Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II: candidate for a Tat cofactor

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Veröffentlicht in:	Journal of Virology 1995-03, Vol.69 (3), p.1612-1620
Hauptverfasser:	Herrmann, C H, Rice, A P
Format:	Artikel
Sprache:	eng
Schlagworte:	AIDS/HIV Cell Nucleus - enzymology Dichlororibofuranosylbenzimidazole - pharmacology Gene Expression Regulation, Viral Gene Products, tat - metabolism HeLa Cells - enzymology HIV-1 - metabolism HIV-2 - metabolism human immunodeficiency virus 1 human immunodeficiency virus 2 Humans Phosphorylation Positive Transcriptional Elongation Factor B Protein Binding Protein-Serine-Threonine Kinases - antagonists & inhibitors Protein-Serine-Threonine Kinases - metabolism RNA Polymerase II - metabolism Signal Transduction tat Gene Products, Human Immunodeficiency Virus Transcription, Genetic
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Zusammenfassung:	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.69.3.1612-1620.1995