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  Cleavage of vimentin by different retroviral proteases

Snášel, J., Shoeman, R. L., Horejší, M., Hrušková−Heidingsfeldová, O., Sedlácek, J., Ruml, T., et al. (2000). Cleavage of vimentin by different retroviral proteases. Archives of Biochemistry and Biophysics, 377(2), 241-245. doi:10.1006/abbi.2000.1776.

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ArchBiochemBiophys_377_2000_241.pdf (Any fulltext), 75KB
 
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 Creators:
Snášel, Jan, Author
Shoeman, Robert L.1, Author           
Horejší, Magda, Author
Hrušková−Heidingsfeldová, Olga, Author
Sedlácek, Juraj, Author
Ruml, Tomáš, Author
Pichová, Iva, Author
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: mouse vimentin; HIV-1 protease; HIV-2 protease; MAV proteases; BLV protease; M-PMV protease
 Abstract: Proteases (PRs) of retroviruses cleave viral polyproteins into their mature structural proteins and replication enzymes. Besides this essential role in the replication cycle of retroviruses, PRs also cleave a variety of host cell proteins. We have analyzed the in vitro cleavage of mouse vimentin by proteases of human immunodeficiency virus type 1 (HIV-1) and type 2 (HIV-2), bovine leukemia virus (BLV), Mason-Pfizer monkey virus (M-PMV), myeloblastosis-associated virus (MAV), and two active-site mutants of MAV PR. Retroviral proteases display significant differences in specificity requirements. Here, we show a comparison of substrate specificities of several retroviral proteases on vimentin as a substrate. Vimentin was cleaved by all the proteases at different sites and with different rates. The results show that the physiologically important cellular protein vimentin can be degraded by different retroviral proteases.

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Language(s): eng - English
 Dates: 1999-08-112000-01-242002-05-252000-05-15
 Publication Status: Issued
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Archives of Biochemistry and Biophysics
Source Genre: Journal
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Publ. Info: New York : Academic Press
Pages: - Volume / Issue: 377 (2) Sequence Number: - Start / End Page: 241 - 245 Identifier: ISSN: 0003-9861
CoNE: https://pure.mpg.de/cone/journals/resource/991042745826956