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Bernard T. Golding

Researcher at Newcastle University

Publications -  429
Citations -  11038

Bernard T. Golding is an academic researcher from Newcastle University. The author has contributed to research in topics: Radical & Cyclin-dependent kinase. The author has an hindex of 54, co-authored 425 publications receiving 10214 citations. Previous affiliations of Bernard T. Golding include National University of Colombia & University of North Carolina at Chapel Hill.

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Identification of a highly potent and selective DNA-dependent protein kinase (DNA-PK) inhibitor (NU7441) by screening of chromenone libraries.

TL;DR: A solution-phase multiple-parallel synthesis approach was employed for the preparation of 6, 7- and 8-aryl-substituted chromenone libraries, which were screened as inhibitors of the DNA repair enzyme DNA-dependent protein kinase (DNA-PK) and resulted in the identification of 8-dibenzothiophen-4-yl-2-morpholin-4,yl-chromen-4 one as a highly potent and selective DNA-PK inhibitor.
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Resistance-modifying agents. 9. Synthesis and biological properties of benzimidazole inhibitors of the DNA repair enzyme poly(ADP-ribose) polymerase

TL;DR: The preclinical development of 2-aryl-1H-benzimidazole-4-carboxamides as resistance-modifying agents in cancer chemotherapy is described, and important hydrogen-bonding and hydrophobic interactions with the protein have been identified for this inhibitor.
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Metagenomic analysis and metabolite profiling of deep-sea sediments from the Gulf of Mexico following the Deepwater Horizon oil spill

TL;DR: The hypothesis that increased hydrocarbon exposure results in an altered sediment microbial community structure that reflects the prospects for oil biodegradation under the prevailing conditions is examined and increased exposure to hydrocarbons enriches Deltaproteobacteria, which are known to be capable of anaerobic hydrocarbon metabolism.
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Radical enzymes in anaerobes.

TL;DR: Two radical enzymes are discussed, pyruvate:ferredoxin oxidoreductase and methane-forming methyl-CoM reductase, which catalyze their main reaction in two-electron steps, but subsequent electron transfers proceed via radicals.