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Items: 1 to 20 of 104


A tightly regulated molecular toggle controls AAA+ disaggregase.

Oguchi Y, Kummer E, Seyffer F, Berynskyy M, Anstett B, Zahn R, Wade RC, Mogk A, Bukau B.

Nat Struct Mol Biol. 2012 Dec;19(12):1338-46. doi: 10.1038/nsmb.2441. Epub 2012 Nov 18.


M domains couple the ClpB threading motor with the DnaK chaperone activity.

Haslberger T, Weibezahn J, Zahn R, Lee S, Tsai FT, Bukau B, Mogk A.

Mol Cell. 2007 Jan 26;25(2):247-60.


Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments.

Haslberger T, Zdanowicz A, Brand I, Kirstein J, Turgay K, Mogk A, Bukau B.

Nat Struct Mol Biol. 2008 Jun;15(6):641-50. doi: 10.1038/nsmb.1425. Epub 2008 May 18.


Domain stability in the AAA+ ATPase ClpB from Escherichia coli.

Nagy M, Akoev V, Zolkiewski M.

Arch Biochem Biophys. 2006 Sep 1;453(1):63-9. Epub 2006 Mar 23.


Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity.

Mogk A, Schlieker C, Strub C, Rist W, Weibezahn J, Bukau B.

J Biol Chem. 2003 May 16;278(20):17615-24. Epub 2003 Mar 6.


Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency.

Zhang T, Ploetz EA, Nagy M, Doyle SM, Wickner S, Smith PE, Zolkiewski M.

Proteins. 2012 Dec;80(12):2758-68. doi: 10.1002/prot.24159. Epub 2012 Sep 15.


Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces.

Seyffer F, Kummer E, Oguchi Y, Winkler J, Kumar M, Zahn R, Sourjik V, Bukau B, Mogk A.

Nat Struct Mol Biol. 2012 Dec;19(12):1347-55. doi: 10.1038/nsmb.2442. Epub 2012 Nov 18.


Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation.

Desantis ME, Sweeny EA, Snead D, Leung EH, Go MS, Gupta K, Wendler P, Shorter J.

J Biol Chem. 2014 Jan 10;289(2):848-67. doi: 10.1074/jbc.M113.520759. Epub 2013 Nov 26.


Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB.

Nagy M, Wu HC, Liu Z, Kedzierska-Mieszkowska S, Zolkiewski M.

Protein Sci. 2009 Feb;18(2):287-93. doi: 10.1002/pro.36.


Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation.

Carroni M, Kummer E, Oguchi Y, Wendler P, Clare DK, Sinning I, Kopp J, Mogk A, Bukau B, Saibil HR.

Elife. 2014 Apr 30;3:e02481. doi: 10.7554/eLife.02481.


Characterization of a trap mutant of the AAA+ chaperone ClpB.

Weibezahn J, Schlieker C, Bukau B, Mogk A.

J Biol Chem. 2003 Aug 29;278(35):32608-17. Epub 2003 Jun 12.


The elusive middle domain of Hsp104 and ClpB: location and function.

Desantis ME, Shorter J.

Biochim Biophys Acta. 2012 Jan;1823(1):29-39. doi: 10.1016/j.bbamcr.2011.07.014. Epub 2011 Jul 24. Review.


Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity.

Watanabe YH, Nakazaki Y, Suno R, Yoshida M.

Biochem J. 2009 Jun 12;421(1):71-7. doi: 10.1042/BJ20082238.


Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system.

Doyle SM, Hoskins JR, Wickner S.

Proc Natl Acad Sci U S A. 2007 Jul 3;104(27):11138-44. Epub 2007 Jun 1.


The ClpB/Hsp104 molecular chaperone-a protein disaggregating machine.

Lee S, Sowa ME, Choi JM, Tsai FT.

J Struct Biol. 2004 Apr-May;146(1-2):99-105. Review.


Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation.

Miot M, Reidy M, Doyle SM, Hoskins JR, Johnston DM, Genest O, Vitery MC, Masison DC, Wickner S.

Proc Natl Acad Sci U S A. 2011 Apr 26;108(17):6915-20. doi: 10.1073/pnas.1102828108. Epub 2011 Apr 7.


Novel insights into the mechanism of chaperone-assisted protein disaggregation.

Weibezahn J, Schlieker C, Tessarz P, Mogk A, Bukau B.

Biol Chem. 2005 Aug;386(8):739-44. Review.


Analysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangement.

Yamasaki T, Oohata Y, Nakamura T, Watanabe YH.

J Biol Chem. 2015 Apr 10;290(15):9789-800. doi: 10.1074/jbc.M114.617696. Epub 2015 Feb 24.

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