Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Kathryn J. Howard"'
Publikováno v:
Biochemistry. 48:7646-7655
Crystal structures and simulations suggest that conformational changes are critical for the function of HIV-1 reverse transcriptase. The enzyme is an asymmetric heterodimer of two subunits, p66 and p51. The two subunits have the same N-terminal seque
Autor:
Stuart F. J. Le Grice, Judith G. Levin, Jennifer T. Miller, Michael D. Powell, Kathryn J. Howard, Amnon Hizi, Klara Post, Jianhui Guo
Publikováno v:
Journal of Virology. 77:7623-7634
Human immunodeficiency virus type 2 (HIV-2) infection is a serious problem in West Africa and Asia. However, there have been relatively few studies of HIV-2 reverse transcriptase (RT), a potential target for antiviral therapy. Detailed knowledge of H
Autor:
Judith G. Levin, Stuart F. J. Le Grice, William A. Beard, Kathryn J. Howard, Samuel H. Wilson, Thomas A. Darden, Michael D. Powell, Thomas A. Kunkel, Katarzyna Bebenek
Publikováno v:
Journal of Biological Chemistry. 274:19885-19893
During retrovirus replication, reverse transcriptase (RT) must specifically interact with the polypurine tract (PPT) to generate and subsequently remove the RNA primer for plus-strand DNA synthesis. We have investigated the role that human immunodefi
Autor:
Bernard Ehresmann, Xuguang Li, Stuart F. J. Le Grice, Jason W. Rausch, Kathryn J. Howard, Roger S. Goody, Mark A. Wainberg, Scott R. Stetor, Eric J. Arts, Thomas W. North, Birgitta M. Wöhrl
Publikováno v:
Proceedings of the National Academy of Sciences. 93:10063-10068
Initiation of minus (-) strand DNA synthesis was examined on templates containing R, U5, and primer-binding site regions of the human immunodeficiency virus type 1 (HIV-1), feline immunodeficiency virus (FIV), and equine infectious anemia virus (EIAV
Autor:
Kathryn J. Howard, Stephen J. Benkovic, Madhumita Ghosh, Stuart F. J. Le Grice, Stephen H. Hughes, Craig E. Cameron
Publikováno v:
Journal of Biological Chemistry. 270:7068-7076
The properties of recombinant p66/p51 human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) containing C-terminal truncations in its p66 polypeptide were evaluated. Deletion end points partly or completely removed alpha-helix E' of the
Publikováno v:
Journal of Biological Chemistry. 269:8541-8548
A comparative study of recombinant 51- and 66-kDa subunits comprising equine infectious anemia virus reverse transcriptase (EIAV RT) is reported. Both polypeptides sedimented as stable homodimers (molecular mass, 102 and 132 kDa, respectively) when a
Publikováno v:
Journal of Biological Chemistry. 269:1388-1393
A contribution of the 51-kDa subunit of human immunodeficiency virus type-1 reverse transcriptase to activities of the parental heterodimer (p66/p51) was assessed in "selectively deleted" heterodimers whose p51 component contained C-terminal truncati
Interaction of tRNA(Lys-3) with multiple forms of human immunodeficiency virus reverse transcriptase
Publikováno v:
Journal of Biological Chemistry. 267:15952-15957
The interaction of several forms (p51, p66, and p66/p51) of recombinant human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) with a synthetic derivative of its cognate replication primer, tRNA(Lys-3), has been determined by gel-mobili
Autor:
Valerie A. Braz, Kathryn J. Howard
Native gel electrophoresis is used as a tool to assess structural differences in proteins. This article presents an application to separate oligomeric forms of proteins such as human immunodeficiency virus type 1 (HIV-1) reverse transcriptase monomer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3affae0fc8f2915c2ea347402c446646
https://europepmc.org/articles/PMC2898288/
https://europepmc.org/articles/PMC2898288/
Publikováno v:
Journal of Biological Chemistry. 265:11928-11935
In animal cells, unliganded steroid receptors are complexed with a 90-kDa heat shock protein, HSP90; hormone binding by the receptor leads to the release of HSP90. We found that the 795-amino acid rat glucocorticoid receptor protein formed oligomeric