Publikation:

Trigger factor flexibility

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Gamerdinger_284743.pdf
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2014

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http://nbn-resolving.de/urn:nbn:de:bsz:352-284743
DOI (zitierfähiger Link)
https://doi.org/10.1126/science.1254064
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Biologie: Publikationen
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Published

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Science. 2014, 344(6184), pp. 590-591. ISSN 0036-8075. eISSN 1095-9203. Available under: doi: 10.1126/science.1254064

Zusammenfassung

Molecular chaperones are found in all cells and are essential for maintaining a functional proteome. The main function of chaperones is to promote correct protein folding by protecting non-native proteins from folding along pathways that lead to protein misfolding and aggregation. To fulfill this task, chaperones must recognize a non-native protein, transiently bind to it, and then release it at precisely the right time to allow the substrate to proceed with its folding course. Many but not all chaperones use adenosine 5'-triphosphate (ATP) to control the dynamic substrate binding and release cycle (1). On page 597 of this issue, Saio et al. (2) unravel the structural basis and underlying mechanism of action of the ATP-independent chaperone trigger factor (TF).

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Fachgebiet (DDC)
570 Biowissenschaften, Biologie

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ISO 690GAMERDINGER, Martin, Elke DEUERLING, 2014. Trigger factor flexibility. In: Science. 2014, 344(6184), pp. 590-591. ISSN 0036-8075. eISSN 1095-9203. Available under: doi: 10.1126/science.1254064
BibTex
@article{Gamerdinger2014-05-09Trigg-28474,
  year={2014},
  doi={10.1126/science.1254064},
  title={Trigger factor flexibility},
  number={6184},
  volume={344},
  issn={0036-8075},
  journal={Science},
  pages={590--591},
  author={Gamerdinger, Martin and Deuerling, Elke}
}
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