Pieter C. Dorrestein
University of Montana
565 Papers
1.3K Citations
Pieter C. Dorrestein is an academic researcher from University of Montana. The author has contributed to research in topics: Biology & Microbiome. The author has an hindex of 85, co-authored 470 publications. Previous affiliations of Pieter C. Dorrestein include University of California, Santa Cruz & Northern Arizona University.
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Papers
Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole synthase/sulfur carrier protein complex.
Ethan C. Settembre,Pieter C. Dorrestein,Huili Zhai,Abhishek Chatterjee,Fred W. McLafferty,Tadhg P. Begley,Steven E. Ealick +6 more
TL;DR: Comparison of the ThiS binding surface to the surface of ubiquitin identified a conserved hydrophobic patch of unknown function on Ubiquitin that may be involved in complex formation between ubiquit in and one of its binding partners.
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Impact of a Transposon Insertion in phzF2 on the Specialized Metabolite Production and Interkingdom Interactions of Pseudomonas aeruginosa
Vanessa V. Phelan,Wilna J. Moree,Julieta Aguilar,Dale S. Cornett,Alexandra Koumoutsi,Suzanne M. Noble,Kit Pogliano,Carlos A. Guerrero,Pieter C. Dorrestein,Pieter C. Dorrestein +9 more
TL;DR: In this study, a combination of IMS and liquid chromatography-tandem mass spectrometry was used to visualize the impact on specialized metabolite production of a transposon insertion into a Pseudomonas aeruginosa phenazine biosynthetic gene, phzF2.
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Chemoenzymatic Synthesis of Acyl Coenzyme A Substrates Enables in Situ Labeling of Small Molecules and Proteins
Vinayak Agarwal,Stefan Diethelm,Lauren Ray,Neha Garg,Takayoshi Awakawa,Pieter C. Dorrestein,Bradley S. Moore +6 more
TL;DR: A chemoenzymatic approach to generate fully functional acyl coenzyme A molecules that are then used as substrates to drive in situ acyl transfer reactions is described, with potential applications in wide-ranging chemical biology studies that utilize acylCoen enzyme A substrates.
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Legonaridin, a new member of linaridin RiPP from a Ghanaian Streptomyces isolate
Mostafa E. Rateb,Mostafa E. Rateb,Yin Zhai,Emmanuelle Ehrner,Christopher M. Rath,Xiaoling Wang,Jioji N. Tabudravu,Rainer Ebel,Mervin Bibb,Kwaku Kyeremeh,Pieter C. Dorrestein,Pieter C. Dorrestein,Kui Hong,Marcel Jaspars,Hai Deng +14 more
TL;DR: This is the first time that NMR spectroscopy is used to establish the 2-D structure of a linaridin RiPP, a rare linear ribosomally-synthesized and post-translationally modified peptides (RiPPs) comprising a new subfamily of Linaridins.
Iron acquisition in the marine actinomycete genus Salinispora is controlled by the desferrioxamine family of siderophores
Alexandra A. Roberts,Andrew W. Schultz,Roland D. Kersten,Pieter C. Dorrestein,Pieter C. Dorrestein,Bradley S. Moore,Bradley S. Moore +6 more
TL;DR: This study isolated and characterized desferrioxamines (DFOs) B and E from all three recognized Salinispora species and linked their biosyntheses in S. arenicola CNS-205 to the des locus through PCR-directed mutagenesis, indicating that DFOs are the primary siderophores in laboratory cultures of Salinipora.
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