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Cited by 425

The DOI matches its Crossref record; 82 of the 82 references it cites were found in a registry or an index.

Viral Late Domains

Open access
Freed, Eric O.·2002·Journal of Virology

Abstract

Domains have been identified in the Gag proteins of a number of retroviruses, and in the matrix proteins of the rhabdoviruses and filoviruses, that play a critical role in the pinching off of virus particles from the plasma membrane. These sequences are collectively termed late or L domains to reflect their function late in the virus budding process. One of the intriguing features of these L domains is that they all contain highly conserved motifs known to mediate protein-protein interactions between cellular proteins. Three classes of motifs have been defined in viral L domains: PTAP, PPXY, and YXXL. In each case, the integrity of these motifs appears to be essential for L domain activity, suggesting that L domains function by interacting with a host factor(s). This minireview summarizes the present state of our knowledge concerning viral L domain function and describes recent tantalizing clues regarding the identity of the cellular partners with which L domains interact.

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Crossref · 10.1128/jvi.76.10.4679-4687.2002

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Metadata

Authors
Freed, E. O.
Venue
Journal of Virology
Published
2002-05-15
Volume
76
Issue
10
Pages
4679-4687
ISSN
  • 0022-538X (ISSN-L)
  • 1098-5514
OpenAlex
W2009465113
Cited by
425
References
82
FWCI
13.09
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Viral Late Domains. https://app.cochat.ai/papers/10.1128/jvi.76.10.4679-4687.2002
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Freed, E. O. (2002). Viral Late Domains. Journal of Virology. https://doi.org/10.1128/jvi.76.10.4679-4687.2002

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