--- res: bibo_abstract: - "Significance\r\n The hierarchical assembly pathway of the cytoskeletal protein vimentin may be responsible for the astonishing mechanical properties of the emerging filaments, such as high flexibility and extensibility, and thus play a key role in cellular mechanics. A two-step assembly mechanism, involving a lateral and a subsequent elongational step, has been established; however, the elongational step could not be followed in solution. Here, we show direct in situ observation and modeling of the elongation reaction of the filaments on the relevant length and time scales, using time-resolved, multiangle static and dynamic light scattering. We thus achieve sufficient spatio-temporal resolution without the need of labeling, staining, or adsorption to substrates.@eng" bibo_authorlist: - foaf_Person: foaf_givenName: Carlos G. foaf_name: Lopez, Carlos G. foaf_surname: Lopez - foaf_Person: foaf_givenName: Oliva foaf_name: Saldanha, Oliva foaf_surname: Saldanha - foaf_Person: foaf_givenName: Klaus foaf_name: Huber, Klaus foaf_surname: Huber foaf_workInfoHomepage: http://www.librecat.org/personId=237 - foaf_Person: foaf_givenName: Sarah foaf_name: Köster, Sarah foaf_surname: Köster bibo_doi: 10.1073/pnas.1606372113 bibo_issue: '40' bibo_volume: 113 dct_date: 2016^xs_gYear dct_isPartOf: - http://id.crossref.org/issn/0027-8424 - http://id.crossref.org/issn/1091-6490 dct_language: eng dct_publisher: Proceedings of the National Academy of Sciences@ dct_subject: - Multidisciplinary dct_title: 'Lateral association and elongation of vimentin intermediate filament proteins: A time-resolved light-scattering study@' ...