Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI029306-05
Application #
3144039
Study Section
Special Emphasis Panel (ARR (V1))
Project Start
1989-11-01
Project End
1993-12-31
Budget Start
1993-11-01
Budget End
1993-12-31
Support Year
5
Fiscal Year
1994
Total Cost
Indirect Cost
Name
Wistar Institute
Department
Type
DUNS #
042250712
City
Philadelphia
State
PA
Country
United States
Zip Code
19104
Tomkowicz, Brian; Singh, Satya P; Lai, Derhsing et al. (2005) Mutational analysis reveals an essential role for the LXXLL motif in the transformation function of the human herpesvirus-8 oncoprotein, kaposin. DNA Cell Biol 24:10-20
Tungaturthi, Parithosh K; Sawaya, Bassel E; Ayyavoo, Velpandi et al. (2004) HIV-1 Vpr: genetic diversity and functional features from the perspective of structure. DNA Cell Biol 23:207-22
Tungaturthi, Parithosh K; Sawaya, Bassel E; Singh, Satya P et al. (2003) Role of HIV-1 Vpr in AIDS pathogenesis: relevance and implications of intravirion, intracellular and free Vpr. Biomed Pharmacother 57:20-4
Cartas, M; Singh, S P; Serio, D et al. (2001) Intravirion display of a peptide corresponding to the dimer structure of protease attenuates HIV-1 replication. DNA Cell Biol 20:797-805
Singh, S P; Tungaturthi, P; Cartas, M et al. (2001) Virion-associated HIV-1 Vpr: variable amount in virus particles derived from cells upon virus infection or proviral DNA transfection. Virology 283:78-83
Singh, S P; Tomkowicz, B; Lai, D et al. (2000) Functional role of residues corresponding to helical domain II (amino acids 35 to 46) of human immunodeficiency virus type 1 Vpr. J Virol 74:10650-7
Lai, D; Singh, S P; Cartas, M et al. (2000) Extent of incorporation of HIV-1 Vpr into the virus particles is flexible and can be modulated by expression level in cells. FEBS Lett 469:191-5
Serio, D; Singh, S P; Cartas, M A et al. (2000) Antiviral agent based on the non-structural protein targeting the maturation process of HIV-1: expression and susceptibility of chimeric Vpr as a substrate for cleavage by HIV-1 protease. Protein Eng 13:431-6
Singh, S P; Lai, D; Cartas, M et al. (2000) Epitope-tagging approach to determine the stoichiometry of the structural and nonstructural proteins in the virus particles: amount of Vpr in relation to Gag in HIV-1. Virology 268:364-71
Serio, D; Weber, I T; Harrison, R W et al. (1999) Epitope-based assay to determine the efficiency of cleavage by HIV-1 protease. Biotechniques 26:242-4, 246

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