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A deubiquitinating enzyme encoded by HSV-1 belongs to a family of cysteine proteases that is conserved across the family Herpesviridae.

Abstract:

We have discovered a ubiquitin (Ub)-specific cysteine protease encoded within the N-terminal approximately 500 residues of the UL36 gene product, the largest (3164 aa) tegument protein of herpes simplex virus 1 (HSV-1). Enzymatic activity of this fragment, UL36USP, is detectable only after cleavage of UL36USP from full-length UL36 and occurs late during viral replication. UL36USP bears no homology to known deubiquitinating enzymes (DUBs) or Ub binding proteins. Sequence alignment of the large...

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Publication status:
Published

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Authors


Kattenhorn, LM More by this author
Korbel, GA More by this author
Kessler, BM More by this author
Spooner, E More by this author
Ploegh, HL More by this author
Journal:
Molecular cell
Volume:
19
Issue:
4
Pages:
547-557
Publication date:
2005-08-05
DOI:
EISSN:
1097-4164
ISSN:
1097-2765
URN:
uuid:119f09de-1cd9-4bd9-9653-2c340cf1f40c
Source identifiers:
19410
Local pid:
pubs:19410

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