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Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question.
Dougan DA, Mogk A, Bukau B. Dougan DA, et al. Cell Mol Life Sci. 2002 Oct;59(10):1607-16. doi: 10.1007/pl00012487. Cell Mol Life Sci. 2002. PMID: 12475170 Review.
In Escherichia coli protein quality control is carried out by a protein network, comprising chaperones and proteases. Central to this network are two protein families, the AAA+ and the Hsp70 family. ...In contrast to ClpB, many AAA+ proteins associate with a peptida …
In Escherichia coli protein quality control is carried out by a protein network, comprising chaperones and proteases. Central to this …
The ftsH gene of Bacillus subtilis is involved in major cellular processes such as sporulation, stress adaptation and secretion.
Deuerling E, Mogk A, Richter C, Purucker M, Schumann W. Deuerling E, et al. Mol Microbiol. 1997 Mar;23(5):921-33. doi: 10.1046/j.1365-2958.1997.2721636.x. Mol Microbiol. 1997. PMID: 9076729
The ftsH gene of Bacillus subtilis has been identified as a general stress gene which is transiently induced after thermal or osmotic upshift. ...Most of these results can be explained by the failure to synthesize appropriate amounts of Spo0A protein in the ftsH null mutan …
The ftsH gene of Bacillus subtilis has been identified as a general stress gene which is transiently induced after thermal or osmotic …
The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis.
Mogk A, Homuth G, Scholz C, Kim L, Schmid FX, Schumann W. Mogk A, et al. EMBO J. 1997 Aug 1;16(15):4579-90. doi: 10.1093/emboj/16.15.4579. EMBO J. 1997. PMID: 9303302 Free PMC article.
Upon removal of urea, HrcA had a strong tendency to aggregate, but aggregation could be suppressed significantly by the addition of GroEL. ...These results suggest that the GroE chaperonin machine modulates the activity of the HrcA repressor and therefore point to a
Upon removal of urea, HrcA had a strong tendency to aggregate, but aggregation could be suppressed significantly by the addition of G …
Nonnative proteins induce expression of the Bacillus subtilis CIRCE regulon.
Mogk A, Völker A, Engelmann S, Hecker M, Schumann W, Völker U. Mogk A, et al. J Bacteriol. 1998 Jun;180(11):2895-900. doi: 10.1128/JB.180.11.2895-2900.1998. J Bacteriol. 1998. PMID: 9603878 Free PMC article.
Introduction of the hrcA gene and a transcriptional fusion under the control of the CIRCE operator into Escherichia coli allowed induction of this fusion by heat shock, ethanol stress, and overproduction of GroESL substrates. ...
Introduction of the hrcA gene and a transcriptional fusion under the control of the CIRCE operator into Escherichia coli allowed indu …
Construction and analysis of hybrid Escherichia coli-Bacillus subtilis dnaK genes.
Mogk A, Bukau B, Lutz R, Schumann W. Mogk A, et al. J Bacteriol. 1999 Mar;181(6):1971-4. doi: 10.1128/JB.181.6.1971-1974.1999. J Bacteriol. 1999. PMID: 10074100 Free PMC article.
The highly conserved DnaK chaperones consist of an N-terminal ATPase domain, a central substrate-binding domain, and a C-terminal domain whose function is not known. ...The ATPase domain and the substrate-binding domain form a species-specific functional unit …
The highly conserved DnaK chaperones consist of an N-terminal ATPase domain, a central substrate-binding domain, and a C-termi …
Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones.
Laufen T, Mayer MP, Beisel C, Klostermeier D, Mogk A, Reinstein J, Bukau B. Laufen T, et al. Proc Natl Acad Sci U S A. 1999 May 11;96(10):5452-7. doi: 10.1073/pnas.96.10.5452. Proc Natl Acad Sci U S A. 1999. PMID: 10318904 Free PMC article.
Hsp70 chaperones assist a large variety of protein folding processes within the entire lifespan of proteins. Central to these activities is the regulation of Hsp70 by DnaJ cochaperones. DnaJ stimulates Hsp70 to hydrolyze ATP, a key step that closes its substrate-bin …
Hsp70 chaperones assist a large variety of protein folding processes within the entire lifespan of proteins. Central to these activit …
The Bacillus subtilis htpG gene is not involved in thermal stress management.
Versteeg S, Mogk A, Schumann W. Versteeg S, et al. Mol Gen Genet. 1999 Apr;261(3):582-8. doi: 10.1007/s004380051004. Mol Gen Genet. 1999. PMID: 10323241
In the second case, the htpG gene was fused to a xylose-dependent promoter, allowing expression of the gene to be controlled. ...It could be shown that the HtpG protein does not act as a cellular thermometer in B. subtilis....
In the second case, the htpG gene was fused to a xylose-dependent promoter, allowing expression of the gene to be controlled. ...It c …
Role of region C in regulation of the heat shock gene-specific sigma factor of Escherichia coli, sigma32.
Arsène F, Tomoyasu T, Mogk A, Schirra C, Schulze-Specking A, Bukau B. Arsène F, et al. J Bacteriol. 1999 Jun;181(11):3552-61. doi: 10.1128/JB.181.11.3552-3561.1999. J Bacteriol. 1999. PMID: 10348869 Free PMC article.
Region C is thus a prime candidate for mediating stress control of sigma32, a hypothesis that we tested in the present study. A peptide comprising the central DnaK binding site was an excellent substrate for FtsH, while a peptide comprising the periphe …
Region C is thus a prime candidate for mediating stress control of sigma32, a hypothesis that we tested in the present study. …
Post-transcriptional regulation of the Bacillus subtilis dnaK operon.
Homuth G, Mogk A, Schumann W. Homuth G, et al. Mol Microbiol. 1999 Jun;32(6):1183-97. doi: 10.1046/j.1365-2958.1999.01428.x. Mol Microbiol. 1999. PMID: 10383760
A crucial factor determining the low stability of two transcripts is the presence of the CIRCE element at their 5' ends. We demonstrate that CIRCE leads to the destabilization of mRNAs, but only if it is located in the immediate vicinity of a Shine-Dalgarno sequence
A crucial factor determining the low stability of two transcripts is the presence of the CIRCE element at their 5' ends. We demonstra
Trigger factor and DnaK cooperate in folding of newly synthesized proteins.
Deuerling E, Schulze-Specking A, Tomoyasu T, Mogk A, Bukau B. Deuerling E, et al. Nature. 1999 Aug 12;400(6745):693-6. doi: 10.1038/23301. Nature. 1999. PMID: 10458167
These findings show in vivo activity for a ribosome-associated chaperone, trigger factor, in general protein folding, and functional cooperation of this protein with a cytosolic Hsp70. Trigger factor and DnaK cooperate to promote proper folding of a variety o …
These findings show in vivo activity for a ribosome-associated chaperone, trigger factor, in general protein folding, and functional …
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