Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI025308-08
Application #
2062949
Study Section
AIDS and Related Research Study Section 3 (ARRC)
Project Start
1987-09-30
Project End
1996-11-30
Budget Start
1994-12-01
Budget End
1996-11-30
Support Year
8
Fiscal Year
1995
Total Cost
Indirect Cost
Name
Baylor College of Medicine
Department
Microbiology/Immun/Virology
Type
Schools of Medicine
DUNS #
074615394
City
Houston
State
TX
Country
United States
Zip Code
77030
Yang, X; Herrmann, C H; Rice, A P (1996) The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for function. J Virol 70:4576-84
Herrmann, C H; Gold, M O; Rice, A P (1996) Viral transactivators specifically target distinct cellular protein kinases that phosphorylate the RNA polymerase II C-terminal domain. Nucleic Acids Res 24:501-8
Herrmann, C H; Rice, A P (1995) 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. J Virol 69:1612-20
Rhim, H; Rice, A P (1995) HIV-1 Tat protein is able to efficiently transactivate the HIV-2 LTR through a TAR RNA element lacking both dinucleotide bulge binding sites. Virology 206:673-8
Echetebu, C O; Rhim, H; Herrmann, C H et al. (1994) Construction and characterization of a potent HIV-2 Tat transdominant mutant protein. J Acquir Immune Defic Syndr 7:655-64
Rhim, H; Rice, A P (1994) Functional significance of the dinucleotide bulge in stem-loop1 and stem-loop2 of HIV-2 TAR RNA. Virology 202:202-11
Rhim, H; Rice, A P (1994) Exon2 of HIV-2 Tat contributes to transactivation of the HIV-2 LTR by increasing binding affinity to HIV-2 TAR RNA. Nucleic Acids Res 22:4405-13
Rhim, H; Echetebu, C O; Herrmann, C H et al. (1994) Wild-type and mutant HIV-1 and HIV-2 Tat proteins expressed in Escherichia coli as fusions with glutathione S-transferase. J Acquir Immune Defic Syndr 7:1116-21
Herrmann, C H; Rice, A P (1993) Specific interaction of the human immunodeficiency virus Tat proteins with a cellular protein kinase. Virology 197:601-8
Rice, A P; Wilson, E; Chan, F (1993) Limited proteolytic digestions identify common structural features of HIV-1 Tat proteins expressed during infection from alternatively spliced mRNAs. J Acquir Immune Defic Syndr 6:344-52

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