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The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins.
Parsell DA, Lindquist S. Parsell DA, et al. Annu Rev Genet. 1993;27:437-96. doi: 10.1146/ Annu Rev Genet. 1993. PMID: 8122909 Review. No abstract available.
Protein disaggregation mediated by heat-shock protein Hsp104.
Parsell DA, Kowal AS, Singer MA, Lindquist S. Parsell DA, et al. Nature. 1994 Dec 1;372(6505):475-8. doi: 10.1038/372475a0. Nature. 1994. PMID: 7984243
Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation.
Parsell DA, Sauer RT. Parsell DA, et al. Genes Dev. 1989 Aug;3(8):1226-32. doi: 10.1101/gad.3.8.1226. Genes Dev. 1989. PMID: 2676724
Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes.
Parsell DA, Kowal AS, Lindquist S. Parsell DA, et al. J Biol Chem. 1994 Feb 11;269(6):4480-7. J Biol Chem. 1994. PMID: 8308017 Free article.
The ATPase activity of Hsp104, effects of environmental conditions and mutations.
Schirmer EC, Queitsch C, Kowal AS, Parsell DA, Lindquist S. Schirmer EC, et al. Among authors: parsell da. J Biol Chem. 1998 Jun 19;273(25):15546-52. doi: 10.1074/jbc.273.25.15546. J Biol Chem. 1998. PMID: 9624144 Free article.
Genetic evidence for a functional relationship between Hsp104 and Hsp70.
Sanchez Y, Parsell DA, Taulien J, Vogel JL, Craig EA, Lindquist S. Sanchez Y, et al. Among authors: parsell da. J Bacteriol. 1993 Oct;175(20):6484-91. doi: 10.1128/jb.175.20.6484-6491.1993. J Bacteriol. 1993. PMID: 8407824 Free PMC article.
The role of heat-shock proteins in thermotolerance.
Parsell DA, Taulien J, Lindquist S. Parsell DA, et al. Philos Trans R Soc Lond B Biol Sci. 1993 Mar 29;339(1289):279-85; discussion 285-6. doi: 10.1098/rstb.1993.0026. Philos Trans R Soc Lond B Biol Sci. 1993. PMID: 8098532 Review.
Hsp104 is a highly conserved protein with two essential nucleotide-binding sites.
Parsell DA, Sanchez Y, Stitzel JD, Lindquist S. Parsell DA, et al. Nature. 1991 Sep 19;353(6341):270-3. doi: 10.1038/353270a0. Nature. 1991. PMID: 1896074
The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli.
Parsell DA, Sauer RT. Parsell DA, et al. J Biol Chem. 1989 May 5;264(13):7590-5. J Biol Chem. 1989. PMID: 2651442
An essential proline in lambda repressor is required for resistance to intracellular proteolysis.
Reidhaar-Olson JF, Parsell DA, Sauer RT. Reidhaar-Olson JF, et al. Among authors: parsell da. Biochemistry. 1990 Aug 21;29(33):7563-71. doi: 10.1021/bi00485a004. Biochemistry. 1990. PMID: 2148681
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