---
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@'
...