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Published in 2022 at "Chemmedchem"
DOI: 10.1002/cmdc.202200334
Abstract: Human cytomegalovirus (HCMV) replication requires a metal‐dependent endonuclease at the C‐terminus of pUL89 (pUL89‐C) for viral genome packaging and cleavage. We have previously shown that pUL89‐C can be pharmacologically inhibited with designed metal‐chelating compounds. We…
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Keywords:
pul89;
human cytomegalovirus;
hydroxy naphthyridine;
endonuclease ... See more keywords
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Published in 2018 at "Antiviral Research"
DOI: 10.1016/j.antiviral.2018.01.015
Abstract: ABSTRACT Human cytomegalovirus terminase complex cleaves the concatemeric genomic viral DNA into unit lengths during genome packaging and particle assembly. Terminase complex ATPase and endonuclease activity is provided by the viral protein pUL89. pUL89 is…
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Keywords:
endonuclease activity;
replication;
pul89;
hydroxypyrimidine diones ... See more keywords
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Published in 2022 at "Journal of medicinal chemistry"
DOI: 10.1021/acs.jmedchem.2c00203
Abstract: Human cytomegalovirus (HCMV) terminase complex entails a metal-dependent endonuclease at the C-terminus of pUL89 (pUL89-C). We report herein the design, synthesis, and characterization of dihydroxypyrimidine (DHP) acid (14), methyl ester (13), and amide (15) subtypes…
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Keywords:
pul89;
endonuclease;
dihydroxypyrimidine;
human cytomegalovirus ... See more keywords
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Published in 2023 at "Molecules"
DOI: 10.3390/molecules28093938
Abstract: Replication of Human Cytomegalovirus (HCMV) requires the presence of a metal-dependent endonuclease at the C-terminus of pUL89, in order to properly pack and cleave the viral genome. Therefore, pUL89 is an attractive target to design…
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Keywords:
pul89 endonuclease;
small molecule;
pul89;
endonuclease ... See more keywords