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Items: 1 to 20 of 83

1.
Structure and function of the GroE chaperone
S. Walter
Cell Mol Life Sci. 2002 Oct; 59(10): 1589–1597. doi: 10.1007/PL00012485
PMCID:
PMC11337506
AbstractPDF–226K
2.
Epoxidized graphene grid for highly efficient high-resolution cryoEM structural analysis
Junso Fujita, Fumiaki Makino, Haruyasu Asahara, Maiko Moriguchi, Shota Kumano, Itsuki Anzai, Jun-ichi Kishikawa, Yoshiharu Matsuura, Takayuki Kato, Keiichi Namba, Tsuyoshi Inoue
Sci Rep. 2023; 13: 2279. Published online 2023 Feb 8. doi: 10.1038/s41598-023-29396-0
PMCID:
PMC9908306
AbstractArticlePDF–3.0M
3.
The Functional Differences between the GroEL Chaperonin of Escherichia coli and the HtpB Chaperonin of Legionella pneumophila Can Be Mapped to Specific Amino Acid Residues
Karla N. Valenzuela-Valderas, Gabriel Moreno-Hagelsieb, John R. Rohde, Rafael A. Garduño
Biomolecules. 2022 Jan; 12(1): 59. Published online 2021 Dec 31. doi: 10.3390/biom12010059
PMCID:
PMC8774168
AbstractArticlePDF–5.4M
4.
Local energetic frustration affects the dependence of green fluorescent protein folding on the chaperonin GroEL
Boudhayan Bandyopadhyay, Adi Goldenzweig, Tamar Unger, Orit Adato, Sarel J. Fleishman, Ron Unger, Amnon Horovitz
J Biol Chem. 2017 Dec 15; 292(50): 20583–20591. Published online 2017 Oct 24. doi: 10.1074/jbc.M117.808576
PMCID:
PMC5733594
AbstractArticlePDF–1.1M
5.
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
6.
The binary protein-protein interaction landscape of Escherichia coli
Seesandra V. Rajagopala, Patricia Sikorski, Ashwani Kumar, Roberto Mosca, James Vlasblom, Roland Arnold, Jonathan Franca-Koh, Suman B. Pakala, Sadhna Phanse, Arnaud Ceol, Roman Häuser, Gabriella Siszler, Stefan Wuchty, Andrew Emili, Mohan Babu, Patrick Aloy, Rembert Pieper, Peter Uetz
Nat Biotechnol. Author manuscript; available in PMC 2014 Sep 1.
Published in final edited form as: Nat Biotechnol. 2014 Mar; 32(3): 285–290. Published online 2014 Feb 23. doi: 10.1038/nbt.2831
PMCID:
PMC4123855
AbstractArticlePDF–1.1M
7.
GroEL stimulates protein folding through forced unfolding
Zong Lin, Damian Madan, Hays S Rye
Nat Struct Mol Biol. Author manuscript; available in PMC 2013 Aug 15.
Published in final edited form as: Nat Struct Mol Biol. 2008 Mar; 15(3): 303–311. Published online 2008 Mar 2. doi: 10.1038/nsmb.1394
PMCID:
PMC3744391
AbstractArticlePDF–1.9M
8.
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
9.
YajL, Prokaryotic Homolog of Parkinsonism-associated Protein DJ-1, Functions as a Covalent Chaperone for Thiol Proteome
Hai-Tuong Le, Valérie Gautier, Fatoum Kthiri, Abderrahim Malki, Nadia Messaoudi, Mouadh Mihoub, Ahmed Landoulsi, Young Jun An, Sun-Shin Cha, Gilbert Richarme
J Biol Chem. 2012 Feb 17; 287(8): 5861–5870. Published online 2011 Dec 7. doi: 10.1074/jbc.M111.299198
PMCID:
PMC3285355
AbstractArticlePDF–1.2M
10.
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
11.
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
12.
Nuclear Magnetic Resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL
Eda Koculi, Reto Horst, Arthur L Horwich, Kurt Wüthrich
Protein Sci. 2011 Aug; 20(8): 1380–1386. Published online 2011 Jun 1. doi: 10.1002/pro.665
PMCID:
PMC3189523
AbstractArticlePDF–298K
13.
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
14.
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
15.
Assembly reflects evolution of protein complexes
Emmanuel D. Levy, Elisabetta Boeri Erba, Carol V. Robinson, Sarah A. Teichmann
Nature. Author manuscript; available in PMC 2009 Mar 19.
Published in final edited form as: Nature. 2008 Jun 26; 453(7199): 1262–1265. Published online 2008 Jun 18. doi: 10.1038/nature06942
PMCID:
PMC2658002
AbstractArticlePDF–1.5M
16.
GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side
Yali Li, Xinfeng Gao, Lingling Chen
J Biol Chem. 2009 Feb 13; 284(7): 4324–4331. doi: 10.1074/jbc.M804818200
PMCID:
PMC2640968
AbstractArticlePDF–452K
17.
Lysine Acetylation Is a Highly Abundant and Evolutionarily Conserved Modification in Escherichia Coli
Junmei Zhang, Robert Sprung, Jimin Pei, Xiaohong Tan, Sungchan Kim, Heng Zhu, Chuan-Fa Liu, Nick V. Grishin, Yingming Zhao
Mol Cell Proteomics. 2009 Feb; 8(2): 215–225. doi: 10.1074/mcp.M800187-MCP200
PMCID:
PMC2634580
AbstractArticlePDF–262K
18.
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
19.
GroEL as a molecular scaffold for structural analysis of the anthrax toxin pore
Hiroo Katayama, Blythe E Janowiak, Marek Brzozowski, Jordan Juryck, Scott Falke, Edward P Gogol, R John Collier, Mark T Fisher
Nat Struct Mol Biol. Author manuscript; available in PMC 2009 Jan 1.
Published in final edited form as: Nat Struct Mol Biol. 2008 Jul; 15(7): 754–760. Published online 2008 Jun 22. doi: 10.1038/nsmb.1442
PMCID:
PMC2504863
AbstractArticlePDF–644K
20.
Concerted release of substrate domains from GroEL by ATP is demonstrated with FRET
Niv Papo, Yakov Kipnis, Gilad Haran, Amnon Horovitz
J Mol Biol. Author manuscript; available in PMC 2009 Jul 18.
Published in final edited form as: J Mol Biol. 2008 Jul 18; 380(4): 717–725. Published online 2008 May 17. doi: 10.1016/j.jmb.2008.05.021
PMCID:
PMC2504006
AbstractArticlePDF–1.4M

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