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Items: 1 to 20 of 50

1.

Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance.

Jung G, Jones G, Masison DC.

Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9936-41. Epub 2002 Jul 8.

3.

Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions.

Kryndushkin DS, Smirnov VN, Ter-Avanesyan MD, Kushnirov VV.

J Biol Chem. 2002 Jun 28;277(26):23702-8. Epub 2002 Mar 28.

4.

Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes.

Brinker A, Scheufler C, Von Der Mulbe F, Fleckenstein B, Herrmann C, Jung G, Moarefi I, Hartl FU.

J Biol Chem. 2002 May 31;277(22):19265-75. Epub 2002 Mar 4.

5.

Hsp70 chaperone machines.

Mayer MP, Brehmer D, Gässler CS, Bukau B.

Adv Protein Chem. 2001;59:1-44. Review. No abstract available.

PMID:
11868269
6.

HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor.

Hernández MP, Chadli A, Toft DO.

J Biol Chem. 2002 Apr 5;277(14):11873-81. Epub 2002 Jan 23.

7.

Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s.

Pfund C, Huang P, Lopez-Hoyo N, Craig EA.

Mol Biol Cell. 2001 Dec;12(12):3773-82.

8.
9.

Chaperones that cure yeast artificial [PSI+] and their prion-specific effects.

Kushnirov VV, Kryndushkin DS, Boguta M, Smirnov VN, Ter-Avanesyan MD.

Curr Biol. 2000 Nov 16;10(22):1443-6.

10.

A role for cytosolic hsp70 in yeast [PSI(+)] prion propagation and [PSI(+)] as a cellular stress.

Jung G, Jones G, Wegrzyn RD, Masison DC.

Genetics. 2000 Oct;156(2):559-70.

11.
12.

Multistep mechanism of substrate binding determines chaperone activity of Hsp70.

Mayer MP, Schröder H, Rüdiger S, Paal K, Laufen T, Bukau B.

Nat Struct Biol. 2000 Jul;7(7):586-93.

PMID:
10876246
13.

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.

Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I.

Cell. 2000 Apr 14;101(2):199-210.

14.

Structural insights into substrate binding by the molecular chaperone DnaK.

Pellecchia M, Montgomery DL, Stevens SY, Vander Kooi CW, Feng HP, Gierasch LM, Zuiderweg ER.

Nat Struct Biol. 2000 Apr;7(4):298-303.

PMID:
10742174
16.
17.

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones.

Laufen T, Mayer MP, Beisel C, Klostermeier D, Mogk A, Reinstein J, Bukau B.

Proc Natl Acad Sci U S A. 1999 May 11;96(10):5452-7.

18.

Prion domain initiation of amyloid formation in vitro from native Ure2p.

Taylor KL, Cheng N, Williams RW, Steven AC, Wickner RB.

Science. 1999 Feb 26;283(5406):1339-43.

19.

The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments.

Edskes HK, Gray VT, Wickner RB.

Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1498-503.

20.

Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing.

Newnam GP, Wegrzyn RD, Lindquist SL, Chernoff YO.

Mol Cell Biol. 1999 Feb;19(2):1325-33.

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