Cytomegalovirus Capsid Protease: Biological Substrates Are Cleaved More Efficiently by Full-Length Enzyme (pUL80a) than by the Catalytic Domain (Assemblin)

Cytomegalovirus Capsid Protease: Biological Substrates Are Cleaved More Efficiently by Full-Length Enzyme (pUL80a) than by the Catalytic Domain (Assemblin)

Author's Correction ( vol. 85 , p. 7951 ) Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribe...

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Veröffentlicht in:Journal of Virology 2011-04, Vol.85 (7), p.3526-3534
Hauptverfasser: FERNANDES, Steve M, BRIGNOLE, Edward J, GIBSON, Wade
Format: Artikel
Sprache:eng
Schlagworte:
Biological and medical sciences
Catalytic Domain
Chromatography, Affinity - methods
Cytomegalovirus - enzymology
Endopeptidases - isolation & purification
Endopeptidases - metabolism
Fundamental and applied biological sciences. Psychology
Human cytomegalovirus
Humans
Microbiology
Miscellaneous
Serine Endopeptidases - isolation & purification
Serine Endopeptidases - metabolism
Structure and Assembly
Viral Proteins - isolation & purification
Viral Proteins - metabolism
Virology
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Zusammenfassung:Author's Correction ( vol. 85 , p. 7951 ) Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
ISSN:0022-538X
1098-5514
DOI:10.1128/JVI.02663-10