Crystal structure of HIV-1 Tat complexed with human P-TEFb

[20] Processing of X-ray diffraction data collected in oscillation mode

Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475 · see citing works

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,720 · see citing works

WebLogo: A Sequence Logo Generator: Figure 1Preprint

Crooks, G. E., Hon, G. C., Chandonia, J., & Brenner, S. E. (2004) · Genome Research · doi:10.1101/gr.849004 · Cited by 12,433 · see citing works

Controlling the elongation phase of transcription with P-TEFb

Peterlin, B. M., & Price, D. H. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.014 · Cited by 1,144 · see citing works

Crystal structure of the p27Kip1 cyclin-dependent-kinase inibitor bound to the cyclin A–Cdk2 complex

Russo, A. A., Jeffrey, P. D., Patten, A. K., Massagué, J., & Pavletich, N. P. (1996) · Nature · doi:10.1038/382325a0 · Cited by 899 · see citing works

Mechanisms of cyclin-dependent kinase regulation: structures of cdks, their cyclin activators, and cip and INK4 inhibitors

Pavletich, N. P. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2640 · Cited by 746 · see citing works

Transcription elongation factor P-TEFb is required for HIV-1 Tat transactivation in vitroPreprint

Zhu, Y., Peery, T., Peng, J., Ramanathan, Y., Marshall, N. F., Marshall, T. K., Amendt, B. A., Mathews, M. B., & Price, D. H. (1997) · Genes & Development · doi:10.1101/gad.11.20.2622 · Cited by 700 · see citing works

Control of RNA Polymerase II Elongation Potential by a Novel Carboxyl-terminal Domain Kinase

Marshall, N. F., Peng, J., Xie, Z., & Price, D. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.43.27176 · Cited by 662 · see citing works

Global and regional distribution of HIV-1 genetic subtypes and recombinants in 2004

Hemelaar, J., Gouws, E., Ghys, P. D., & Osmanov, S. (2006) · AIDS · doi:10.1097/01.aids.0000247564.73009.bc · Cited by 627 · see citing works

Flavopiridol Inactivates P-TEFb and Blocks Most RNA Polymerase II Transcription in Vivo

Chao, S., & Price, D. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102306200 · Cited by 623 · see citing works

P-TEFb kinase is required for HIV Tat transcriptional activation in vivo and in vitroPreprint

Mancebo, H. S. Y., Lee, G., Flygare, J. A., Tomassini, J. E., Luu, P., Zhu, Y., Peng, J., Blau, C., Hazuda, D. J., Price, D. H., et al. (1997) · Genes & Development · doi:10.1101/gad.11.20.2633 · Cited by 546 · see citing works

Identification of multiple cyclin subunits of human P-TEFb.Preprint

Peng, J.-M., Zhu, Y., Milton, J. T., & Price, D. (1998) · Genes & Development · doi:10.1101/gad.12.5.755 · Cited by 531 · see citing works

Inhibition of P-TEFb (CDK9/Cyclin T) Kinase and RNA Polymerase II Transcription by the Coordinated Actions of HEXIM1 and 7SK snRNA

Yik, J. H. N., Chen, R., Nishimura, R., Jennings, J. L., Link, A. J., & Zhou, Q. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00388-5 · Cited by 464 · see citing works

The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 proteinPreprint

Garber, M. E., Wei, P., KewalRamani, V. N., Mayall, T. P., Herrmann, C. H., Rice, A. P., Littman, D. R., & Jones, K. A. (1998) · Genes & Development · doi:10.1101/gad.12.22.3512 · Cited by 430 · see citing works

Structural and functional characterization of human immunodeficiency virus tat protein

Ruben, S. M., Perkins, A., Purcell, R. D., Joung, K., Sia, R. A. L., Burghoff, R. L., Haseltine, W. A., & Rosen, C. A. (1989) · Journal of Virology · doi:10.1128/jvi.63.1.1-8.1989 · Cited by 424 · see citing works

Multifaceted Activities of the HIV-1 Transactivator of Transcription, Tat

Jeang, K., Xiao, H., & Rich, E. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.28837 · Cited by 416 · see citing works

Structural basis for transcription elongation by bacterial RNA polymerase

Vassylyev, D. G., Vassylyeva, M. N., Perederina, A. A., Tahirov, T. H., & Artsimovitch, I. (2007) · Nature · doi:10.1038/nature05932 · Cited by 409 · see citing works

The structure of P‐TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation

Baumli, S., Lolli, G., Lowe, E. D., Troiani, S., Rusconi, L., Bullock, A. N., Debreczeni, J. E., Knapp, S., & Johnson, L. N. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.121 · Cited by 357 · see citing works

Tat Modifies the Activity of CDK9 To Phosphorylate Serine 5 of the RNA Polymerase II Carboxyl-Terminal Domain during Human Immunodeficiency Virus Type 1 Transcription

Zhou, M., Halanski, M. A., Radonovich, M. F., Kashanchi, F., Peng, J., Price, D. H., & Brady, J. N. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.14.5077-5086.2000 · Cited by 261 · see citing works

Recruitment of a protein complex containing Tat and cyclin T1 to TAR governs the species specificity of HIV‐1 Tat

Bieniasz, P. D., Grdina, T. A., Bogerd, H. P., & Cullen, B. R. (1998) · The EMBO Journal · doi:10.1093/emboj/17.23.7056 · Cited by 260 · see citing works

The Yin and Yang of P-TEFb Regulation: Implications for Human Immunodeficiency Virus Gene Expression and Global Control of Cell Growth and Differentiation

Zhou, Q., & Yik, J. H. N. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00011-06 · Cited by 260 · see citing works

Multiple functional domains of Tat, thetrans-activator of HIV-1, defined by mutational analysis

Kuppuswamy, M. N., Subramanian, T., Srinivasan, A., & Chinnadurai, G. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.9.3551 · Cited by 252 · see citing works

MAQ1 and 7SK RNA Interact with CDK9/Cyclin T Complexes in a Transcription-Dependent Manner

Michels, A. A., Nguyen, V. T., Fraldi, A., Labas, V., Edwards, M., Bonnet, F., Lania, L., & Bensaude, O. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.14.4859-4869.2003 · Cited by 230 · see citing works

Cyclin K Functions as a CDK9 Regulatory Subunit and Participates in RNA Polymerase II Transcription

Fu, T.-J., Peng, J., Lee, G., Price, D. H., & Flores, O. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.49.34527 · Cited by 224 · see citing works

Analysis of the Large Inactive P-TEFb Complex Indicates That It Contains One 7SK Molecule, a Dimer of HEXIM1 or HEXIM2, and Two P-TEFb Molecules Containing Cdk9 Phosphorylated at Threonine 186

Li, Q., Price, J. P., Byers, S. A., Cheng, D., Peng, J., & Price, D. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502712200 · Cited by 215 · see citing works

Specific versus non-specific contacts in protein crystals

Janin, J. (1997) · Nature Structural Biology · doi:10.1038/nsb1297-973 · Cited by 206 · see citing works

Tat competes with HEXIM1 to increase the active pool of P-TEFb for HIV-1 transcription

Barborič, M., Yik, J. H. N., Czudnochowski, N., Yang, Z., Chen, R., Contreras, X., Geyer, M., Peterlin, B. M., & Zhou, Q. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm063 · Cited by 188 · see citing works

The Remarkable Frequency of Human Immunodeficiency Virus Type 1 Genetic Recombination

Onafuwa-Nuga, A., & Telesnitsky, A. (2009) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00012-09 · Cited by 174 · see citing works

Phosphorylated Positive Transcription Elongation Factor b (P-TEFb) Is Tagged for Inhibition through Association with 7SK snRNA

Chen, R., Yang, Z., & Zhou, Q. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310044200 · Cited by 166 · see citing works

The Ability of Positive Transcription Elongation Factor b To Transactivate Human Immunodeficiency Virus Transcription Depends on a Functional Kinase Domain, Cyclin T1, and Tat

Fujinaga, K., Cujec, T. P., Peng, J., Garriga, J., Price, D. H., Graña, X., & Peterlin, B. M. (1998) · Journal of Virology · doi:10.1128/jvi.72.9.7154-7159.1998 · Cited by 165 · see citing works

Manipulation of P-TEFb control machinery by HIV: recruitment of P-TEFb from the large form by Tat and binding of HEXIM1 to TAR

Sedore, S. C., Byers, S. A., Biglione, S., Price, J. P., Maury, W. J., & Price, D. H. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm443 · Cited by 157 · see citing works

A 1.3-Å resolution crystal structure of the HIV-1 trans-activation response region RNA stem reveals a metal ion-dependent bulge conformation

Ippolito, J. A., & Steitz, T. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.17.9819 · Cited by 141 · see citing works

Mutational analysis of the conserved cysteine-rich region of the human immunodeficiency virus type 1 Tat protein

Rice, A. P., & Carlotti, F. (1990) · Journal of Virology · doi:10.1128/jvi.64.4.1864-1868.1990 · Cited by 98 · see citing works

Optimum solubility (OS) screening: an efficient method to optimize buffer conditions for homogeneity and crystallization of proteins

Jancarik, J., Pufan, R., Hong, C., Kim, S., & Kim, R. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904010972 · Cited by 94 · see citing works

What does the structure-function relationship of the HIV-1 Tat protein teach us about developing an AIDS vaccine?

Campbell, G. R., & Loret, E. P. (2009) · Retrovirology · doi:10.1186/1742-4690-6-50 · Cited by 93 · see citing works

TAR RNA loop: A scaffold for the assembly of a regulatory switch in HIV replication

Richter, S. N., Ping, Y., & Rana, T. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.122119999 · Cited by 84 · see citing works

Interactions between Tat and TAR and Human Immunodeficiency Virus Replication Are Facilitated by Human Cyclin T1 but Not Cyclins T2a or T2b

Wimmer, J., Fujinaga, K., Taube, R., Cujec, T. P., Zhu, Y., Peng, J., Price, D. H., & Peterlin, B. M. (1999) · Virology · doi:10.1006/viro.1998.9589 · Cited by 81 · see citing works

HIV-1 Tat Interacts with Cyclin T1 to Direct the P-TEFb CTD Kinase Complex to TAR RNAPreprint

Garber, M. E., Wei, P., & Jones, K. A. (1998) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1998.63.371 · Cited by 78 · see citing works

Structural insights into the Cyclin T1–Tat–TAR RNA transcription activation complex from EIAV

Anand, K., Schulte, A., Vogel‐Bachmayr, K., Scheffzek, K., & Geyer, M. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1513 · Cited by 78 · see citing works

Tat acetylation modulates assembly of a viral-host RNA–protein transcription complex

D’Orso, I., & Frankel, A. D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900012106 · Cited by 67 · see citing works

Interactions between Equine Cyclin T1, Tat, and TAR Are Disrupted by a Leucine-to-Valine Substitution Found in Human Cyclin T1

Taube, R., Fujinaga, K., Irwin, D., Wimmer, J., Geyer, M., & Peterlin, B. M. (2000) · Journal of Virology · doi:10.1128/jvi.74.2.892-898.2000 · Cited by 37 · see citing works

RNA‐driven cyclin‐dependent kinase regulation: When CDK9/cyclin T subunits of P‐TEFb meet their ribonucleoprotein partners

Michels, A. A., & Bensaude, O. (2008) · Biotechnology Journal · doi:10.1002/biot.200800104 · Cited by 34 · see citing works

Moving Forward in HIV Vaccine Development

Letvin, N. L. (2009) · Science · doi:10.1126/science.1183278 · Cited by 31 · see citing works

Conservative Mutations in the Putative Metal-Binding Region of Human Immunodeficiency Virus Tat Disrupt Virus Replication

Sadaie, M. R., Mukhopadhyaya, R., BENAISSA, Z. N., Pavlakis, G. N., & Wong‐Staal, F. (1990) · AIDS Research and Human Retroviruses · doi:10.1089/aid.1990.6.1257 · Cited by 23 · see citing works

High-Resolution Crystals of Methionine Aminopeptidase fromPyrococcus furiosusObtained by Water-Mediated Transformation

Tahirov, T. H., Oki, H., Tomitake Tsukihara, A., Ogasahara, K., Yutani, K., Libeu, C. P., Izu, Y., Tsunasawa, S., & Kato, I. (1998) · Journal of Structural Biology · doi:10.1006/jsbi.1997.3940 · Cited by 21 · see citing works

Role of the HIV-1 Positive Elongation Factor P-TEFb and Inhibitors Thereof

Wang, Y., Liu, X., & Clercq, E. D. (2009) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557510909030379 · Cited by 19 · see citing works

Mutagenesis of EIAV TAT Reveals Structural Features Essential for Transcriptional Activation and TAR Element Recognition

Derse, D., & Newbold, S. H. (1993) · Virology · doi:10.1006/viro.1993.1291 · Cited by 18 · see citing works

RNA Polymerase II Elongation Control

Zhou, Q., Li, T., & Price, D. H. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052610-095910 · Cited by 568 · see citing works

HIV LatencyPreprint

Siliciano, R. F., & Greene, W. C. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a007096 · Cited by 509 · see citing works

Transcriptional and Posttranscriptional Regulation of HIV-1 Gene Expression

Karn, J., & Stoltzfus, C. M. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006916 · Cited by 437 · see citing works

The structural biology of HIV-1: mechanistic and therapeutic insights

Engelman, A., & Cherepanov, P. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2747 · Cited by 426 · see citing works

Mediator kinase inhibition further activates super-enhancer-associated genes in AML

Pelish, H. E., Liau, B. B., Nitulescu, I. I., Tangpeerachaikul, A., Poss, Z. C., Silva, D. H. D., Caruso, B., Arefolov, A., Fadeyi, O., Christie, A. L., et al. (2015) · Nature · doi:10.1038/nature14904 · Cited by 397 · see citing works

HIV-1 transcription and latency: an update

Lint, C. M. V., Bouchat, S., & Marcello, A. (2013) · Retrovirology · doi:10.1186/1742-4690-10-67 · Cited by 336 · see citing works

Structure and mechanism of the RNA polymerase II transcription machineryPreprint

Schier, A. C., & Taatjes, D. J. (2020) · Genes & Development · doi:10.1101/gad.335679.119 · Cited by 301 · see citing works

The Control of HIV Transcription: Keeping RNA Polymerase II on Track

Ott, M., Geyer, M., & Zhou, Q. (2011) · Cell Host & Microbe · doi:10.1016/j.chom.2011.11.002 · Cited by 284 · see citing works

Structural insights into the functional diversity of the CDK–cyclin family

Wood, D. J., & Endicott, J. (2018) · Open Biology · doi:10.1098/rsob.180112 · Cited by 264 · see citing works

NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers

Sekhar, A., & Kay, L. E. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305688110 · Cited by 251 · see citing works

The Ins and Outs of HIV ‐1 Tat

Debaisieux, S., Rayne, F., Yezid, H., & Beaumelle, B. D. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01286.x · Cited by 245 · see citing works

CDK1 structures reveal conserved and unique features of the essential cell cycle CDK

Brown, N. R., Korolchuk, S., Martin, M. P., Stanley, W. A., Moukhametzianov, R., Noble, M. E. M., & Endicott, J. (2015) · Nature Communications · doi:10.1038/ncomms7769 · Cited by 238 · see citing works

Brd4 activates P-TEFb for RNA polymerase II CTD phosphorylation

Itzen, F., Greifenberg, A. K., Bösken, C. A., & Geyer, M. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku449 · Cited by 237 · see citing works

Transcriptional control of HIV latency: Cellular signaling pathways, epigenetics, happenstance and the hope for a cure

Mbonye, U. R., & Karn, J. (2014) · Virology · doi:10.1016/j.virol.2014.02.008 · Cited by 226 · see citing works

CDK9: a signaling hub for transcriptional control

Bacon, C. W., & D’Orso, I. (2018) · Transcription · doi:10.1080/21541264.2018.1523668 · Cited by 201 · see citing works

Serine-7 but not serine-5 phosphorylation primes RNA polymerase II CTD for P-TEFb recognition

Czudnochowski, N., Bösken, C. A., & Geyer, M. (2012) · Nature Communications · doi:10.1038/ncomms1846 · Cited by 191 · see citing works

The Molecular Basis for Human Immunodeficiency Virus Latency

Mbonye, U., & Karn, J. (2017) · Annual Review of Virology · doi:10.1146/annurev-virology-101416-041646 · Cited by 182 · see citing works

7SK snRNA: a noncoding RNA that plays a major role in regulating eukaryotic transcription

Peterlin, B. M., Brogie, J. E., & Price, D. H. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.106 · Cited by 181 · see citing works

The molecular biology of HIV latency: breaking and restoring the Tat-dependent transcriptional circuit

Karn, J. (2010) · Current Opinion in HIV and AIDS · doi:10.1097/coh.0b013e328340ffbb · Cited by 178 · see citing works

P-TEFb: The master regulator of transcription elongation

Fujinaga, K., Huang, F., & Peterlin, B. M. (2023) · Molecular Cell · doi:10.1016/j.molcel.2022.12.006 · Cited by 156 · see citing works

Ready, pause, go: regulation of RNA polymerase II pausing and release by cellular signaling pathways

Liu, X., Kraus, W. L., & Bai, X. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.07.003 · Cited by 152 · see citing works

Tat is a multifunctional viral protein that modulates cellular gene expression and functions

Clark, E. A., Nava, B. C., & Caputi, M. (2017) · Oncotarget · doi:10.18632/oncotarget.15174 · Cited by 132 · see citing works

Curcumin inhibits HIV-1 by promoting Tat protein degradation

Ali, A., & Banerjea, A. C. (2016) · Scientific Reports · doi:10.1038/srep27539 · Cited by 122 · see citing works

The nexus between RNA-binding proteins and their effectors

He, S., Valkov, E., Cheloufi, S., & Murn, J. (2022) · Nature Reviews Genetics · doi:10.1038/s41576-022-00550-0 · Cited by 119 · see citing works

RNA Polymerase II Transcription Elongation Control

Guo, J., & Price, D. H. (2013) · Chemical Reviews · doi:10.1021/cr400105n · Cited by 117 · see citing works

CBFβ Stabilizes HIV Vif to Counteract APOBEC3 at the Expense of RUNX1 Target Gene Expression

Kim, D. Y., Kwon, E., Hartley, P. D., Crosby, D. C., Mann, S., Krogan, N. J., & Gross, J. D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.12.012 · Cited by 116 · see citing works

Perspective of Cyclin-dependent kinase 9 (CDK9) as a Drug Target

Kryštof, V., Baumli, S., & Fürst, R. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212800672750 · Cited by 112 · see citing works

The Mechanism of Release of P-TEFb and HEXIM1 from the 7SK snRNP by Viral and Cellular Activators Includes a Conformational Change in 7SK

Krueger, B. J., Varzavand, K., Cooper, J. J., & Price, D. H. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012335 · Cited by 111 · see citing works

Protein intrinsic disorder as a flexible armor and a weapon of HIV-1

Xue, B., Mizianty, M. J., Kurgan, L., & Uversky, V. N. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0859-3 · Cited by 107 · see citing works

Control of HIV Latency by Epigenetic and Non-Epigenetic Mechanisms

Karn, J., & Mbonye, U. R. (2011) · Current HIV Research · doi:10.2174/157016211798998736 · Cited by 99 · see citing works

CDK9 keeps RNA polymerase II on track

Egloff, S. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03878-8 · Cited by 99 · see citing works

HIV Tat protein and amyloid-β peptide form multifibrillar structures that cause neurotoxicity

Hategan, A. P., Bianchet, M. A., Steiner, J. P., Karnaukhova, E., Masliah, E., Fields, A., Lee, M., Dickens, A. M., Haughey, N. J., Dimitriadis, E. K., et al. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3379 · Cited by 93 · see citing works

Phosphorylation of CDK9 at Ser175 Enhances HIV Transcription and Is a Marker of Activated P-TEFb in CD4+ T Lymphocytes

Mbonye, U. R., Gokulrangan, G., Datt, M., Dobrowolski, C. N., Cooper, M., Chance, M. R., & Karn, J. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003338 · Cited by 93 · see citing works

HIV-1 Tat recruits transcription elongation factors dispersed along a flexible AFF4 scaffold

Chou, S., Upton, H., Bao, K., Schulze-Gahmen, U., Samelson, A. J., He, N., Nowak, A., Lu, H., Krogan, N. J., Zhou, Q., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216971110 · Cited by 93 · see citing works

Transcription Factors Mediate the Enzymatic Disassembly of Promoter-Bound 7SK snRNP to Locally Recruit P-TEFb for Transcription Elongation

McNamara, R. P., McCann, J. L., Gudipaty, S. A., & D’Orso, I. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.11.003 · Cited by 90 · see citing works

HIV Genome-Wide Protein Associations: a Review of 30 Years of Research

Li, G., & Clercq, E. D. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00065-15 · Cited by 90 · see citing works

Didehydro-Cortistatin A Inhibits HIV-1 by Specifically Binding to the Unstructured Basic Region of Tat

Mediouni, S., Chinthalapudi, K., Ekka, M. K., Usui, I., Jablonski, J. A., Clementz, M. A., Mousseau, G., Nowak, J., Macherla, V. R., Beverage, J. N., et al. (2019) · mBio · doi:10.1128/mbio.02662-18 · Cited by 84 · see citing works

Structural mechanism for HIV-1 TAR loop recognition by Tat and the super elongation complex

Schulze‐Gahmen, U., & Hurley, J. H. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1806438115 · Cited by 82 · see citing works

Synthesis and Evaluation of Phosphorus Containing, Specific CDK9/CycT1 Inhibitors

Németh, G., Greff, Z., Sipos, A., Varga, Z., Székely, R., Sebestyén, M., Jászay, Z. M., Béni, S., Nemes, Z., Pirat, J., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401742r · Cited by 81 · see citing works

AFF1 is a ubiquitous P-TEFb partner to enable Tat extraction of P-TEFb from 7SK snRNP and formation of SECs for HIV transactivation

Lu, H., Li, Z., Xue, Y., Schulze‐Gahmen, U., Johnson, J. R., Krogan, N. J., Alber, T., & Zhou, Q. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318503111 · Cited by 80 · see citing works

The AFF4 scaffold binds human P-TEFb adjacent to HIV Tat

Schulze‐Gahmen, U., Upton, H. E., Birnberg, A., Bao, K., Chou, S., Krogan, N. J., Zhou, Q., & Alber, T. (2013) · eLife · doi:10.7554/elife.00327 · Cited by 79 · see citing works

Architecture and RNA binding of the human negative elongation factor

Vos, S. M., Pöllmann, D., Caizzi, L., Hofmann, K., Rombaut, P., Zimniak, T., Herzog, F., & Cramer, P. (2016) · eLife · doi:10.7554/elife.14981 · Cited by 78 · see citing works

HIV, Tat and dopamine transmission

Gaskill, P. J., Miller, D. R., Gamble‐George, J., Yano, H., & Khoshbouei, H. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.04.015 · Cited by 77 · see citing works

Genetic variation and function of the HIV-1 Tat protein

Spector, C., Mele, A. R., Wigdahl, B. L., & Nonnemacher, M. R. (2019) · Medical Microbiology and Immunology · doi:10.1007/s00430-019-00583-z · Cited by 77 · see citing works

Inhibition of Both HIV-1 Reverse Transcription and Gene Expression by a Cyclic Peptide that Binds the Tat-Transactivating Response Element (TAR) RNA

Lalonde, M. S., Lobritz, M. A., Ratcliff, A. N., Chamanian, M., Athanassiou, Z., Tyagi, M., Wong, J. Y., Robinson, J. A., Karn, J., Varani, G., et al. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002038 · Cited by 76 · see citing works

Comparative Structural and Functional Studies of 4-(Thiazol-5-yl)-2-(phenylamino)pyrimidine-5-carbonitrile CDK9 Inhibitors Suggest the Basis for Isotype Selectivity

Hole, A. J., Baumli, S., Shao, H., Shi, S., Huang, S., Pepper, C. J., Fischer, P. M., Wang, S., Endicott, J., & Noble, M. E. M. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm301495v · Cited by 73 · see citing works

Targeting HIV Transcription: The Quest for a Functional Cure

Mousseau, G., Mediouni, S., & Valente, S. T. (2015) · Current topics in microbiology and immunology · doi:10.1007/82_2015_435 · Cited by 72 · see citing works

HIV Control Is Mediated in Part by CD8 + T-Cell Targeting of Specific Epitopes

Pereyra, F., Heckerman, D. E., Carlson, J. M., Kadie, C. M., Soghoian, D. Z., Karel, D., Goldenthal, A. R., Davis, O. B., DeZiel, C. E., Lin, T.-H., et al. (2014) · Journal of Virology · doi:10.1128/jvi.01004-14 · Cited by 72 · see citing works

The emerging picture of CDK9/P-TEFb: more than 20 years of advances since PITALRE

Paparidis, N. F. D. S., Durvale, M. D. C., & Canduri, F. (2016) · Molecular BioSystems · doi:10.1039/c6mb00387g · Cited by 72 · see citing works

Distinct layers of BRD4-PTEFb reveal bromodomain-independent function in transcriptional regulation

Zheng, B., Gold, S. R., Iwanaszko, M., Howard, B. C., Wang, L., & Shilatifard, A. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.06.032 · Cited by 71 · see citing works

Cyclin-dependent kinase 7 (CDK7)-mediated phosphorylation of the CDK9 activation loop promotes P-TEFb assembly with Tat and proviral HIV reactivation

Mbonye, U. R., Wang, B., Gokulrangan, G., Shi, W., Yang, S., & Karn, J. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001347 · Cited by 71 · see citing works

RNA-directed remodeling of the HIV-1 protein Rev orchestrates assembly of the Rev–Rev response element complex

Jayaraman, B., Crosby, D. C., Homer, C. M., Ribeiro, I., Mavor, D., & Frankel, A. D. (2014) · eLife · doi:10.7554/elife.04120 · Cited by 69 · see citing works

Extracellular vesicles in virus infection and pathogenesis

McNamara, R. P., & Dittmer, D. P. (2020) · Current Opinion in Virology · doi:10.1016/j.coviro.2020.07.014 · Cited by 68 · see citing works

Structure of a low-population binding intermediate in protein-RNA recognition

Borkar, A. N., Bardaro, M. F., Camilloni, C., Aprile, F. A., Varani, G., & Vendruscolo, M. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1521349113 · Cited by 66 · see citing works

The CDK9 C-helix Exhibits Conformational Plasticity That May Explain the Selectivity of CAN508

Baumli, S., Hole, A. J., Noble, M. E. M., & Endicott, J. (2012) · ACS Chemical Biology · doi:10.1021/cb2004516 · Cited by 63 · see citing works

Lost in Transcription: Molecular Mechanisms that Control HIV Latency

Taube, R., & Peterlin, B. M. (2013) · Viruses · doi:10.3390/v5030902 · Cited by 63 · see citing works

Structural insight into the mechanism of stabilization of the 7SK small nuclear RNA by LARP7

Uchikawa, E., Natchiar, K., Han, X. Y., Proux, F., Roblin, P., Zhang, E., Durand, A., Klaholz, B. P., & Dock‐Brégeon, A. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv173 · Cited by 60 · see citing works

Crystal structure of HIV-1 Tat complexed with human P-TEFb and AFF4

Gu, J., Babayeva, N. D., Suwa, Y., Baranovskiy, A. G., Price, D. H., & Tahirov, T. H. (2014) · Cell Cycle · doi:10.4161/cc.28756 · Cited by 58 · see citing works

Tits and bits of HIV Tat protein

Johri, M. K., Mishra, R., Chhatbar, C., Unni, S. K., & Singh, S. K. (2011) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2011.546339 · Cited by 58 · see citing works

Insights into HIV-1 proviral transcription from integrative structure and dynamics of the Tat:AFF4:P-TEFb:TAR complex

Schulze‐Gahmen, U., Echeverria, I., Stjepanović, G., Bai, Y., Lu, H., Schneidman‐Duhovny, D., Doudna, J. A., Zhou, Q., Šali, A., & Hurley, J. H. (2016) · eLife · doi:10.7554/elife.15910 · Cited by 58 · see citing works

Crosstalk between histone modifications indicates that inhibition of arginine methyltransferase CARM1 activity reverses HIV latency

Zhang, Z., Nikolai, B. C., Gates, L. A., Jung, S. Y., Siwak, E. B., He, B., Rice, A. P., O’Malley, B. W., & Feng, Q. F. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx550 · Cited by 58 · see citing works

Making Sense of Multifunctional Proteins: Human Immunodeficiency Virus Type 1 Accessory and Regulatory Proteins and Connections to Transcription

Faust, T. B., Binning, J. M., Gross, J. D., & Frankel, A. D. (2017) · Annual Review of Virology · doi:10.1146/annurev-virology-101416-041654 · Cited by 58 · see citing works

Live-cell imaging reveals the spatiotemporal organization of endogenous RNA polymerase II phosphorylation at a single gene

Forero-Quintero, L. S., Raymond, W., Handa, T., Saxton, M. N., Morisaki, T., Kimurâ, H., Bertrand, É., Munsky, B. E., & Stasevich, T. J. (2021) · Nature Communications · doi:10.1038/s41467-021-23417-0 · Cited by 58 · see citing works

AFF4 binding to Tat-P-TEFb indirectly stimulates TAR recognition of super elongation complexes at the HIV promoter

Schulze‐Gahmen, U., Lu, H., Zhou, Q., & Alber, T. (2014) · eLife · doi:10.7554/elife.02375 · Cited by 56 · see citing works

An ultra-high affinity ligand of HIV-1 TAR reveals the RNA structure recognized by P-TEFb

Shortridge, M. D., Wille, P. T., Jones, A. N., Davidson, A., Bogdanović, J., Arts, E. J., Karn, J., Robinson, J. A., & Varani, G. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky1197 · Cited by 56 · see citing works

Transition Step during Assembly of HIV Tat:P-TEFb Transcription Complexes and Transfer to TAR RNA

D’Orso, I., Jang, G. Μ., Pastuszak, A. W., Faust, T. B., Quezada, E. M., Booth, D. S., & Frankel, A. D. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00206-12 · Cited by 54 · see citing works

Functional Segregation of Overlapping Genes in HIV

Fernandes, J. D., Faust, T. B., Strauli, N. B., Smith, C. L., Crosby, D. C., Nakamura, R. L., Hernandez, R. D., & Frankel, A. D. (2016) · Cell · doi:10.1016/j.cell.2016.11.031 · Cited by 54 · see citing works

Viral–Host Interactions That Control HIV-1 Transcriptional Elongation

Lu, H., Li, Z., Xue, Y., & Zhou, Q. (2013) · Chemical Reviews · doi:10.1021/cr400120z · Cited by 52 · see citing works

HIV and Alzheimer’s disease: complex interactions of HIV-Tat with amyloid β peptide and Tau protein

Hategan, A. P., Masliah, E., & Nath, A. (2019) · Journal of NeuroVirology · doi:10.1007/s13365-019-00736-z · Cited by 52 · see citing works

Reconstitution of a functional 7SK snRNP

Brogie, J. E., & Price, D. H. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx262 · Cited by 51 · see citing works

HIV-1 Tat: An update on transcriptional and non-transcriptional functions

Ali, A., Mishra, R., Kaur, H., & Banerjea, A. C. (2021) · Biochimie · doi:10.1016/j.biochi.2021.07.001 · Cited by 50 · see citing works

CDK2 Regulates HIV-1 Transcription by Phosphorylation of CDK9 on Serine 90

Breuer, D., Kotelkin, A., Ammosova, T., Kumari, N., Ivanov, A. I., Ilatovskiy, A. V., Beullens, M., Roane, P. R., Bollen, M., Petukhov, M., et al. (2012) · Retrovirology · doi:10.1186/1742-4690-9-94 · Cited by 50 · see citing works

Discovery of coumarin derivatives as potent and selective cyclin-dependent kinase 9 (CDK9) inhibitors with high antitumour activity

Xu, J., Li, H., Wang, X., Huang, J., Li, S., Liu, C., Dong, R., Zhu, G., Duan, C., Jiang, F., et al. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112424 · Cited by 50 · see citing works

An evolutionary conserved Hexim1 peptide binds to the Cdk9 catalytic site to inhibit P-TEFb

Kobbi, L., Demey, E., Brayé, F., Proux, F., Kolesnikova, O., Vinh, J., Poterszman, A., & Bensaude, O. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612331113 · Cited by 47 · see citing works

Fragment based search for small molecule inhibitors of HIV-1 Tat-TAR

Zeiger, M., Stark, S., Kalden, E., Ackermann, B., Ferner, J., Scheffer, U., Shoja-Bazargani, F., Erdel, V., Schwalbe, H., & Göbel, M. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.11.004 · Cited by 45 · see citing works

Face-time with TAR: Portraits of an HIV-1 RNA with diverse modes of effector recognition relevant for drug discovery

Chavali, S. S., Bonn, R. B., & Wedekind, J. E. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.006860 · Cited by 45 · see citing works

Effect of Mimetic CDK9 Inhibitors on HIV-1-Activated Transcription

Duyne, R. V., Guendel, I., Jaworski, E. M., Sampey, G. C., Klase, Z. A., Chen, H., Zeng, C., Kovalskyy, D., el Kouni, M. H., Lepene, B. S., et al. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.12.005 · Cited by 44 · see citing works

Discovery and SAR of novel pyrazolo[1,5-a]pyrimidines as inhibitors of CDK9

Phillipson, L. J., Segal, D., Nero, T. L., Parker, M. W., Wan, S. S., de Silva, M., Guthridge, M. A., Wei, A. H., & Burns, C. J. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.08.035 · Cited by 43 · see citing works

HIV Tat/P-TEFb Interaction: A Potential Target for Novel Anti-HIV Therapies

Asamitsu, K., Fujinaga, K., & Okamoto, T. (2018) · Molecules · doi:10.3390/molecules23040933 · Cited by 42 · see citing works

The Block-and-Lock Strategy for Human Immunodeficiency Virus Cure: Lessons Learned from Didehydro–Cortistatin A

Li, C., Mori, L., & Valente, S. T. (2020) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiaa681 · Cited by 42 · see citing works

Role of Host Factors on the Regulation of Tat-Mediated HIV-1 Transcription

Mousseau, G., & Valente, S. T. (2017) · Current Pharmaceutical Design · doi:10.2174/1381612823666170622104355 · Cited by 41 · see citing works

The Drosophila 7SK snRNP and the essential role of dHEXIM in development

Nguyen, D. K., Krueger, B. J., Sedore, S. C., Brogie, J. E., Rogers, J. T., Rajendra, T. K., Saunders, A., Matera, A. G., Lis, J. T., Uguen, P., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks191 · Cited by 41 · see citing works

Structural characterization of the cyclin-dependent protein kinase family

Endicott, J., & Noble, M. E. M. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130097 · Cited by 40 · see citing works

Structures of the CDK12/CycK complex with AMP-PNP reveal a flexible C-terminal kinase extension important for ATP binding

Dixon-Clarke, S. E., Elkins, J. M., Cheng, S.-W. G., Morin, G. B., & Bullock, A. N. (2015) · Scientific Reports · doi:10.1038/srep17122 · Cited by 38 · see citing works

Transcription elongation control by the 7SK snRNP complex: Releasing the pause

McNamara, R. P., Bacon, C. W., & D’Orso, I. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1181241 · Cited by 38 · see citing works

The CDK9 Tail Determines the Reaction Pathway of Positive Transcription Elongation Factor b

Baumli, S., Hole, A. J., Wang, L.-Z., Noble, M. E. M., & Endicott, J. (2012) · Structure · doi:10.1016/j.str.2012.08.011 · Cited by 38 · see citing works

Computer‐Aided Design, Synthesis and Validation of 2‐Phenylquinazolinone Fragments as CDK9 Inhibitors with Anti‐HIV‐1 Tat‐Mediated Transcription Activity

Sancineto, L., Iraci, N., Massari, S., Attanasio, V., Corazza, G., Barreca, M. L., Sabatini, S., Manfroni, G., Avanzi, N. R., Cecchetti, V., et al. (2013) · ChemMedChem · doi:10.1002/cmdc.201300287 · Cited by 37 · see citing works

Structural basis for ELL2 and AFF4 activation of HIV-1 proviral transcription

Qi, S., Li, Z., Schulze‐Gahmen, U., Stjepanović, G., Zhou, Q., & Hurley, J. H. (2017) · Nature Communications · doi:10.1038/ncomms14076 · Cited by 37 · see citing works

P-TEFb goes viral

Zaborowska, J., Isa, N. F., & Murphy, S. (2015) · Inside the Cell · doi:10.1002/icl3.1037 · Cited by 36 · see citing works

The HIV-1 Tat protein recruits a ubiquitin ligase to reorganize the 7SK snRNP for transcriptional activation

Faust, T. B., Li, Y., Bacon, C. W., Jang, G. Μ., Weiss, A., Jayaraman, B., Newton, B. W., Krogan, N. J., D’Orso, I., & Frankel, A. D. (2018) · eLife · doi:10.7554/elife.31879 · Cited by 35 · see citing works

Vitamin E TPGS based transferosomes augmented TAT as a promising delivery system for improved transdermal delivery of raloxifene

Alhakamy, N. A., Fahmy, U. A., & Ahmed, O. A. A. (2019) · PLoS ONE · doi:10.1371/journal.pone.0226639 · Cited by 35 · see citing works

Varying Modulation of HIV-1 LTR Activity by BAF Complexes

Duyne, R. V., Guendel, I., Narayanan, A., Gregg, E. W., Shafagati, N., Tyagi, M., Easley, R., Klase, Z. A., Nekhai, S. A., Kehn‐Hall, K., et al. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.06.001 · Cited by 35 · see citing works

The role of HIV Tat protein in HIV-related cardiovascular diseases

Jiang, Y., Chai, L., Fasae, M. B., & Bai, Y. (2018) · Journal of Translational Medicine · doi:10.1186/s12967-018-1500-0 · Cited by 35 · see citing works

P‐TEFb goes viral

Zaborowska, J., Isa, N. F., & Murphy, S. (2016) · BioEssays · doi:10.1002/bies.201670912 · Cited by 34 · see citing works

Tat basic domain: A “Swiss army knife” of HIV‐1 Tat?

Kurnaeva, M. A., Sheval, E. V., Musinova, Y. R., & Vassetzky, Y. S. (2019) · Reviews in Medical Virology · doi:10.1002/rmv.2031 · Cited by 33 · see citing works

Tat-Based Therapies as an Adjuvant for an HIV-1 Functional Cure

Jin, H., Li, D., Lin, M., Li, L., & Harrich, D. (2020) · Viruses · doi:10.3390/v12040415 · Cited by 33 · see citing works

The CD8 + T Cell Noncytotoxic Antiviral Responses

Morvan, M. G., Teque, F., Locher, C. P., & Levy, J. A. (2021) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00155-20 · Cited by 33 · see citing works

PJA2 ubiquitinates the HIV-1 Tat protein with atypical chain linkages to activate viral transcription

Faust, T. B., Li, Y., Jang, G. Μ., Johnson, J. R., Yang, S., Weiss, A., Krogan, N. J., & Frankel, A. D. (2017) · Scientific Reports · doi:10.1038/srep45394 · Cited by 32 · see citing works

Withaferin A Suppresses Beta Amyloid in APP Expressing Cells: Studies for Tat and Cocaine Associated Neurological Dysfunctions

Tiwari, S., Atluri, V. S. R., Yndart, A., Jayant, R. D., Kaushik, A. K., Geiger, J. D., & Nair, M. N. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00291 · Cited by 32 · see citing works

Blood-brain barrier penetration of an Aβ-targeted, arginine-rich, d -enantiomeric peptide

Jiang, N., Frenzel, D., Schartmann, E., van Groen, T., Kadish, I., Shah, N. J., Langen, K., Willbold, D., & Willuweit, A. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2016.07.002 · Cited by 32 · see citing works

HIV-1 Tat: Its Dependence on Host Factors is Crystal Clear

D’Orso, I., & Frankel, A. D. (2010) · Viruses · doi:10.3390/v2102226 · Cited by 19 · see citing works

Crystal structure of HIV-1 Tat complexed with human P-TEFb and AFF4

Gu, J., Babayeva, N. D., Suwa, Y., Baranovskiy, A. G., Price, D. H., & Tahirov, T. H. (2014) · Cell Cycle · doi:10.4161/cc.28756 · Cited by 58 · see citing works

Tat-SF: A Cellular Factor for Regulation of Transcriptional Elongation by HIV Tat

Zhou, Q., & Luo, K. (1999) · Defense Technical Information Center (DTIC)

The Control of HIV Transcription: Keeping RNA Polymerase II on Track

Ott, M., Geyer, M., & Zhou, Q. (2011) · Cell Host & Microbe · doi:10.1016/j.chom.2011.11.002 · Cited by 284 · see citing works

Tat-SF: A Cellular Factor for Regulation of Transcriptional Elongatin by HIV Tat-

Zhou, Q., & Lou, K. (2000) · Defense Technical Information Center (DTIC) · doi:10.21236/ada391394