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Items: 1 to 20 of 68

1.
Hinge-linker elements in the AAA+ protein unfoldase ClpX mediate intersubunit communication, assembly, and mechanical activity
Tristan A. Bell, Tania A. Baker, Robert T. Sauer
Biochemistry. Author manuscript; available in PMC 2020 Mar 24.
Published in final edited form as: Biochemistry. 2018 Dec 11; 57(49): 6787–6796. Published online 2018 Nov 20. doi: 10.1021/acs.biochem.8b00907
PMCID:
PMC7091491
AbstractArticlePDF–921K
2.
Deciphering the roles of multi-component recognition signals by the AAA+ unfoldase, ClpX
Lorraine Ling, Sherwin P. Montaño, Robert T. Sauer, Phoebe A. Rice, Tania A. Baker
J Mol Biol. Author manuscript; available in PMC 2016 Sep 11.
Published in final edited form as: J Mol Biol. 2015 Sep 11; 427(18): 2966–2982. Published online 2015 Mar 19. doi: 10.1016/j.jmb.2015.03.008
PMCID:
PMC4569521
AbstractArticlePDF–2.0M
3.
Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine
Benjamin M. Stinson, Andrew R. Nager, Steven E. Glynn, Karl R. Schmitz, Tania A. Baker, Robert T. Sauer
Cell. Author manuscript; available in PMC 2014 Apr 25.
Published in final edited form as: Cell. 2013 Apr 25; 153(3): 628–639. doi: 10.1016/j.cell.2013.03.029
PMCID:
PMC3674332
AbstractArticlePDF–4.2M
4.
Crystal structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine
Steven E. Glynn, Andreas Martin, Andrew R. Nager, Tania A. Baker, Robert T. Sauer
Cell. Author manuscript; available in PMC 2010 Nov 13.
Published in final edited form as: Cell. 2009 Nov 13; 139(4): 744–756. doi: 10.1016/j.cell.2009.09.034
PMCID:
PMC2778613
AbstractArticlePDF–4.2M
5.
Unique contacts direct high-priority recognition of the tetrameric transposase-DNA complex by the AAA+ unfoldase ClpX
Aliaa H. Abdelhakim, Elizabeth C. Oakes, Robert T. Sauer, Tania A. Baker
Mol Cell. Author manuscript; available in PMC 2009 Jul 28.
Published in final edited form as: Mol Cell. 2008 Apr 11; 30(1): 39–50. doi: 10.1016/j.molcel.2008.02.013
PMCID:
PMC2717000
AbstractArticlePDF–2.8M
6.
Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding
Andreas Martin, Tania A. Baker, Robert T. Sauer
Nat Struct Mol Biol. Author manuscript; available in PMC 2009 May 1.
Published in final edited form as: Nat Struct Mol Biol. 2008 Nov; 15(11): 1147–1151. Published online 2008 Oct 19. doi: 10.1038/nsmb.1503
PMCID:
PMC2610342
AbstractArticlePDF–1002K
7.
Activation of a Dormant ClpX Recognition Motif of Bacteriophage Mu Repressor by Inducing High Local Flexibility
Kimberly R. Marshall-Batty, Hiroshi Nakai
J Biol Chem. 2008 Apr 4; 283(14): 9060–9070. doi: 10.1074/jbc.M705508200
PMCID:
PMC2431027
AbstractArticlePDF–687K
8.
Remodeling protein complexes: Insights from the AAA+ unfoldase ClpX and Mu transposase
Briana M. Burton, Tania A. Baker
Protein Sci. 2005 Aug; 14(8): 1945–1954. doi: 10.1110/ps.051417505
PMCID:
PMC2279306
AbstractArticlePDF–428K
9.
Specificity in substrate and cofactor recognition by the N-terminal domain of the chaperone ClpX
Guillaume Thibault, Jovana Yudin, Philip Wong, Vladimir Tsitrin, Remco Sprangers, Rongmin Zhao, Walid A. Houry
Proc Natl Acad Sci U S A. 2006 Nov 21; 103(47): 17724–17729. Published online 2006 Nov 7. doi: 10.1073/pnas.0601505103
PMCID:
PMC1693814
AbstractArticlePDF–1.0M
10.
ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis.
R Kruklitis, D J Welty, H Nakai
EMBO J. 1996 Feb 15; 15(4): 935–944.
PMCID:
PMC450291
SummaryPage BrowsePDF–2.4M
11.
The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone.
A Wawrzynow, D Wojtkowiak, J Marszalek, B Banecki, M Jonsen, B Graves, C Georgopoulos, M Zylicz
EMBO J. 1995 May 1; 14(9): 1867–1877. doi: 10.1002/j.1460-2075.1995.tb07179.x
PMCID:
PMC398286
SummaryPage BrowsePDF–2.1M
12.
Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates
Samia M. Siddiqui, Robert T. Sauer, Tania A. Baker
Genes Dev. 2004 Feb 15; 18(4): 369–374. doi: 10.1101/gad.1170304
PMCID:
PMC359390
AbstractArticlePDF–203K
13.
The replication initiation protein of the broad-host-range plasmid RK2 is activated by the ClpX chaperone
Igor Konieczny, Donald R. Helinski
Proc Natl Acad Sci U S A. 1997 Dec 23; 94(26): 14378–14382. doi: 10.1073/pnas.94.26.14378
PMCID:
PMC24985
AbstractArticlePDF–204K
14.
A split protease-E. coli ClpXP system quantifies protein–protein interactions in Escherichia coli cells
Shengchen Wang, Faying Zhang, Meng Mei, Ting Wang, Yueli Yun, Shihui Yang, Guimin Zhang, Li Yi
Commun Biol. 2021; 4: 841. Published online 2021 Jul 6. doi: 10.1038/s42003-021-02374-w
PMCID:
PMC8260793
AbstractArticlePDF–2.3M
15.
Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX
Benjamin M. Stinson, Vladimir Baytshtok, Karl R. Schmitz, Tania A. Baker, Robert T. Sauer
Nat Struct Mol Biol. Author manuscript; available in PMC 2015 Nov 1.
Published in final edited form as: Nat Struct Mol Biol. 2015 May; 22(5): 411–416. Published online 2015 Apr 13. doi: 10.1038/nsmb.3012
PMCID:
PMC4424054
AbstractArticlePDF–1.0M
16.
ClpX(P) Generates Mechanical Force to Unfold and Translocate Its Protein Substrates
Rodrigo A. Maillard, Gheorghe Chistol, Maya Sen, Maurizio Righini, Jiongyi Tan, Christian M. Kaiser, Courtney Hodges, Andreas Martin, Carlos Bustamante
Cell. Author manuscript; available in PMC 2013 Jun 19.
Published in final edited form as: Cell. 2011 Apr 29; 145(3): 459–469. doi: 10.1016/j.cell.2011.04.010
PMCID:
PMC3686100
AbstractArticlePDF–2.4M
17.
Versatile modes of peptide recognition by the ClpX N domain mediate alternative adaptor-binding specificities in different bacterial species
Tahmeena Chowdhury, Peter Chien, Shamsah Ebrahim, Robert T Sauer, Tania A Baker
Protein Sci. 2010 Feb; 19(2): 242–254. Published online 2009 Dec 10. doi: 10.1002/pro.306
PMCID:
PMC2865724
AbstractArticlePDF–867K
18.
Conformation of a plasmid replication initiator protein affects its proteolysis by ClpXP system
Marcin Pierechod, Agnieszka Nowak, Anna Saari, Elzbieta Purta, Janusz M Bujnicki, Igor Konieczny
Protein Sci. 2009 Mar; 18(3): 637–649. Published online 2009 Jan 28. doi: 10.1002/pro.68
PMCID:
PMC2760369
AbstractArticlePDF–520K
19.
Engineering Synthetic Adaptors and Substrates for Controlled ClpXP Degradation
Joseph H. Davis, Tania A. Baker, Robert T. Sauer
J Biol Chem. 2009 Aug 14; 284(33): 21848–21855. Published online 2009 Jun 23. doi: 10.1074/jbc.M109.017624
PMCID:
PMC2755909
AbstractArticlePDF–871K
20.
Polypeptide translocation by the AAA+ ClpXP protease machine
Sarah R. Barkow, Igor Levchenko, Tania A. Baker, Robert T. Sauer
Chem Biol. Author manuscript; available in PMC 2009 Dec 26.
Published in final edited form as: Chem Biol. 2009 Jun 26; 16(6): 605–612. doi: 10.1016/j.chembiol.2009.05.007
PMCID:
PMC2718738
AbstractArticlePDF–752K

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