{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_created":"2024-01-22T08:07:02Z","intvolume":"        29","publisher":"Royal Society of Chemistry","language":[{"iso":"eng"}],"year":"2023","author":[{"full_name":"Wruck, F.","last_name":"Wruck","first_name":"F."},{"orcid":"0000-0001-6406-524X","first_name":"Mario","last_name":"Avellaneda Sarrió","full_name":"Avellaneda Sarrió, Mario","id":"DC4BA84C-56E6-11EA-AD5D-348C3DDC885E"},{"full_name":"Naqvi, M. M.","last_name":"Naqvi","first_name":"M. M."},{"first_name":"E. J.","full_name":"Koers, E. J.","last_name":"Koers"},{"last_name":"Till","full_name":"Till, K.","first_name":"K."},{"full_name":"Gross, L.","last_name":"Gross","first_name":"L."},{"full_name":"Moayed, F.","last_name":"Moayed","first_name":"F."},{"full_name":"Roland, A.","last_name":"Roland","first_name":"A."},{"full_name":"Heling, L. W. H. J.","last_name":"Heling","first_name":"L. W. H. J."},{"first_name":"A.","last_name":"Mashaghi","full_name":"Mashaghi, A."},{"last_name":"Tans","full_name":"Tans, S. J.","first_name":"S. J."}],"publication_status":"published","page":"278-318","day":"01","month":"11","date_updated":"2024-01-23T12:01:53Z","status":"public","department":[{"_id":"MiSi"}],"article_processing_charge":"No","date_published":"2023-11-01T00:00:00Z","title":"Probing Single Chaperone Substrates","quality_controlled":"1","volume":29,"type":"book_chapter","publication_identifier":{"eisbn":["9781839165993"],"isbn":["9781839162824"]},"_id":"14848","citation":{"mla":"Wruck, F., et al. “Probing Single Chaperone Substrates.” <i>Biophysics of Molecular Chaperones</i>, edited by Sebastian Hiller et al., vol. 29, Royal Society of Chemistry, 2023, pp. 278–318, doi:<a href=\"https://doi.org/10.1039/bk9781839165986-00278\">10.1039/bk9781839165986-00278</a>.","ieee":"F. Wruck <i>et al.</i>, “Probing Single Chaperone Substrates,” in <i>Biophysics of Molecular Chaperones</i>, vol. 29, S. Hiller, M. Liu, and L. He, Eds. Royal Society of Chemistry, 2023, pp. 278–318.","short":"F. Wruck, M. Avellaneda Sarrió, M.M. Naqvi, E.J. Koers, K. Till, L. Gross, F. Moayed, A. Roland, L.W.H.J. Heling, A. Mashaghi, S.J. Tans, in:, S. Hiller, M. Liu, L. He (Eds.), Biophysics of Molecular Chaperones, Royal Society of Chemistry, 2023, pp. 278–318.","chicago":"Wruck, F., Mario Avellaneda Sarrió, M. M. Naqvi, E. J. Koers, K. Till, L. Gross, F. Moayed, et al. “Probing Single Chaperone Substrates.” In <i>Biophysics of Molecular Chaperones</i>, edited by Sebastian Hiller, Maili Liu, and Lichun He, 29:278–318. Royal Society of Chemistry, 2023. <a href=\"https://doi.org/10.1039/bk9781839165986-00278\">https://doi.org/10.1039/bk9781839165986-00278</a>.","apa":"Wruck, F., Avellaneda Sarrió, M., Naqvi, M. M., Koers, E. J., Till, K., Gross, L., … Tans, S. J. (2023). Probing Single Chaperone Substrates. In S. Hiller, M. Liu, &#38; L. He (Eds.), <i>Biophysics of Molecular Chaperones</i> (Vol. 29, pp. 278–318). Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/bk9781839165986-00278\">https://doi.org/10.1039/bk9781839165986-00278</a>","ista":"Wruck F, Avellaneda Sarrió M, Naqvi MM, Koers EJ, Till K, Gross L, Moayed F, Roland A, Heling LWHJ, Mashaghi A, Tans SJ. 2023.Probing Single Chaperone Substrates. In: Biophysics of Molecular Chaperones. New Developments in NMR, vol. 29, 278–318.","ama":"Wruck F, Avellaneda Sarrió M, Naqvi MM, et al. Probing Single Chaperone Substrates. In: Hiller S, Liu M, He L, eds. <i>Biophysics of Molecular Chaperones</i>. Vol 29. Royal Society of Chemistry; 2023:278-318. doi:<a href=\"https://doi.org/10.1039/bk9781839165986-00278\">10.1039/bk9781839165986-00278</a>"},"alternative_title":["New Developments in NMR"],"oa_version":"None","editor":[{"first_name":"Sebastian","last_name":"Hiller","full_name":"Hiller, Sebastian"},{"first_name":"Maili","last_name":"Liu","full_name":"Liu, Maili"},{"last_name":"He","full_name":"He, Lichun","first_name":"Lichun"}],"doi":"10.1039/bk9781839165986-00278","abstract":[{"text":"Regulating protein states is considered the core function of chaperones. However, despite their importance to all major cellular processes, the conformational changes that chaperones impart on polypeptide chains are difficult to study directly due to their heterogeneous, dynamic, and multi-step nature. Here, we review recent advances towards this aim using single-molecule manipulation methods, which are rapidly revealing new mechanisms of conformational control and helping to define a different perspective on the chaperone function.","lang":"eng"}],"publication":"Biophysics of Molecular Chaperones"}