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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 Laboratory
Carl R. Woese Institute for Genomic Biology
Research output
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Article
›
peer-review
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Keyphrases
Cyanobacteria
100%
Claisen Rearrangement
100%
Ribosomal Peptide
100%
Prenylation
100%
Prenylated
100%
Leader Sequence
66%
Natural Products
66%
Tyrosine
66%
Cyclic Peptide
66%
Post-translational Modification
33%
Physiological Temperature
33%
Protein Family
33%
Recognition Elements
33%
Aqueous Buffer
33%
Threonine
33%
Enzyme Family
33%
Common Model
33%
Prenyltransferase
33%
Peptide Natural Products
33%
Cyanobactins
33%
O-prenylation
33%
Macrocyclic Peptides
33%
Prenylated Phenolic Compounds
33%
Tyrosine Derivatives
33%
Peptide Biosynthesis
33%
Biochemistry, Genetics and Molecular Biology
Cyanobacteria
100%
Prenylation
100%
Peptide
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%
Pharmacology, Toxicology and Pharmaceutical Science
Cyanobacteria
100%
Peptide
100%
Natural Product
75%
Tyrosine
50%
Enzymes
50%
Cyclopeptide
50%
Signal Peptide
50%
Buffer
25%
Serine
25%
Threonine
25%
Dimethylallyltransferase
25%
Tyrosine Derivative
25%