol. 2006; 2: 2006.0008. Published online 2006 Feb 21. doi: 10.1038/msb4100050
PMCID:
PMC1681482
AbstractArticlePDF–400K
20.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110
Koji Hayashi, Naoki Morooka, Yoshihiro Yamamoto, Katsutoshi Fujita, Katsumi Isono, Sunju Choi, Eiichi Ohtsubo, Tomoya Baba, Barry L Wanner, Hirotada Mori, Takashi Horiuchi
Mol Syst Biol. 2006; 2: 2006.0007. Published online 2006 Feb 21. doi: 10.1038/msb4100049
PMCID:
PMC1681481
AbstractArticlePDF–141K

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