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McIntosh, John A., Donia, Mohamed S., Nair, Satish K., Schmidt, Eric W. (2011) Enzymatic Basis of Ribosomal Peptide Prenylation in Cyanobacteria. Journal Of The American Chemical Society, 133 (34) 13698-13705 doi:10.1021/ja205458h

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Reference TypeJournal (article/letter/editorial)
TitleEnzymatic Basis of Ribosomal Peptide Prenylation in Cyanobacteria
JournalJournal Of The American Chemical Society
AuthorsMcIntosh, John A.Author
Donia, Mohamed S.Author
Nair, Satish K.Author
Schmidt, Eric W.Author
Year2011 (August 31)Volume133
Issue34
PublisherAmerican Chemical Society (ACS)
DOIdoi:10.1021/ja205458hSearch in ResearchGate
Generate Citation Formats
Mindat Ref. ID1738344Long-form Identifiermindat:1:5:1738344:6
GUID0
Full ReferenceMcIntosh, John A., Donia, Mohamed S., Nair, Satish K., Schmidt, Eric W. (2011) Enzymatic Basis of Ribosomal Peptide Prenylation in Cyanobacteria. Journal Of The American Chemical Society, 133 (34) 13698-13705 doi:10.1021/ja205458h
Plain TextMcIntosh, John A., Donia, Mohamed S., Nair, Satish K., Schmidt, Eric W. (2011) Enzymatic Basis of Ribosomal Peptide Prenylation in Cyanobacteria. Journal Of The American Chemical Society, 133 (34) 13698-13705 doi:10.1021/ja205458h
In(2011, August) Journal Of The American Chemical Society Vol. 133 (34) American Chemical Society (ACS)

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McIntosh, John A., Robertson, Charles R., Agarwal, Vinayak, Nair, Satish K., Bulaj, Grzegorz W., Schmidt, Eric W. (2010) Circular Logic: Nonribosomal Peptide-like Macrocyclization with a Ribosomal Peptide Catalyst. Journal Of The American Chemical Society, 132 (44) 15499-15501 doi:10.1021/ja1067806
McIntosh, John A., Donia, Mohamed S., Schmidt, Eric W. (2009) Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds. Natural Product Reports, 26 (4). 537pp. doi:10.1039/b714132g
McIntosh, John A., Donia, Mohamed S., Schmidt, Eric W. (2010) Insights into Heterocyclization from Two Highly Similar Enzymes. Journal Of The American Chemical Society, 132 (12) 4089-4091 doi:10.1021/ja9107116
Tianero, Ma. Diarey B., Donia, Mohamed S., Young, Travis S., Schultz, Peter G., Schmidt, Eric W. (2012) Ribosomal Route to Small-Molecule Diversity. Journal Of The American Chemical Society, 134 (1) 418-425 doi:10.1021/ja208278k
Schmidt, Eric W., Donia, Mohamed S., McIntosh, John A., Fricke, W. Florian, Ravel, Jacques (2012) Origin and Variation of Tunicate Secondary Metabolites. Journal of Natural Products, 75. 295-304 doi:10.1021/np200665k
Hao, Yue, Pierce, Elizabeth, Roe, Daniel, Morita, Maho, McIntosh, John A., Agarwal, Vinayak, Cheatham, Thomas E., Schmidt, Eric W., Nair, Satish K. (2016) Molecular basis for the broad substrate selectivity of a peptide prenyltransferase. Proceedings of the National Academy of Sciences, 113 (49) 14037-14042 doi:10.1073/pnas.1609869113
Sardar, Debosmita, Hao, Yue, Lin, Zhenjian, Morita, Maho, Nair, Satish K., Schmidt, Eric W. (2017) Enzymatic N- and C-Protection in Cyanobactin RiPP Natural Products. Journal Of The American Chemical Society, 139 (8) 2884-2887 doi:10.1021/jacs.6b12872
Estrada, Paola, Morita, Maho, Hao, Yue, Schmidt, Eric W., Nair, Satish K. (2018) A Single Amino Acid Switch Alters the Isoprene Donor Specificity in Ribosomally Synthesized and Post-Translationally Modified Peptide Prenyltransferases. Journal Of The American Chemical Society, 140 (26) 8124-8127 doi:10.1021/jacs.8b05187
Lee, Jaeheon, McIntosh, John, Hathaway, Brian J., Schmidt, Eric W. (2009) Using Marine Natural Products to Discover a Protease that Catalyzes Peptide Macrocyclization of Diverse Substrates. Journal Of The American Chemical Society, 131 (6) 2122-2124 doi:10.1021/ja8092168
Morita, Maho, Hao, Yue, Jokela, Jouni K., Sardar, Debosmita, Lin, Zhenjian, Sivonen, Kaarina, Nair, Satish K., Schmidt, Eric W. (2018) Post-Translational Tyrosine Geranylation in Cyanobactin Biosynthesis. Journal Of The American Chemical Society, 140 (19) 6044-6048 doi:10.1021/jacs.8b03137
Mahanta, Nilkamal, Liu, Andi, Dong, Shihui, Nair, Satish K., Mitchell, Douglas A. (2018) Enzymatic reconstitution of ribosomal peptide backbone thioamidation. Proceedings of the National Academy of Sciences, 115 (12) 3030-3035 doi:10.1073/pnas.1722324115
 
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