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Joseph Groom

Researcher at University of Washington

Publications -  13
Citations -  277

Joseph Groom is an academic researcher from University of Washington. The author has contributed to research in topics: Clostridium thermocellum & Caldicellulosiruptor bescii. The author has an hindex of 7, co-authored 13 publications receiving 202 citations. Previous affiliations of Joseph Groom include University of Georgia & Oak Ridge National Laboratory.

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Base-resolution detection of N4-methylcytosine in genomic DNA using 4mC-Tet-assisted-bisulfite- sequencing

TL;DR: A next-generation sequencing method that rapidly and cost efficiently reveals the genome-wide locations of 4mC for bacterial species with an available assembled reference genome to study the methylation of a member of the hyperthermophilc genus, Caldicellulosiruptor.
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Homologous Expression of the Caldicellulosiruptor bescii CelA Reveals that the Extracellular Protein Is Glycosylated

TL;DR: A new expression vector was constructed for C. bescii and was able, for the first time, to express significant quantities of full-length protein in vivo in the native host, allowing the study of the mechanism of protein glycosylation in this thermophile.
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Rare earth element alcohol dehydrogenases widely occur among globally distributed, numerically abundant and environmentally important microbes.

TL;DR: An inventory of genes potentially encoding Ln3+-dependent enzymes, closely related to the previously characterized XoxF and ExaF/PedH enzymes are compiled, demonstrating a range of catalytic properties and substrate and cofactor specificities.
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A Mutagenic Screen Identifies a TonB-Dependent Receptor Required for the Lanthanide Metal Switch in the Type I Methanotroph "Methylotuvimicrobium buryatense" 5GB1C.

TL;DR: The TonB-dependent receptor LanA is the first lanthanum receptor identified in a methanotroph and advances the knowledge of microbe-metal interactions in environmental niches that impact atmospheric methane levels, and are thus relevant to climate change.
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Heterologous complementation of a pyrF deletion in Caldicellulosiruptor hydrothermalis generates a new host for the analysis of biomass deconstruction

TL;DR: The use of C. hydrothermalis as a host for homologous and heterologous expression of enzymes important for biomass deconstruction will enable the identification of enzymes that contribute to the special ability of these bacteria to degrade complex lignocellulosic substrates as well as facilitate the construction of strains to improve and extend their substrate utilization capabilities.