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Items: 1 to 20 of 54


Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation.

Zietkiewicz S, Lewandowska A, Stocki P, Liberek K.

J Biol Chem. 2006 Mar 17;281(11):7022-9. Epub 2006 Jan 16.


The amino-terminal domain of ClpB supports binding to strongly aggregated proteins.

Barnett ME, Nagy M, Kedzierska S, Zolkiewski M.

J Biol Chem. 2005 Oct 14;280(41):34940-5. Epub 2005 Aug 2.


The N-terminal domain of Escherichia coli ClpB enhances chaperone function.

Chow IT, Barnett ME, Zolkiewski M, Baneyx F.

FEBS Lett. 2005 Aug 15;579(20):4242-8.


Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication.

Song Y, Wu YX, Jung G, Tutar Y, Eisenberg E, Greene LE, Masison DC.

Eukaryot Cell. 2005 Feb;4(2):289-97.


Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.

Weibezahn J, Tessarz P, Schlieker C, Zahn R, Maglica Z, Lee S, Zentgraf H, Weber-Ban EU, Dougan DA, Tsai FT, Mogk A, Bukau B.

Cell. 2004 Nov 24;119(5):653-65.


Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it.

Inoue Y, Taguchi H, Kishimoto A, Yoshida M.

J Biol Chem. 2004 Dec 10;279(50):52319-23. Epub 2004 Sep 23.


Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation.

Zietkiewicz S, Krzewska J, Liberek K.

J Biol Chem. 2004 Oct 22;279(43):44376-83. Epub 2004 Aug 9.


Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers.

Shorter J, Lindquist S.

Science. 2004 Jun 18;304(5678):1793-7. Epub 2004 May 20.


Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104.

Lum R, Tkach JM, Vierling E, Glover JR.

J Biol Chem. 2004 Jul 9;279(28):29139-46. Epub 2004 May 5.


Versatile PCR-mediated insertion or deletion mutagenesis.

Lee J, Lee HJ, Shin MK, Ryu WS.

Biotechniques. 2004 Mar;36(3):398-400. No abstract available.


Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region.

Schirmer EC, Homann OR, Kowal AS, Lindquist S.

Mol Biol Cell. 2004 May;15(5):2061-72. Epub 2004 Feb 20.


The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104.

Grimminger V, Richter K, Imhof A, Buchner J, Walter S.

J Biol Chem. 2004 Feb 27;279(9):7378-83. Epub 2003 Dec 10.


The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state.

Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, Tsai FT.

Cell. 2003 Oct 17;115(2):229-40.


Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104.

Kryndushkin DS, Alexandrov IM, Ter-Avanesyan MD, Kushnirov VV.

J Biol Chem. 2003 Dec 5;278(49):49636-43. Epub 2003 Sep 24.


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.


Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ+].

Lopez N, Aron R, Craig EA.

Mol Biol Cell. 2003 Mar;14(3):1172-81.


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.


AAA proteins.

Lupas AN, Martin J.

Curr Opin Struct Biol. 2002 Dec;12(6):746-53. Review.

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