Poly(ADP-ribose) Polymerase-1 Is a Negative Regulator of HIV-1 Transcription through Competitive Binding to TAR RNA with Tat·Positive Transcription Elongation Factor b (p-TEFb) Complex
Marianne Parent,Tetsu M.C. Yung,Ann Rancourt,Erick L.Y. Ho,Stéphane Vispé,Fumihiko Suzuki-Matsuda,Aki Uehara,Tadashi Wada,Hiroshi Handa,Masahiko S. Satoh +9 more
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TLDR
The results suggest that PARP-1 acts as a negative regulator of HIV-1 transcription through competitive binding with Tat or the Tat·P-TEFb complex to TAR RNA.About:
This article is published in Journal of Biological Chemistry.The article was published on 2005-01-07 and is currently open access. It has received 34 citations till now. The article focuses on the topics: General transcription factor & RNA polymerase II.read more
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Survey of the year 2003 commercial optical biosensor literature
Rebecca L. Rich,David G. Myszka +1 more
TL;DR: In this overview, 13 papers that should be on everyone's ‘must read’ list for 2003 are spotlighted and examples of how to identify and interpret high‐quality biosensor data are provided.
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The expanding field of poly(ADP‐ribosyl)ation reactions
TL;DR: The mechanisms controlling the biosynthesis of this complex macromolecule and some of its main biological functions are reviewed, with an emphasis on the most recent advances and hypotheses that have developed in this rapidly growing field.
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Reactivation of latent HIV-1 by inhibition of BRD4
Jian Zhu,Gaurav D. Gaiha,Sinu P. John,Thomas Pertel,Christopher R. Chin,Geng Gao,Hongjing Qu,Bruce D. Walker,Bruce D. Walker,Stephen J. Elledge,Stephen J. Elledge,Abraham L. Brass +11 more
TL;DR: In multiple instances, JQ1, when used in combination with the NF-κB activators Prostratin or PHA, enhanced the in vitro reactivation of latent HIV-1 in primary T cells and suggests that combinatorial therapies that activate HDFs and antagonize HIV-2 competitive factors may be useful for curing HIV- 1 infection.
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Identification of Cellular Interaction Partners of the Influenza Virus Ribonucleoprotein Complex and Polymerase Complex Using Proteomic-Based Approaches
Daniel C. Mayer,Kaaweh Molawi,Luis Martinez-Sobrido,Alexander Ghanem,Stefan Thomas,Sacha Baginsky,Jonas Grossmann,§ and Adolfo García-Sastre,Martin Schwemmle +8 more
TL;DR: Proteomics-based approaches represent powerful tools to identify novel vRNP-associated cellular factors for further characterization and revealed that NPM is recruited to sites of viral transcription and replication in infected cells, indicating its role in viral RNA synthesis.
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The impact of PARPs and ADP-ribosylation on inflammation and host–pathogen interactions
Anthony R. Fehr,Sasha A Singh,Catherine M Kerr,Shin Mukai,Hideyuki Higashi,Masanori Aikawa,Masanori Aikawa +6 more
TL;DR: The current understanding of the mechanisms by which PARPs promote or suppress proinflammatory activation of macrophages, and various roles PARPs play in virus infections are given.
References
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DNA topoisomerases: structure, function, and mechanism.
TL;DR: Surprisingly, despite little or no sequence homology, both type IA and type IIA topoisomerases from prokaryotes and the typeIIA enzymes from eukaryotes share structural folds that appear to reflect functional motifs within critical regions of the enzymes.
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Poly(adp-ribosyl)ation reactions in the regulation of nuclear functions
TL;DR: The total dependence of poly(ADP-ribose) synthesis on DNA strand breaks strongly suggests that this post-translational modification is involved in the metabolism of nucleic acids, and the presence of PARP in these multiprotein complexes clearly supports an important role for poly(ADE-ribosyl)ation reactions in DNA transactions.
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A Novel CDK9-Associated C-Type Cyclin Interacts Directly with HIV-1 Tat and Mediates Its High-Affinity, Loop-Specific Binding to TAR RNA
Ping Wei,Mitchell E Garber,Mitchell E Garber,Shi-Min Fang,Wolfgang H. Fischer,Katherine A. Jones +5 more
TL;DR: It is proposed that Tat directs cyclin T-CDK9 to RNAPII through cooperative binding to TAR RNA, and confers a requirement for sequences in the loop of TAR that are not recognized by Tat alone.
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NELF, a Multisubunit Complex Containing RD, Cooperates with DSIF to Repress RNA Polymerase II Elongation
Yuki Yamaguchi,Toshiyuki Takagi,Tadashi Wada,Keiichi Yano,Akiko Furuya,Seiji Sugimoto,Jun Hasegawa,Hiroshi Handa +7 more
TL;DR: The identification and purification from HeLa nuclear extract of a third protein factor required for DRB-sensitive transcription, termed negative elongation factor (NELF), cooperates with DSIF and strongly represses pol II elongation.
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Dsif, a novel transcription elongation factor that regulates rna polymerase ii processivity, is composed of human spt4 and spt5 homologs
Tadashi Wada,Toshiyuki Takagi,Yuki Yamaguchi,Anwarul Ferdous,Takeshi Imai,Susumu Hirose,Seiji Sugimoto,Keiichi Yano,Grant A. Hartzog,Fred Winston,Stephen Buratowski,Hiroshi Handa +11 more
TL;DR: The combination of biochemical studies on DSIF and genetic analysis of Spt4 and Spt5 in yeast indicates that DSIF associates with RNA Pol II and regulates its processivity in vitro and in vivo.