D
David Harrich
Researcher at QIMR Berghofer Medical Research Institute
Publications - 86
Citations - 4554
David Harrich is an academic researcher from QIMR Berghofer Medical Research Institute. The author has contributed to research in topics: Reverse transcriptase & Viral replication. The author has an hindex of 33, co-authored 85 publications receiving 4152 citations. Previous affiliations of David Harrich include Griffith University & Royal Children's Hospital.
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Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs.
TL;DR: Results indicate that TDP-43 is capable of modulating both in vitro and in vivo HIV-1 gene expression by either altering or blocking the assembly of transcription complexes that are capable of responding to Tat.
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Ivermectin is a specific inhibitor of importin α/β-mediated nuclear import able to inhibit replication of HIV-1 and dengue virus.
TL;DR: It is established for the first time that ivermectin has potent antiviral activity towards both HIV-1 and dengue virus, both of which are strongly reliant on importin α/β nuclear import, with respect to the HIV- 1 integrase and NS5 (non-structural protein 5) polymerase proteins respectively.
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Human immunodeficiency virus type 1 LTR TATA and TAR region sequences required for transcriptional regulation.
TL;DR: It is suggested that multiple determinants, including protein binding, the loop sequence, and RNA or DNA secondary structure, are important in tat‐activation and suggests that tat may interact with cellular proteins binding to DNA to increase HIV gene expression.
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Functional domains required for tat-induced transcriptional activation of the HIV-1 long terminal repeat.
TL;DR: It is suggested that several domains of tat protein are involved in transcriptional activation with the cysteine‐rich domain being required for complete activity of the tatprotein.
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Purification of the human immunodeficiency virus type 1 enhancer and TAR binding proteins EBP-1 and UBP-1.
TL;DR: The binding of highly purified cellular proteins to important transcriptional regulatory regions in the HIV LTR is demonstrated by both UV cross‐linking and DNase I footprinting.