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  Intermediate filament assembly and stability in vitro: effect and implications of the removal of head and tail domains of vimentin by the human immunodeficiency virus type 1 protease

Shoeman, R. L., Mothes, E., Kesselmeier, C., & Traub, P. (1990). Intermediate filament assembly and stability in vitro: effect and implications of the removal of head and tail domains of vimentin by the human immunodeficiency virus type 1 protease. Cell Biology International Reports, 14(7), 583-594. doi:10.1016/0309-1651(90)90038-Z.

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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-0000-7853-C Versions-Permalink: https://hdl.handle.net/21.11116/0000-0000-7854-B
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CellBiolIntRep_14_1990_583.pdf (beliebiger Volltext), 3MB
 
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https://www.sciencedirect.com/science/article/pii/030916519090038Z/pdf?md5=94012bce20a176035f4a4186f2e89c9b&pid=1-s2.0-030916519090038Z-main.pdf (beliebiger Volltext)
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https://doi.org/10.1016/0309-1651(90)90038-Z (beliebiger Volltext)
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 Urheber:
Shoeman, Robert L.1, 2, 3, Autor           
Mothes, Elfriede, Autor
Kesselmeier, Cornelia, Autor
Traub, Peter, Autor
Affiliations:
1Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society, ou_1497692              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
3Analytical Protein Biochemistry, Max Planck Institute for Medical Research, Max Planck Society, ou_1497690              

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 Zusammenfassung: The intermediate filament subunit protein vimentin is efficiently cleaved in vitro by purified human immunodeficiency virus type 1 protease. Immunological data confirm that identical sites are cleaved when vimentin is polymerized into filaments or occurs as protofilaments. The primary cleavage gives rise to a molecule lacking most of the tail domain and which not only remains in preformed filaments, but is also capable of polymerizing into essentially normal 10 nm filaments. However, these filaments show a propensity to form large lateral aggregates. The three secondary cleavage products of vimentin additionally lack portions of the head domain, are almost quantitatively (greater than 95%) released from preformed filaments and are not capable of forming filaments de novo. These results extend the limits of the head and tail domains of vimentin that play a role in filament formation and stability.

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Sprache(n): eng - English
 Datum: 1990-03-241990-04-222004-12-021990-07
 Publikationsstatus: Erschienen
 Seiten: 12
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1016/0309-1651(90)90038-Z
URI: https://www.ncbi.nlm.nih.gov/pubmed/2203542
URI: https://www.ncbi.nlm.nih.gov/m/pubmed/2203542/
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Titel: Cell Biology International Reports
  Alternativer Titel : Cell Biol. Int. Rep.
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: Amsterdam [u.a. : Elsevier
Seiten: - Band / Heft: 14 (7) Artikelnummer: - Start- / Endseite: 583 - 594 Identifikator: ISSN: 0309-1651