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  Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease

Shoeman, R. L., Hartig, R., Hauses, C., & Traub, P. (2002). Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease. Cell Biology International, 26(6), 529-539. doi:10.1006/cbir.2002.0895.

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CellBiolInt_26_2002_529.pdf (Any fulltext), 309KB
 
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 Creators:
Shoeman, Robert L.1, Author           
Hartig, Roland, Author
Hauses, Claudia, Author
Traub, Peter, 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: focal adhesion plaque; HIV-1 protease; vinculin; vimentin; focal adhesion plaque kinase
 Abstract: Focal adhesion plaques were severely affected in human embryonic fibroblasts permeabilized with digitonin and incubated in buffer containing the human immunodeficiency virus type 1 protease (HIV-1 PR). A mutant HIV-1 PR (3271 HIV-1 PR) had no effect on focal adhesion plaques. Similar effects were seen with cells microinjected with either HIV-1 PR or 3271 HIV-1 PR. Immunoblots of the human embryonic fibroblasts demonstrated that a number of focal adhesion plaque proteins were specifically cleaved by HIV-1 PR. These included fimbrin, focal adhesion plaque kinase (FAK), talin, and, to a lesser extent, filamin, spectrin and fibronectin. Proteins detected by antibodies to beta 4 integrin and alpha 3 integrin were also cleaved by the HIV-1 PR. Control experiments demonstrated that the effect and protein cleavages described are due to action of the HIV-1 PR and not to the action of endogenous host cell proteases.

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Language(s): eng - English
 Dates: 2001-11-142002-03-122013-01-022002-06
 Publication Status: Issued
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 Rev. Type: Peer
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Title: Cell Biology International
  Other : Cell Biol. Int.
Source Genre: Journal
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Publ. Info: London, UK : Academic Press
Pages: - Volume / Issue: 26 (6) Sequence Number: - Start / End Page: 529 - 539 Identifier: ISSN: 1065-6995
CoNE: https://pure.mpg.de/cone/journals/resource/954927651824