K
Kathleen M. Downey
Researcher at University of Miami
Publications - 58
Citations - 4359
Kathleen M. Downey is an academic researcher from University of Miami. The author has contributed to research in topics: DNA polymerase & DNA polymerase delta. The author has an hindex of 36, co-authored 58 publications receiving 4314 citations. Previous affiliations of Kathleen M. Downey include Howard Hughes Medical Institute.
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Journal ArticleDOI
Functional identity of proliferating cell nuclear antigen and a DNA polymerase-δ auxiliary protein
Gregory Prelich,Cheng-Keat Tan,Matthew Kostura,Michael B. Mathews,Antero G. So,Kathleen M. Downey,Bruce Stillman +6 more
TL;DR: It is shown that PCNA and the polyrnerase-δ auxiliary protein have similar electrophoretic behaviour and are both recognized by anti-PCNA human autoantibodies, and both proteins are functionally equivalent; they stimulate SV40 DNA replication in vitro and increase the processivity of calf thymus DNA polymerase- δ.
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Nonnucleoside reverse transcriptase inhibitors that potently and specifically block human immunodeficiency virus type 1 replication
Donna Lee Romero,Mariano Busso,C.‐K. Tan,Fritz Reusser,J R Palmer,S M Poppe,Paul A. Aristoff,Kathleen M. Downey,Antero G. So,Lionel Resnick +9 more
TL;DR: Evaluation of a BHAP in HIV-1-infected SCID-hu mice (severe combined immunodeficient mice implanted with human fetal lymph node) showed that the compound could block HIV- 1 replication in vivo.
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A new mammalian DNA polymerase with 3' to 5' exonuclease activity: DNA polymerase δ
TL;DR: A new species of DNA polymerase has been purified more than 10 000-fold from the cytoplasm of erythroid hyperplastic bone marrow and results are consistent with the coexistence of two enzyme activities in a single protein.
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Further studies on calf thymus DNA polymerase delta purified to homogeneity by a new procedure.
TL;DR: DNA polymerase delta from calf thymus has been purified to apparent homogeneity by a new procedure which utilizes hydrophobic interaction chromatography with phenyl-Sepharose at an early step to separate most of the calcium-dependent protease activity from DNA polymeraseDelta and alpha.
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U-90152, a potent inhibitor of human immunodeficiency virus type 1 replication.
T J Dueweke,S M Poppe,Donna Lee Romero,S. M. Swaney,Antero G. So,Kathleen M. Downey,Irene W. Althaus,Fritz Reusser,Mariano Busso,Lionel Resnick +9 more
TL;DR: Although the RT amino acid substitutions K103N (lysine 103 to asparagine) and Y181C (tyrosine 181 to cysteine), which confer cross-resistance to several nonnucleoside inhibitors, also decrease the potency of U-90152, this drug retains significant activity against these mutant RTs in vitro.