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Enzymatic basis of ribosomal peptide prenylation in cyanobacteria
John A. McIntosh
, Mohamed S. Donia
,
Satish K. Nair
, Eric W. Schmidt
Biochemistry
Chemistry
School of Molecular and Cellular Biology
Materials Research Lab
Carl R. Woese Institute for Genomic Biology
Research output
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Article
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peer-review
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Keyphrases
Cyanobacteria
100%
Ribosomal Peptide
100%
Prenylation
100%
Claisen Rearrangement
50%
Leader Sequence
33%
Natural Products
33%
Tyrosine
33%
Cyclic Peptide
33%
Post-translational Modification
16%
Physiological Temperature
16%
Protein Family
16%
Recognition Elements
16%
Aqueous Buffer
16%
Threonine
16%
Enzyme Family
16%
Common Model
16%
Prenyltransferase
16%
Peptide Natural Products
16%
Cyanobactins
16%
O-prenylation
16%
Macrocyclic Peptides
16%
Prenylated Phenolic Compounds
16%
Tyrosine Derivatives
16%
Peptide Biosynthesis
16%
Biochemistry, Genetics and Molecular Biology
Cyanobacteria
100%
Prenylation
100%
Tyrosine
75%
Claisen Rearrangement
75%
Enzyme
50%
Signal Peptide
50%
Cyclic Peptide
50%
Anabolism
25%
Posttranslational Modification
25%
Protein Family
25%
Drive
25%
Dimethylallyltranstransferase
25%
Protein Synthesis
25%
Prenyltransferase
25%
Serine
25%
Threonine
25%