Proteolytic activity of human cytomegalovirus UL80 protease cleavage site mutants.
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Assembly of herpes simplex virus capsids using the human cytomegalovirus scaffold protein: critical role of the C terminusAssembly of the herpes simplex virus capsid: requirement for the carboxyl-terminal twenty-five amino acids of the proteins encoded by the UL26 and UL26.5 genesSpecific inhibition of human cytomegalovirus glycoprotein B-mediated fusion by a novel thiourea small molecule.Cleavage of human cytomegalovirus protease pUL80a at internal and cryptic sites is not essential but enhances infectivity.Cytomegalovirus assemblin (pUL80a): cleavage at internal site not essential for virus growth; proteinase absent from virions.Enzymatic activities of human cytomegalovirus maturational protease assemblin and its precursor (pPR, pUL80a) are comparable: [corrected] maximal activity of pPR requires self-interaction through its scaffolding domain.Tetracycline repressor-regulated gene repression in recombinant human cytomegalovirusHuman cytomegalovirus US2 destabilizes major histocompatibility complex class I heavy chains.Characterization of a soluble stable human cytomegalovirus protease and inhibition by M-site peptide mimics.Cytomegalovirus protein substrates are not cleaved by the herpes simplex virus type 1 proteinase.Human cytomegalovirus proteinase: candidate glutamic acid identified as third member of putative active-site triad.Multiple independent loci within the human cytomegalovirus unique short region down-regulate expression of major histocompatibility complex class I heavy chains.Cytomegalovirus assemblin: the amino and carboxyl domains of the proteinase form active enzyme when separately cloned and coexpressed in eukaryotic cells.Independently cloned halves of cytomegalovirus assemblin, An and Ac, can restore proteolytic activity to assemblin mutants by intermolecular complementation.Expression and characterization of recombinant murine cytomegalovirus protease.An acidic cluster of human cytomegalovirus UL99 tegument protein is required for trafficking and function.Chemokine sequestration by viral chemoreceptors as a novel viral escape strategy: withdrawal of chemokines from the environment of cytomegalovirus-infected cells.Sequential autoprocessing of Marek's disease herpesvirus protease differs from that of other herpesvirusesCytomegalovirus capsid protease: biological substrates are cleaved more efficiently by full-length enzyme (pUL80a) than by the catalytic domain (assemblin)
P2860
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P2860
Proteolytic activity of human cytomegalovirus UL80 protease cleavage site mutants.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Proteolytic activity of human cytomegalovirus UL80 protease cleavage site mutants.
@en
type
label
Proteolytic activity of human cytomegalovirus UL80 protease cleavage site mutants.
@en
prefLabel
Proteolytic activity of human cytomegalovirus UL80 protease cleavage site mutants.
@en
P2093
P2860
P1433
P1476
Proteolytic activity of human cytomegalovirus UL80 protease cleavage site mutants.
@en
P2093
Bebernitz GA
Johnston SH
Muzithras VP
P2860
P304
P407
P577
1994-06-01T00:00:00Z