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Relevant bibliographies by topics / Transactivation

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Academic literature on the topic 'Transactivation'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 March 2023

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Journal articles on the topic "Transactivation"

1

Wierstra, Inken, and Jürgen Alves. "Despite its strong transactivation domain, transcription factor FOXM1c is kept almost inactive by two different inhibitory domains." Biological Chemistry 387, no. 7 (July 1, 2006): 963–76. http://dx.doi.org/10.1515/bc.2006.120.

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Abstract FOXM1c (MPP2) is an activating transcription factor with several nuclear localization signals, a forkhead domain for DNA binding, and a very strong acidic transactivation domain. Despite its very strong transactivation domain, FOXM1c is kept almost inactive by two different independent inhibitory domains, the N-terminus and the central domain. The N-terminus as a specific negative-regulatory domain directly binds to and thus inhibits the transactivation domain completely. However, it lacks any transrepression potential. In contrast, the central domain functions as a strong RB-independent transrepression domain and as an RB-recruiting negative-regulatory domain. The N-terminus alone is sufficient to eliminate transactivation, while the central domain alone represses the transactivation domain only partially. This hierarchy of the two inhibitory domains offers the possibility to activate the almost inactive wild type in two steps in vitro: deletion of the N-terminus results in a strong transactivator, while additional deletion of the central domain in a very strong transactivator. We suggest that the very high potential of the transactivation domain has to be tightly controlled by these two inhibitory domains because FOXM1 stimulates proliferation by promoting G1/S transition, as well as G2/M transition, and because deregulation of such potent activators of proliferation can result in tumorigenesis.

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Boulanger, Marie-Chloé, Chen Liang, Rodney S. Russell, Rongtuan Lin, Mark T. Bedford, Mark A. Wainberg, and Stéphane Richard. "Methylation of Tat by PRMT6 Regulates Human Immunodeficiency Virus Type 1 Gene Expression." Journal of Virology 79, no. 1 (January 1, 2005): 124–31. http://dx.doi.org/10.1128/jvi.79.1.124-131.2005.

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ABSTRACT The human immunodeficiency virus (HIV) transactivator protein, Tat, stimulates transcription from the viral long terminal repeats via an arginine-rich transactivating domain. Since arginines are often known to be methylated, we investigated whether HIV type 1 (HIV-1) Tat was a substrate for known protein arginine methyltransferases (PRMTs). Here we identify Tat as a substrate for the arginine methyltransferase, PRMT6. Tat is specifically associated with and methylated by PRMT6 within cells. Overexpression of wild-type PRMT6, but not a methylase-inactive PRMT6 mutant, decreased Tat transactivation of an HIV-1 long terminal repeat luciferase reporter plasmid in a dose-dependent manner. Knocking down PRMT6 consistently increased HIV-1 production in HEK293T cells and also led to increased viral infectiousness as shown in multinuclear activation of a galactosidase indicator assays. Our study demonstrates that arginine methylation of Tat negatively regulates its transactivation activity and that PRMT6 acts as a restriction factor for HIV replication.

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Bull, P., K. L. Morley, M. F. Hoekstra, T. Hunter, and I. M. Verma. "The mouse c-rel protein has an N-terminal regulatory domain and a C-terminal transcriptional transactivation domain." Molecular and Cellular Biology 10, no. 10 (October 1990): 5473–85. http://dx.doi.org/10.1128/mcb.10.10.5473-5485.1990.

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We have shown that the murine c-rel protein can act as a transcriptional transactivator in both yeast and mammalian cells. Fusion proteins generated by linking rel sequences to the DNA-binding domain of the yeast transcriptional activator GAL4 activate transcription from a reporter gene linked in cis to a GAL4 binding site. The full-length mouse c-rel protein (588 amino acids long) is a poor transactivator; however, the C-terminal portion of the protein between amino acid residues 403 to 568 is a potent transcriptional transactivator. Deletion of the N-terminal half of the c-rel protein augments its transactivation function. We propose that c-rel protein has an N-terminal regulatory domain and a C-terminal transactivation domain which together modulate its function as a transcriptional transactivator.

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Bull, P., K. L. Morley, M. F. Hoekstra, T. Hunter, and I. M. Verma. "The mouse c-rel protein has an N-terminal regulatory domain and a C-terminal transcriptional transactivation domain." Molecular and Cellular Biology 10, no. 10 (October 1990): 5473–85. http://dx.doi.org/10.1128/mcb.10.10.5473.

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We have shown that the murine c-rel protein can act as a transcriptional transactivator in both yeast and mammalian cells. Fusion proteins generated by linking rel sequences to the DNA-binding domain of the yeast transcriptional activator GAL4 activate transcription from a reporter gene linked in cis to a GAL4 binding site. The full-length mouse c-rel protein (588 amino acids long) is a poor transactivator; however, the C-terminal portion of the protein between amino acid residues 403 to 568 is a potent transcriptional transactivator. Deletion of the N-terminal half of the c-rel protein augments its transactivation function. We propose that c-rel protein has an N-terminal regulatory domain and a C-terminal transactivation domain which together modulate its function as a transcriptional transactivator.

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Pei, D. Q., and C. H. Shih. "An "attenuator domain" is sandwiched by two distinct transactivation domains in the transcription factor C/EBP." Molecular and Cellular Biology 11, no. 3 (March 1991): 1480–87. http://dx.doi.org/10.1128/mcb.11.3.1480-1487.1991.

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C/EBP is a rat liver DNA-binding protein which can act as a transcription factor. Its N-terminal portion contains three distinct domains. The first domain (amino acids 1 to 107) appears to be a highly potent transactivator. The second domain (amino acids 107 to 170) does not appear to exhibit either activation or repression activity. This domain is defined as an "attenuator domain" because its presence under four different sequence contexts reproducibly decreases the effect of transactivation of C/EBP. The third domain (amino acids 171 to 245) is a relatively weaker transactivator with a striking proline-rich motif. Deletional analysis of this third domain has shown that a 45-amino-acid region is sufficient for transactivation. This region (amino acids 171 to 215) contains 12 proline, 6 histidine, and mainly hydrophobic or noncharged amino acids. Further mutational analysis of a highly conserved proline-octamer region within this domain indicates that a specific proline content is not crucial for transactivation.

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Pei, D. Q., and C. H. Shih. "An "attenuator domain" is sandwiched by two distinct transactivation domains in the transcription factor C/EBP." Molecular and Cellular Biology 11, no. 3 (March 1991): 1480–87. http://dx.doi.org/10.1128/mcb.11.3.1480.

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C/EBP is a rat liver DNA-binding protein which can act as a transcription factor. Its N-terminal portion contains three distinct domains. The first domain (amino acids 1 to 107) appears to be a highly potent transactivator. The second domain (amino acids 107 to 170) does not appear to exhibit either activation or repression activity. This domain is defined as an "attenuator domain" because its presence under four different sequence contexts reproducibly decreases the effect of transactivation of C/EBP. The third domain (amino acids 171 to 245) is a relatively weaker transactivator with a striking proline-rich motif. Deletional analysis of this third domain has shown that a 45-amino-acid region is sufficient for transactivation. This region (amino acids 171 to 215) contains 12 proline, 6 histidine, and mainly hydrophobic or noncharged amino acids. Further mutational analysis of a highly conserved proline-octamer region within this domain indicates that a specific proline content is not crucial for transactivation.

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Omoto, Shinya, Ebiamadon Andi Brisibe, Harumi Okuyama, and Yoichi R. Fujii. "Feline foamy virus Tas protein is a DNA-binding transactivator." Journal of General Virology 85, no. 10 (October 1, 2004): 2931–35. http://dx.doi.org/10.1099/vir.0.80088-0.

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Foamy viruses (FVs) harbour a transcriptional transactivator (Tas) and two Tas-responsive promoter regions, one in the 5′ long terminal repeat (LTR) and the other an internal promoter (IP) in the envelope gene. To analyse the mechanism of transactivation of the FVs, the specificity of feline FV (FFV) Tas protein, which is more distantly related to the respective proteins of non-human primate origin, were investigated. FFV Tas has been shown specifically to activate gene expression from the cognate promoters. No cross-transactivation was noted of the prototype foamy virus and human immunodeficiency virus type 1 LTR. The putative transactivation response element of FFV Tas was mapped to the 5′ LTR U3 region (approximately nt −228 to −195). FFV Tas binds to this element in addition to a previously described sequence (position −66 to −51). It is therefore concluded that FFV Tas is a DNA-binding transactivator that interacts with at least two regions in the virus LTR.

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Gutsch, D. E., E. A. Holley-Guthrie, Q. Zhang, B. Stein, M. A. Blanar, A. S. Baldwin, and S. C. Kenney. "The bZIP transactivator of Epstein-Barr virus, BZLF1, functionally and physically interacts with the p65 subunit of NF-kappa B." Molecular and Cellular Biology 14, no. 3 (March 1994): 1939–48. http://dx.doi.org/10.1128/mcb.14.3.1939-1948.1994.

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The Epstein-Barr virus (EBV) BZLF1 (Z) immediate-early transactivator initiates the switch between latent and productive infection in B cells. The Z protein, which has homology to the basic leucine zipper protein c-Fos, transactivates the promoters of several replicative cycle proteins. Transactivation efficiency of the EBV BMRF1 promoter by Z is cell type dependent. In B cells, in which EBV typically exists in a latent form, Z activates the BMRF1 promoter inefficiently. We have discovered that the p65 component of the cellular factor NF-kappa B inhibits transactivation of several EBV promoters by Z. Furthermore, the inhibitor of NF-kappa B, I kappa B alpha, can augment Z-induced transactivation in the B-cell line Raji. Using glutathione S-transferase fusion proteins and coimmunoprecipitation studies, we demonstrate a direct interaction between Z and p65. This physical interaction, which requires the dimerization domain of Z and the Rel homology domain of p65, can be demonstrated both in vitro and in vivo. Inhibition of Z transactivation function by NF-kappa B p65, or possibly by other Rel family proteins, may contribute to the inefficiency of Z transactivator function in B cells and may be a mechanism of maintaining B-cell-specific viral latency.

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Gutsch, D. E., E. A. Holley-Guthrie, Q. Zhang, B. Stein, M. A. Blanar, A. S. Baldwin, and S. C. Kenney. "The bZIP transactivator of Epstein-Barr virus, BZLF1, functionally and physically interacts with the p65 subunit of NF-kappa B." Molecular and Cellular Biology 14, no. 3 (March 1994): 1939–48. http://dx.doi.org/10.1128/mcb.14.3.1939.

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The Epstein-Barr virus (EBV) BZLF1 (Z) immediate-early transactivator initiates the switch between latent and productive infection in B cells. The Z protein, which has homology to the basic leucine zipper protein c-Fos, transactivates the promoters of several replicative cycle proteins. Transactivation efficiency of the EBV BMRF1 promoter by Z is cell type dependent. In B cells, in which EBV typically exists in a latent form, Z activates the BMRF1 promoter inefficiently. We have discovered that the p65 component of the cellular factor NF-kappa B inhibits transactivation of several EBV promoters by Z. Furthermore, the inhibitor of NF-kappa B, I kappa B alpha, can augment Z-induced transactivation in the B-cell line Raji. Using glutathione S-transferase fusion proteins and coimmunoprecipitation studies, we demonstrate a direct interaction between Z and p65. This physical interaction, which requires the dimerization domain of Z and the Rel homology domain of p65, can be demonstrated both in vitro and in vivo. Inhibition of Z transactivation function by NF-kappa B p65, or possibly by other Rel family proteins, may contribute to the inefficiency of Z transactivator function in B cells and may be a mechanism of maintaining B-cell-specific viral latency.

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10

Sjöberg, M., and B. Vennström. "Ligand-dependent and -independent transactivation by thyroid hormone receptor beta 2 is determined by the structure of the hormone response element." Molecular and Cellular Biology 15, no. 9 (September 1995): 4718–26. http://dx.doi.org/10.1128/mcb.15.9.4718.

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Chicken thyroid hormone receptor beta 2 (cTR beta 2) is likely to serve specific functions in gene regulation since it possesses a unique N-terminal domain and is expressed in very few tissues. We demonstrate here that TR beta 2 exhibits distinct transactivation properties which are dependent on the availability of ligand and on the structure of the hormone response element. First, a strong ligand-independent transactivation was observed with hormone response elements composed of direct repeats and everted repeats. Second, TR beta 2 was induced by triiodothyronine to transactivate more efficiently than TR beta 0 on palindromic and everted-repeat types of hormone response elements. However, coexpression of the retinoid X receptor reduced the strong transactivation by TR beta 2 but not by TR beta 0 via palindromic response elements, suggesting that TR beta 2 can transactivate as a homodimer. Finally, the N terminus of TR beta 2 contains two distinct transactivation regions rich in tyrosines, which are essential for transactivation. Our results thus show that the activity of the novel transactivating region of TR beta 2 is dependent on the organization of the half-sites in the response element.

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Dissertations / Theses on the topic "Transactivation"

1

Sutherland, Jacqueline Anderson. "The transactivation functions of Fos." Thesis, University of Cambridge, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.309211.

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2

Park, Frances E. "NF-kB DNA binding and transactivation /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2001. http://wwwlib.umi.com/cr/ucsd/fullcit?p3001261.

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3

Ramakrishnan, Venkatesh. "Structural analysis of a transactivation domain cofactor complex." Doctoral thesis, [S.l. : s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=976325381.

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Bladen, Catherine Louise. "Transcriptional transactivation properties of the human MDM2 oncoprotein." Thesis, University of Newcastle Upon Tyne, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.327321.

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Walker, S. M. "Transactivation of human immunodeficiency virus by human cytomegalovirus." Thesis, University of Cambridge, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.387104.

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Schäfer, Beatrix. "Transactivation of the EGFR Signal in Human Cancer Cells." Diss., lmu, 2004. http://nbn-resolving.de/urn:nbn:de:bvb:19-23041.

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7

Betney, Russell. "Mutational analysis of the human androgen receptor transactivation domain." Thesis, University of Aberdeen, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.401515.

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Mutants were created within the main activation function domain to investigate the structure and function of this region. Structural studies based on limited proteolysis and fluorescence spectroscopy experiments, indicate that though the N-terminus is not as specially structured as either the LBD or DBD, there are regions of specific folding within the activation domain. Results from in silco investigation suggest several possible regions of a helix within the AF-1 domain, and mutants designed to disrupt these regions were less folded than the wild-type protein. Protein-protein interaction studies showed that the four mutants designed to potentially disrupt function rather than structure, had reduced binding to the large subunit of TFIIF - RAP74, but had no effect on binding to the transcriptional co-activator SRC-1a. In a functional assay performed in yeast cells, these four same mutants all showed reduced activity, showing the same trend as binding to RAP74. This could be an indication that the function of the AR is dependent upon binding to the general transcription factor TFIIF. Interestingly one of the mutants that was found to show increased structure over the wild-type protein was previously shown to have a reduced interaction with RAP74. This implies that structure is important for interaction with the transcription machinery. This was confirmed by FTIR experiments which can detect changes in the proportion of secondary structure present in a protein. These data show that the proportion of a helix present in the AF-1 domain increases when it is complexed with RAP74. GST pull-down assays then demonstrated that the complex of AF-1 and RAP74 enhanced the binding of the co-activator SRC-1a. This is the first time that this cooperativity has been demonstrated with nuclear receptors and interacting proteins. Additionally, specific phosphorylation of the AF-1 domain by glycogen synthase kinase 3 also increases the level of binding with SRC-1a. These data together suggest a possible mechanism of action for the androgen receptor and its involvement in regulating transcription.

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Chamberlain, Nancy Louise. "Molecular analysis of transcriptional transactivation by the androgen receptor." Diss., The University of Arizona, 1994. http://hdl.handle.net/10150/186951.

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The physiological effects of steroid hormones are mediated through intracellular receptors that regulate transcription of hormone response element (HRE)-containing genes. Although the androgen receptor (AR) and the glucocorticoid receptor (GR) are coexpressed in many tissues and bind identical HREs, biological actions of each hormone are distinct. Elucidating the mechanisms by which AR and GR regulate transcription of their target genes is vital to understanding cell- and receptor-specific effects of steroid hormones. These receptor-specific effects were investigated using a system in which AR and GR differ in their abilities to activate transcription from the same reporter genes. To determine if the differential activity was due to inherent differences between AR and GR functional domains, the activities of AR/GR chimeric receptors were examined. Functional differences in the N-terminal modulatory domains and, to a lesser degree, the DNA binding domains, contributed to the differential transactivation. A panel of AR derivatives was constructed to examine the function of the N-terminal domain of this receptor. The AR modulatory domain contains a tract of glutamine residues encoded by the trinucleotide CAG. Expansion of this trinucleotide repeat is correlated with the incidence and severity of the degenerative neuromuscular syndrome Kennedy's disease. To investigate the relationship of this repeat to AR function, receptors that varied in the presence, position or size of the polyglutamine tract were constructed. Elimination of the tract resulted in elevated transactivation. Progressive expansion of the repeat caused a linear decrease in transcriptional activation. These results indicate the polyglutamine tract is inhibitory to AR transactivation function. Further analysis of the AR modulatory domain revealed two regions are necessary for maximal transactivation. Secondary structure prediction and site-directed mutagenesis of one region suggest a ten residue acidic amphipathic α-helix is critical for activity. The second region may be a member of the proline-rich class of activation domains. Together, these two regions may form an interaction surface that contacts a limiting factor(s) required for activated transcription. Receptor-selective interactions with promoter- or cell-specific auxiliary factors could control the specificity of steroid-regulated gene networks.

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9

Ramsay, Nicola. "GAL4-mediated transactivation of UAS-linked transgenes in Arabidopsis thaliana." Thesis, University of Warwick, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.484177.

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10

Graham, Neil Stuart. "Development of a transactivation system for use in crop plants." Thesis, University of Warwick, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.343207.

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Books on the topic "Transactivation"

1

Girardi, Anthony J. Viral transactivation. Bethesda, MD: U.S. Dept. of Health and Human Services, Public Health Service, National Institutes of Health, National Cancer Institute, International Cancer Research Data Bank, 1989.

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2

Graham, Neil Stuart. Development of a transactivation system for use in crop plants. [s.l.]: typescript, 1999.

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Ho, Jenny Sau Ling. Characterization of heat shock factor transactivation during heat shock in Drosophila. Ottawa: National Library of Canada, 2002.

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Majumdar, Sonali. Structural and functional divergence of the transcription factor Pit-1: Analysis of the pou and transactivation domains. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1997.

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Siegert, Peter. Pasteurella multocida toxin prevents osteoblast differentiation by transactivation of the MAP-kinase cascade via the Gaq/11 - p63RhoGEF - RhoA axis. Freiburg: Universität, 2013.

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6

Pittol, José Miguel Ramos. Characterization of a novel transactivation domain of NF-kB p65. 2013.

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Hsiung, Marilyn S. Mechanisms of D(4) dopamine receptor-mediated platelet-derived growth factor receptor-beta transactivation. 2006.

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8

Test No. 457: BG1Luc Estrogen Receptor Transactivation Test Method for Identifying Estrogen Receptor Agonists and Antagonists. OECD, 2012. http://dx.doi.org/10.1787/9789264185395-en.

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9

Silver, Sandra Sarniak. Transactivation of herpes simplex virus [symbol for gamma, etc.]-thymidine kinase chimeric genes in different genomic environments. 1985.

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Test No. 455: Performance-Based Test Guideline for Stably Transfected Transactivation In Vitro Assays to Detect Estrogen Receptor Agonists. OECD, 2012. http://dx.doi.org/10.1787/9789264185388-en.

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Book chapters on the topic "Transactivation"

1

Martin, Matthew B., Thomas L. Leeper, and Frank J. Schmidt. "Transactivation of Large Ribozymes." In RNA-RNA Interactions, 57–62. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1896-6_5.

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2

Wang, F., H. Kikutani, S. Tsang, T. Kishimoto, and E. Kieff. "EBNA-2 Transactivation of CD23." In Epstein-Barr Virus and Human Disease • 1990, 43–46. Totowa, NJ: Humana Press, 1991. http://dx.doi.org/10.1007/978-1-4612-0405-3_5.

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Tsang, S., F. Wang, and E. Kieff. "EBNA-2 Transactivation of LMP1." In Epstein-Barr Virus and Human Disease • 1990, 47–51. Totowa, NJ: Humana Press, 1991. http://dx.doi.org/10.1007/978-1-4612-0405-3_6.

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Martin, Matthew B., Thomas L. Leeper, and Frank J. Schmidt. "ERRATUM: Transactivation of Large Ribozymes." In RNA-RNA Interactions, E1. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1896-6_15.

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Löchelt, M. "Foamy Virus Transactivation and Gene Expression." In Foamy Viruses, 27–61. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-55701-9_2.

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Hofschneider, P. H., M. Wollersheim, and P. Zahm. "Transactivation by Hepatitis B Virus DNA." In Organization and Function of the Eucaryotic Genome, 19–20. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-46611-3_23.

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Lasierra, Pilar, and Salomé Prat. "Transient Transactivation Studies in Nicotiana benthamiana Leaves." In Methods in Molecular Biology, 311–22. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7871-7_22.

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Rosenblatt, J. D., S. Miles, J. C. Gasson, and D. Prager. "Transactivation of Cellular Genes by Human Retroviruses." In Transacting Functions of Human Retroviruses, 25–49. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-78929-8_2.

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Padmanabhan, R., A. Tanimoto, and Y. Sasaguri. "Transactivation of Human cdc2 Promoter by Adenovirus E1A." In Current Topics in Microbiology and Immunology, 365–97. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-662-05597-7_12.

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Kruk, Jeff S., Azita Kouchmeshky, Nicholas Grimberg, Marina Rezkella, and Michael A. Beazely. "Transactivation of Receptor Tyrosine Kinases by Dopamine Receptors." In Neuromethods, 211–27. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-2196-6_12.

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Conference papers on the topic "Transactivation"

1

Wu, Jia-Long, Yu-Jen Lin, Shan-Fu Wu, Ying-Ting Lin, Young-Sun Lin, and Chien-Fu Huang. "Repression of Nrf1-Mediated Transactivation by MCRS2." In 2008 2nd International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2008. http://dx.doi.org/10.1109/icbbe.2008.99.

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Shatat, Mohammad, David Nethery, Ragnath Mishra, Emily Wilkenson, David Wyler, James Finigan, and Jeffrey A. Kern. "IL-1² Mediated HER2 Transactivation Alters Pulmonary Epithelial Barrier." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a3623.

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Cao, Subing, Duo Xu, Yanfeng Qi, Yang Zhan, Oliver Sartor, and Yan Dong. "Abstract 4580: A blueprint of androgen receptor splice variant transactivation." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-4580.

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Sales, D., K. Cuevas Mora, W. Roque, and F. Romero. "Impaired HSF1 Transactivation by Sumoylation Drives Cellular Senescence in Lung Fibroblast." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a2278.

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Fulciniti, Mariateresa, Mansa Munshi, Lian Xu, Teresa Calimeri, Kenneth C. Anderson, Steven Treon, and Nikhil C. Munshi. "Abstract 288: Targeting Sp1 transactivation in Waldenstrom's macroglobulinemia: A novel therapeutic option." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-288.

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Higgins, Jillian L., Aileen K. Kraus, Dominic T. Arruda, Hao Guo, Mattew Lautato, Christopher Lautato, Eliana DaCunha, et al. "Abstract 2641: Transactivation of EGFR and mTOR pathway by H2Sin cancer cells." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-2641.

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Higgins, Jillian L., Aileen K. Kraus, Dominic T. Arruda, Hao Guo, Mattew Lautato, Christopher Lautato, Eliana DaCunha, et al. "Abstract 2641: Transactivation of EGFR and mTOR pathway by H2Sin cancer cells." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-2641.

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King, Elizabeth M., Joanna E. Chivers, Mark A. Giembycz, and Robert Newton. "A Role For Transactivation In The Repression Of Inflammatory Genes By Dexamethasone." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a4909.

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Lanier, Viola, Corey Gillespie, Tanisha McGlothen, Toi Dickson, Shanchun Guo, and Ruben R. Gonzalez-Perez. "Abstract 5282: Leptin induces Notch in endothelial cells: Role of VEGFR-2 transactivation." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-5282.

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Buffa, Laura, and Zafar Nawaz. "Abstract 947: Molecular mechanism of WBP-2 coactivation function in estrogen receptor transactivation." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-947.

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Reports on the topic "Transactivation"

1

Chang, Chawnshang. Suppression of Androgen Receptor Transactivation by Akt Kinase. Fort Belvoir, VA: Defense Technical Information Center, January 2005. http://dx.doi.org/10.21236/ada444244.

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Chang, Chanshang. Suppression of Androgen Receptor Transactivation by Akt Kinase. Fort Belvoir, VA: Defense Technical Information Center, January 2004. http://dx.doi.org/10.21236/ada423309.

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Claessens, Frank A. The Hinge Region as a Key Regulatory Element of Androgen Receptor Dimerization DNA Binding and Transactivation. Fort Belvoir, VA: Defense Technical Information Center, May 2004. http://dx.doi.org/10.21236/ada427188.

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Claessens, Frank A. The Hinge Region as a Key Regulatory Element of Androgen Receptor Dimerization, DNA Binding and Transactivation. Fort Belvoir, VA: Defense Technical Information Center, May 2003. http://dx.doi.org/10.21236/ada416797.

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Attardi, Laura D., and Nitin Raj. Identifying p53 Transactivation Domain 1-Specific Inhibitors to Alleviate the Side Effects of Prostate Cancer Therapy. Fort Belvoir, VA: Defense Technical Information Center, September 2013. http://dx.doi.org/10.21236/ada593265.

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Attardi, Laura D., and Nitin Raj. Identifying p53 Transactivation Domain 1-Specific Inhibitors to Alleviate the Side Effects of Prostate Cancer Therapy. Fort Belvoir, VA: Defense Technical Information Center, October 2014. http://dx.doi.org/10.21236/ada617329.

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Chen, Shin. The DNA Sequence Required for the Maximal Transactivation of the VP5 Gene of Herpes Simplex Virus Type 1. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.6600.

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Penn, Linda Z. Exploiting the Novel Repressed Transactivator Assay to Identify Protein Peptide Inhibitors of the Myc Oncoprotein. Fort Belvoir, VA: Defense Technical Information Center, April 2005. http://dx.doi.org/10.21236/ada436402.

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Martin, Brian K., and Jenny Ting. The Effect of MHC Class II Transactivator on the Growth and Metastasis of Breast Tumors. Fort Belvoir, VA: Defense Technical Information Center, June 1999. http://dx.doi.org/10.21236/ada374042.

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Martin, Brian. The Effect of MHC Class II Transactivator (CIITA) on the Growth and Metastasis of Breast Tumors. Fort Belvoir, VA: Defense Technical Information Center, June 1998. http://dx.doi.org/10.21236/ada353890.

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